CFGparadigms - User contributions [en]

Galectin-1

2010-06-12T00:34:31Z

GabrielRabinovich: /* Glycan profiling */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 The specificity of galectin-1 has been analyzed on the CFG glycan array, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 Glycogene microarray data and Glycan array data]

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:32:58Z

GabrielRabinovich: /* Glycan profiling */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 The specificity of galectin-1 has been analyzed on the CFG glycan array, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 Glycan profiling]

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:32:20Z

GabrielRabinovich: /* Glycan profiling */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 The specificity of galectin-1 has been analyzed on the CFG glycan array [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 Glycan profiling]

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:30:36Z

GabrielRabinovich: /* Glycan profiling */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 The specificity of galectin-1 has been analyzed on the CFG glycan array [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20]

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:29:23Z

GabrielRabinovich: Undo revision 589 by GabrielRabinovich (Talk)

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 The specificity of galectin-1 has been analyzed on the CFG glycan array

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:28:56Z

GabrielRabinovich: /* Glycan profiling */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 The specificity of galectin-1 has been analyzed on the CFG glycan array[http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20]

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:27:37Z

GabrielRabinovich: Undo revision 587 by GabrielRabinovich (Talk)

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 The specificity of galectin-1 has been analyzed on the CFG glycan array

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:23:46Z

GabrielRabinovich: /* Glycan profiling */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

 The specificity of galectin-1 has been analyzed on the CFG glycan array[http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20]

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:21:07Z

GabrielRabinovich: /* Glycan profiling */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 The specificity of galectin-1 has been analyzed on the CFG glycan array

=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:19:39Z

GabrielRabinovich: /* Structure */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 Galectin-1 can be found as a monomer as well as a non-covalent homodimer composed of
subunits of 14.5 kDa, each containing an identical CRD.

=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:09:43Z

GabrielRabinovich: /* Biological roles of GBP-ligand interaction */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 Galectin-1 is involved in immunoregulation, cytokine secretion, host-pathogen interactions, cell adhesion and migration and tumor-immune escape.

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:05:21Z

GabrielRabinovich: /* Cellular expression */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 Galectin-1 is expressed in many cell types including muscle, epithelial and endothelial cells. Within the immune system this GBP is considerably up-regulated in activated T lymphocytes, macrophages, uterine NK cells and regulatory T cells.

=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:03:17Z

GabrielRabinovich: /* Carbohydrate ligands */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Galβ1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-12T00:00:39Z

GabrielRabinovich: /* Carbohydrate ligands */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 The ligand of galectin-1 has been shown to by Gal<beta>1-4GlcNAc (or LacNAc).

=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-10T01:25:41Z

GabrielRabinovich:

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* contributes to tumor cell evasion of immune responses.<ref>Rubinstein N, Alvarez M, Zwirner NW, Toscano MA, Ilarregui JM, Bravo A, Mordoh J, Fainboim L, Podhajcer OL, Rabinovich GA. ''Cancer Cell'' 5, 241-251 (2004).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-10T01:22:20Z

GabrielRabinovich:

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease <ref>Rabinovich GA, Toscano MA. Turning "sweet" on immunity: galectin-glycan interactions in immune tolerance and inflammation. ''Nat Rev Immunol'' 9, 338-352 (2009). </ref>.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential <ref>Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. ''J Exp Med'' 190, 385-398 (1999)</ref>
* selectively regulates Th1, Th2 and Th17 cell survival<ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.
* promotes the differentiation of tolerogenic dendritic cells and plays a pivotal role in fetomaternal tolerance <ref>Ilarregui JM, Croci DO, Bianco GA, Toscano MA, Salatino M, Vermeulen ME, Geffner JR, Rabinovich GA.''Nat Immunol'' 10, 981-991 (2009).</ref><ref>Blois SM, ''et al''. A pivotal role for galectin-1 in fetomaternal tolerance. ''Nat Med'' 13,1450-1457 (2007).</ref>
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-10T00:59:09Z

GabrielRabinovich:

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte expansion and increased susceptibility to autoimmune disease.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential.
* selectively regulates T helper cell (Th1, Th2 and Th17) fate <ref>Toscano MA, Bianco GA, Ilarregui JM, Croci DO, Correale J, Hernandez JD, Zwirner NW, Poirier F, Riley EM, Baum LG, Rabinovich GA. Differential glycosylation of Th1, Th2 and Th17 effector cells selectively regulates susceptibility to cell death. ''Nat Immunol'' 8, 825-834 (2007).</ref>
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Galectin-1

2010-06-10T00:51:17Z

GabrielRabinovich: