Difference between revisions of "Galectin-3"
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Galectin-3... | Galectin-3... | ||
* is the only member of chimeric subfamily in mammals | * is the only member of chimeric subfamily in mammals | ||
| − | * is very well-studied | + | * is a very well-studied glycan-binding protein (GBP) |
* crystal structure is known | * crystal structure is known | ||
* has unique functions intra- and extra-cellularly, due to unusual N-terminal domain that can participate in protein-protein interactions | * has unique functions intra- and extra-cellularly, due to unusual N-terminal domain that can participate in protein-protein interactions | ||
| Line 9: | Line 9: | ||
* has unique functions in innate immune response to microbial pathogens | * has unique functions in innate immune response to microbial pathogens | ||
* has been administered in animal models of disease to assess therapeutic potential | * has been administered in animal models of disease to assess therapeutic potential | ||
| − | * binds distinct cell surface glycoprotein ligands in lymphocytes compared to | + | * binds distinct cell surface glycoprotein ligands in lymphocytes compared to Galectin-16 |
* expression is involved in growth modulation<ref>Baptiste, T.A., James, A., Saria, M. & Ochieng, J. Mechano-transduction mediated secretion and uptake of | * expression is involved in growth modulation<ref>Baptiste, T.A., James, A., Saria, M. & Ochieng, J. Mechano-transduction mediated secretion and uptake of | ||
| − | + | Galectin-3 in breast carcinoma cells: implications in the extracellular functions of the lectin. Exp Cell Res 313, 652-664 (2007). </ref> | |
* has anti-apoptotic activity in its intracellular expression<ref>Saegusa, J. et al. Galectin-3 protects keratinocytes from UVB-induced apoptosis by enhancing AKT activation and suppressing ERK activation. J Invest Dermatol 128, 2403-2411 (2008).</ref> | * has anti-apoptotic activity in its intracellular expression<ref>Saegusa, J. et al. Galectin-3 protects keratinocytes from UVB-induced apoptosis by enhancing AKT activation and suppressing ERK activation. J Invest Dermatol 128, 2403-2411 (2008).</ref> | ||
== CFG Participating Investigators contributing to the understanding of this paradigm == | == CFG Participating Investigators contributing to the understanding of this paradigm == | ||
| − | CFG Participating Investigators (PIs) contributing to the understanding of | + | CFG Participating Investigators (PIs) contributing to the understanding of Galectin-3 include: Linda Baum, Susan Bellis, Roger Chammas, Richard Cummings, James Dennis, Margaret, Huflejt, Fu-Tong Liu, Joshiah Ochieng, Noorjahan Panjawani, Mauro Perretti, Avram Raz, James Rini, Maria Roque-Barreira, Sachiko Sato, Tariq Sethi, Irma van Die, Gerardo Vasta, John Wang, Paul Winyard |
== Progress toward understanding this GBP paradigm == | == Progress toward understanding this GBP paradigm == | ||
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<br> | <br> | ||
== CFG resources used in investigations == | == 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-3&maxresults=20 CFG database search results for | + | 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-3&maxresults=20 CFG database search results for Galectin-3]. |
=== Glycan profiling === | === Glycan profiling === | ||
| Line 41: | Line 41: | ||
<br> | <br> | ||
=== Knockout mouse lines === | === Knockout mouse lines === | ||
| − | Galectin-3 knockout mice were [https://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotyped] by the CFG and continue to be used by investigators to study the biological functions of | + | Galectin-3 knockout mice were [https://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotyped] by the CFG and continue to be used by investigators to study the biological functions of Galectin-3. |
=== Glycan array === | === Glycan array === | ||
| − | Investigators have used CFG carbohydrate compounds and glycan array to study ligand binding specificity of | + | Investigators have used CFG carbohydrate compounds and glycan array to study ligand binding specificity of Galectin-3. |
== Related GBPs == | == Related GBPs == | ||
Revision as of 21:18, 6 April 2010
Galectin-3...
- is the only member of chimeric subfamily in mammals
- is a very well-studied glycan-binding protein (GBP)
- crystal structure is known
- has unique functions intra- and extra-cellularly, due to unusual N-terminal domain that can participate in protein-protein interactions
- has a unique mode of multimerization
- is the only known anti-apoptotic galectin
- null mice have distinct phenotypes, including alterations in inflammatory and wound-healing responses, and cyst formation in disease[1]
- has unique functions in innate immune response to microbial pathogens
- has been administered in animal models of disease to assess therapeutic potential
- binds distinct cell surface glycoprotein ligands in lymphocytes compared to Galectin-16
- expression is involved in growth modulation[2]
- has anti-apoptotic activity in its intracellular expression[3]
CFG Participating Investigators contributing to the understanding of this paradigm
CFG Participating Investigators (PIs) contributing to the understanding of Galectin-3 include: Linda Baum, Susan Bellis, Roger Chammas, Richard Cummings, James Dennis, Margaret, Huflejt, Fu-Tong Liu, Joshiah Ochieng, Noorjahan Panjawani, Mauro Perretti, Avram Raz, James Rini, Maria Roque-Barreira, Sachiko Sato, Tariq Sethi, Irma van Die, Gerardo Vasta, John Wang, Paul Winyard
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 CFG database search results for Galectin-3.
Glycan profiling
Glycogene microarray
Knockout mouse lines
Galectin-3 knockout mice were phenotyped by the CFG and continue to be used by investigators to study the biological functions of Galectin-3.
Glycan array
Investigators have used CFG carbohydrate compounds and glycan array to study ligand binding specificity of Galectin-3.
Related GBPs
None in mammals, homologues in invertebrates.
References
- ↑ Chiu, M.G. et al. Galectin-3 associates with the primary cilium and modulates cyst growth in congenital polycystic kidney disease. Am J Pathol 169, 1925-1938 (2006).
- ↑ Baptiste, T.A., James, A., Saria, M. & Ochieng, J. Mechano-transduction mediated secretion and uptake of Galectin-3 in breast carcinoma cells: implications in the extracellular functions of the lectin. Exp Cell Res 313, 652-664 (2007).
- ↑ Saegusa, J. et al. Galectin-3 protects keratinocytes from UVB-induced apoptosis by enhancing AKT activation and suppressing ERK activation. J Invest Dermatol 128, 2403-2411 (2008).
Acknowledgements
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings
