Difference between revisions of "Galectin-9"
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| − | Galectin-9 is the best-studied of the tandem-repeat galectins and the crystal structure of the N-terminal carbohydrate recognition domain (CRD) is known. In addition, | + | Galectin-9 is the best-studied of the tandem-repeat galectins and the crystal structure of the N-terminal carbohydrate recognition domain (CRD) is known. In addition, Galectin-9... |
* uniquely binds poly-N-acetyllactosamine sequences by recognizing internal N-acetyllactosamine repeats<ref>Nagae, M. et al. Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain. Glycobiology 19, 112-117 (2009). </ref> | * uniquely binds poly-N-acetyllactosamine sequences by recognizing internal N-acetyllactosamine repeats<ref>Nagae, M. et al. Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain. Glycobiology 19, 112-117 (2009). </ref> | ||
| − | * binds distinct ligands from [[ | + | * binds distinct ligands from [[Galectin-1]]<ref>Bi, S., Earl, L.A., Jacobs, L. & Baum, L.G. Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways. J Biol Chem 283, 12248-12258 (2008).</ref> |
* has three well-characterized linker domains between the CRDs, generated by alternative splicing, that regulate cellular localization and function of the protein | * has three well-characterized linker domains between the CRDs, generated by alternative splicing, that regulate cellular localization and function of the protein | ||
* is the only tandem-repeat galectin that has been administered in animal models of disease to assess therapeutic potential<ref>Baba, M. et al. Galectin-9 inhibits glomerular hypertrophy in db/db diabetic mice via cell-cycle-dependent mechanisms. J Am Soc Nephrol 16, 3222-3234 (2005). </ref><ref name="Seki 2008">Seki, M. et al. Galectin-9 suppresses the generation of Th17, promotes the induction of regulatory T cells, and regulates experimental autoimmune arthritis. Clin Immunol 127, 78-88 (2008). | * is the only tandem-repeat galectin that has been administered in animal models of disease to assess therapeutic potential<ref>Baba, M. et al. Galectin-9 inhibits glomerular hypertrophy in db/db diabetic mice via cell-cycle-dependent mechanisms. J Am Soc Nephrol 16, 3222-3234 (2005). </ref><ref name="Seki 2008">Seki, M. et al. Galectin-9 suppresses the generation of Th17, promotes the induction of regulatory T cells, and regulates experimental autoimmune arthritis. Clin Immunol 127, 78-88 (2008). | ||
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== 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-9 include: Linda Baum, Richard Cummings, Gabriel Rabinovich, Sachiko Sato |
== 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-9&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-9&maxresults=20 CFG database search results for Galectin-9]. |
=== Glycan profiling === | === Glycan profiling === | ||
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<br> | <br> | ||
=== 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-9. |
== Related GBPs == | == Related GBPs == | ||
Revision as of 21:19, 6 April 2010
Galectin-9 is the best-studied of the tandem-repeat galectins and the crystal structure of the N-terminal carbohydrate recognition domain (CRD) is known. In addition, Galectin-9...
- uniquely binds poly-N-acetyllactosamine sequences by recognizing internal N-acetyllactosamine repeats[1]
- binds distinct ligands from Galectin-1[2]
- has three well-characterized linker domains between the CRDs, generated by alternative splicing, that regulate cellular localization and function of the protein
- is the only tandem-repeat galectin that has been administered in animal models of disease to assess therapeutic potential[3][4][5]
- null mice have increased susceptibility to autoimmune disease
- binds to a unique glycoprotein ligand Tim-3 expressed in Th1 and Th17 cells[4][6][7][8]
CFG Participating Investigators contributing to the understanding of this paradigm
CFG Participating Investigators (PIs) contributing to the understanding of Galectin-9 include: Linda Baum, Richard Cummings, Gabriel Rabinovich, Sachiko Sato
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-9.
Glycan profiling
Glycogene microarray
Knockout mouse lines
Glycan array
Investigators have used CFG carbohydrate compounds and glycan array to study ligand binding specificity of Galectin-9.
Related GBPs
Galectins-4, -6, -8, and -12
References
- ↑ Nagae, M. et al. Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain. Glycobiology 19, 112-117 (2009).
- ↑ Bi, S., Earl, L.A., Jacobs, L. & Baum, L.G. Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways. J Biol Chem 283, 12248-12258 (2008).
- ↑ Baba, M. et al. Galectin-9 inhibits glomerular hypertrophy in db/db diabetic mice via cell-cycle-dependent mechanisms. J Am Soc Nephrol 16, 3222-3234 (2005).
- ↑ 4.0 4.1 Seki, M. et al. Galectin-9 suppresses the generation of Th17, promotes the induction of regulatory T cells, and regulates experimental autoimmune arthritis. Clin Immunol 127, 78-88 (2008).
- ↑ Tsuchiyama, Y. et al. Efficacy of galectins in the amelioration of nephrotoxic serum nephritis in Wistar Kyoto rats. Kidney Int 58, 1941-1952 (2000).
- ↑ Naka, E.L., Ponciano, V.C., Cenedeze, M.A., Pacheco-Silva, A. & Camara, N.O. Detection of the Tim-3 ligand, galectin-9, inside the allograft during a rejection episode. Int Immunopharmacol 9, 658-662 (2009).
- ↑ Niwa, H. et al. Stable form of galectin-9, a Tim-3 ligand, inhibits contact hypersensitivity and psoriatic reactions: a potent therapeutic tool for Th1- and/or Th17-mediated skin inflammation. Clin Immunol 132, 184-194 (2009).
- ↑ Anderson, D.E. TIM-3 as a therapeutic target in human inflammatory diseases. Expert Opin Ther Targets 11, 1005-1009 (2007).
Acknowledgements
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings
