Difference between revisions of "Galectin-9"
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=== Knockout mouse lines === | === Knockout mouse lines === | ||
| + | CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/DataCoreFGJb4.shtml Galectin-9 knockout mice] have been used to study the biological functions of this paradigm GBP. [http://www.functionalglycomics.org/glycomics/publicdata/investigator.jsp?investigator=judyteale (CFG PI data)] | ||
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=== Glycan array === | === Glycan array === | ||
Investigators have used CFG carbohydrate compounds and glycan array screening to study ligand binding specificity of Galectin-9 (for example, click [http://www.functionalglycomics.org/glycomics/HServlet?operation=view&sideMenu=no&psId=primscreen_2735 here]). To see all glycan array results for Galectin-9, click [http://www.functionalglycomics.org/glycomics/search/jsp/result.jsp?query=galectin-9&cat=coreh here]. | Investigators have used CFG carbohydrate compounds and glycan array screening to study ligand binding specificity of Galectin-9 (for example, click [http://www.functionalglycomics.org/glycomics/HServlet?operation=view&sideMenu=no&psId=primscreen_2735 here]). To see all glycan array results for Galectin-9, click [http://www.functionalglycomics.org/glycomics/search/jsp/result.jsp?query=galectin-9&cat=coreh here]. | ||
Revision as of 21:11, 31 March 2011
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
This section documents what is currently known about Galectin-9, its carbohydrate ligand(s), and how they interact to mediate cell communication. Further information can be found in the GBP Molecule Page for human and mouse Galectin-9 in the CFG database.
Carbohydrate ligands
Cellular expression of GBP and ligands
Biosynthesis of ligands
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
Probes for human galectin-9 have been included in all versions of the CFG glycogene chip, and probes for mouse galectin-9 are included on versions 2, 3, and 4.
Knockout mouse lines
CFG-generated Galectin-9 knockout mice have been used to study the biological functions of this paradigm GBP. (CFG PI data)
Glycan array
Investigators have used CFG carbohydrate compounds and glycan array screening to study ligand binding specificity of Galectin-9 (for example, click here). To see all glycan array results for Galectin-9, click here.
Related GBPs
Galectin-4 (CFG data), galectin-6, galectin-8 (CFG data), and galectin-12 (CFG data).
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
