Galectin-9 is a protein that in humans is encoded by the LGALS9gene.[1][2]
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. The protein encoded by this gene is an S-type lectin. This galectin is strongly overexpressed in Hodgkin's disease tissue and it might participate in the interaction between the H&RS cells with their surrounding cells and might thus play a role in the pathogenesis of this disease and/or its consistently associated immunodeficiency. The protein has N- and C- terminal carbohydrate-binding domains connected by a link peptide. Multiple alternatively spliced transcript variants have been found for this gene.[2]
References
↑Tureci O, Schmitt H, Fadle N, Pfreundschuh M, Sahin U (Apr 1997). "Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease". J Biol Chem. 272 (10): 6416–22. doi:10.1074/jbc.272.10.6416. PMID9045665.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Matsumoto R, Matsumoto H, Seki M, et al. (1998). "Human ecalectin, a variant of human galectin-9, is a novel eosinophil chemoattractant produced by T lymphocytes". J. Biol. Chem. 273 (27): 16976–84. doi:10.1074/jbc.273.27.16976. PMID9642261.
Matsumoto R, Hirashima M, Kita H, Gleich GJ (2002). "Biological activities of ecalectin: a novel eosinophil-activating factor". J. Immunol. 168 (4): 1961–7. doi:10.4049/jimmunol.168.4.1961. PMID11823532.
Kageshita T, Kashio Y, Yamauchi A, et al. (2002). "Possible role of galectin-9 in cell aggregation and apoptosis of human melanoma cell lines and its clinical significance". Int. J. Cancer. 99 (6): 809–16. doi:10.1002/ijc.10436. PMID12115481.
Imaizumi T, Kumagai M, Sasaki N, et al. (2002). "Interferon-gamma stimulates the expression of galectin-9 in cultured human endothelial cells". J. Leukoc. Biol. 72 (3): 486–91. PMID12223516.
Asakura H, Kashio Y, Nakamura K, et al. (2003). "Selective eosinophil adhesion to fibroblast via IFN-gamma-induced galectin-9". J. Immunol. 169 (10): 5912–8. doi:10.4049/jimmunol.169.10.5912. PMID12421975.
Kashio Y, Nakamura K, Abedin MJ, et al. (2003). "Galectin-9 induces apoptosis through the calcium-calpain-caspase-1 pathway". J. Immunol. 170 (7): 3631–6. doi:10.4049/jimmunol.170.7.3631. PMID12646627.
Abedin MJ, Kashio Y, Seki M, et al. (2003). "Potential roles of galectins in myeloid differentiation into three different lineages". J. Leukoc. Biol. 73 (5): 650–6. doi:10.1189/jlb.0402163. PMID12714580.
Matsuda A, Suzuki Y, Honda G, et al. (2003). "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways". Oncogene. 22 (21): 3307–18. doi:10.1038/sj.onc.1206406. PMID12761501.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Irie A, Yamauchi A, Kontani K, et al. (2005). "Galectin-9 as a prognostic factor with antimetastatic potential in breast cancer". Clin. Cancer Res. 11 (8): 2962–8. doi:10.1158/1078-0432.CCR-04-0861. PMID15837748.
Kasamatsu A, Uzawa K, Nakashima D, et al. (2005). "Galectin-9 as a regulator of cellular adhesion in human oral squamous cell carcinoma cell lines". Int. J. Mol. Med. 16 (2): 269–73. doi:10.3892/ijmm.16.2.269. PMID16012760.
Dai SY, Nakagawa R, Itoh A, et al. (2005). "Galectin-9 induces maturation of human monocyte-derived dendritic cells". J. Immunol. 175 (5): 2974–81. doi:10.4049/jimmunol.175.5.2974. PMID16116184.
Zhu C, Anderson AC, Schubart A, et al. (2006). "The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity". Nat. Immunol. 6 (12): 1245–52. doi:10.1038/ni1271. PMID16286920.
van de Weyer PS, Muehlfeit M, Klose C, et al. (2007). "A highly conserved tyrosine of Tim-3 is phosphorylated upon stimulation by its ligand galectin-9". Biochem. Biophys. Res. Commun. 351 (2): 571–6. doi:10.1016/j.bbrc.2006.10.079. PMID17069754.