Disease relevance of Lgals9

• Galectin-9 inhibits glomerular hypertrophy in db/db diabetic mice via cell-cycle-dependent mechanisms [1].
• Gal-9 may give an impetus to develop new therapeutic tools targeted toward diabetic nephropathy [1].
• Galectin-9 (Gal-9) was identified previously and demonstrated to have apoptotic potential to thymocytes in mice and activated CD8(+) T cells in nephrotoxic serum nephritis model [1].
• We recently reported the relationship between galectin-9 expression in tumor tissue and distant metastasis in breast cancer [2].
• Galectin-9, a novel prognostic factor with antimetastatic potential in breast cancer [2].

High impact information on Lgals9

• Galectin-9 failed to induce apoptosis in hepatocytes [3].
• The high expression of galectin-9 in the thymus led us to investigate its role in the clonal deletion of thymocytes [3].
• Fusion proteins were generated, which retained lactose-binding activity like the endogenous galectin-9 [3].
• The galectin-9 NCRD can bind both N-acetyllactosamine (Galbeta1-4GlcNAc) and T-antigen (Galbeta1-3GalNAc) with the proper location of Arg-64 [4].
• Data base searches indicate that this gene encodes a novel prototype galectin that contains one putative carbohydrate recognition domain and exhibits most identity to galectin-9/ecalectin, a potent eosinophil chemoattractant [5].

Biological context of Lgals9

• Galectin-9, at 2.5 microM concentration, induced apoptosis in approximately 30% of the thymocytes, as assessed by terminal deoxytransferase-mediated dUTP nick end labeling method [3].
• Galectin-9 had an alternate splicing isoform, exclusively expressed in the small intestine with a 31-amino acid insertion between the N-terminal domain and link peptide [6].
• In this study, the effect of Gal-9 on G1-phase cell-cycle arrest, one of the hallmark pathologic changes in early diabetic nephropathy, was investigated [1].
• Cell-cycle distribution analyses revealed that Gal-9 maintained further progression of cell cycle from the G1 phase [1].
• Gal-9 reversed the high-glucose-mediated upregulation of p27(Kip1) and p21(Cip1) and inhibited cell-cycle-dependent hypertrophy, i.e., reduced [(3)H]proline incorporation [1].

Anatomical context of Lgals9

• Taken together, these findings indicate that galectin-9, a developmentally regulated lectin, plays a role in thymocyte-epithelial interactions relevant to the biology of the thymus [3].
• For further confirming the cell-cycle regulation by Gal-9, conditionally immortalized mouse podocyte cells were cultured under 5.5 and 25 mM d-glucose supplemented with Gal-9 [1].
• Indeed, the galectins have non-identical expression profiles, qualitative differences, e.g. seen for galectin-5-positive bone marrow and erythrocytes or for hitherto unknown expression in cells of the theca folliculi and galectin-9-positive skin epidermis and esophageal epithelium [7].
• Galectin-9, a member of the beta-galactoside-binding animal lectin family, is involved in various cellular biological events, including aggregation and apoptosis, adhesion of cancer cells, and dendritic cell maturation [2].
• Multivariate analysis revealed that galectin-9 status influenced distant metastasis independent of and much more than lymph node metastasis [2].

Other interactions of Lgals9

• Collectively, these data indicate that galectin-9 is a new member of the galectin gene family and has a unique intestinal isoform [6].
• Gal-9 reduced glomerular expression of TGF-beta1 and the number of p27(Kip1)- and p21(Cip1)-positive cells in glomeruli [1].

Analytical, diagnostic and therapeutic context of Lgals9

• In situ hybridization studies revealed an accentuated expression of galectin-9 in liver and thymus of embryonic mice [3].
• By immunofluorescence microscopy, some of the thymocytes undergoing apoptosis had plasmalemmal bound galectin-9 [3].
• Electron microscopy revealed approximately 60% of the thymocytes undergoing apoptosis in the presence of galectin-9 [3].
• A 36-kDa beta-galactoside mammalian lectin protein, designated as galectin-9, was isolated from mouse embryonic kidney by using a degenerate primer polymerase chain reaction and cloning strategy [6].
• Southern blot genomic DNA analyses, using the galectin-9 specific probe derived from the N-terminal carbohydrate-binding domain, indicated the presence of a novel gene encoding galectin-9 in both mice and rats [6].

References