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Gene Review

LGALS2  -  lectin, galactoside-binding, soluble, 2

Homo sapiens

Synonyms: Beta-galactoside-binding lectin L-14-II, Gal-2, Galectin-2, HL14, Lactose-binding lectin 2, ...
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Disease relevance of LGALS2


High impact information on LGALS2

  • Genome-wide association studies have also been undertaken, and the pro-inflammatory cytokine lymphotoxin-alpha (LTA), and its key ligand galectin-2 (LGALS2) have been identified as genes implicated in predisposition for heart attack [4].
  • Galectin-2 is structurally closely related to galectin-1, but has a distinct expression profile primarily confined to the gastrointestinal tract [5].
  • Labeled galectin-2 binds to T cells in a beta-galactoside-specific manner [5].
  • The carbohydrate-dependent binding of galectin-2 induces apoptosis in activated T cells [5].
  • The genomic DNA encoding L-14-II (LGALS2) contains four exons with similar intron placement to L-14-I (LGALS1); but the genomic upstream region, which contains several sequences characteristic of regulatory elements, differs significantly from L-14-I [6].

Biological context of LGALS2


Anatomical context of LGALS2


Associations of LGALS2 with chemical compounds

  • Here we show that LTA protein binds to galectin-2, a member of the galactose-binding lectin family [1].
  • 3) Kinetic analysis of tirilazad hydroxylase activity in three human livers resulted in an apparent Km of 2.12, 1.68 and 1.66 microM, and Vmax = 0.85, 0.44 and 3.45 (nmol/mg protein/min) for HL14, HL17 and HL21, respectively [11].

Other interactions of LGALS2

  • This genetic substitution affects the transcriptional level of galectin-2 in vitro, potentially leading to altered secretion of LTA, which would then affect the degree of inflammation; however, its relevance to other populations remains to be clarified [1].

Analytical, diagnostic and therapeutic context of LGALS2


  1. Functional variation in LGALS2 confers risk of myocardial infarction and regulates lymphotoxin-alpha secretion in vitro. Ozaki, K., Inoue, K., Sato, H., Iida, A., Ohnishi, Y., Sekine, A., Sato, H., Odashiro, K., Nobuyoshi, M., Hori, M., Nakamura, Y., Tanaka, T. Nature (2004) [Pubmed]
  2. Effects of lymphotoxin-alpha gene and galectin-2 gene polymorphisms on inflammatory biomarkers, cellular adhesion molecules and risk of coronary heart disease. Asselbergs, F.W., Pai, J.K., Rexrode, K.M., Hunter, D.J., Rimm, E.B. Clin. Sci. (2007) [Pubmed]
  3. Lymphotoxin-alpha and cardiovascular disease: clinical association and pathogenic mechanisms. Naoum, J.J., Chai, H., Lin, P.H., Lumsden, A.B., Yao, Q., Chen, C. Med. Sci. Monit. (2006) [Pubmed]
  4. Genetic susceptibility to myocardial infarction and coronary artery disease. Topol, E.J., Smith, J., Plow, E.F., Wang, Q.K. Hum. Mol. Genet. (2006) [Pubmed]
  5. Human galectin-2: novel inducer of T cell apoptosis with distinct profile of caspase activation. Sturm, A., Lensch, M., André, S., Kaltner, H., Wiedenmann, B., Rosewicz, S., Dignass, A.U., Gabius, H.J. J. Immunol. (2004) [Pubmed]
  6. Isolation and expression of a gene encoding L-14-II, a new human soluble lactose-binding lectin. Gitt, M.A., Massa, S.M., Leffler, H., Barondes, S.H. J. Biol. Chem. (1992) [Pubmed]
  7. Two members of the S-lac lectin gene family, LGALS1 and LGALS2, reside in close proximity on human chromosome 22q12-q13. Mehrabian, M., Gitt, M.A., Sparkes, R.S., Leffler, H., Barondes, S.H., Lusis, A.J. Genomics (1993) [Pubmed]
  8. Fine-scale SNP map of an 11-kb genomic region at 22q13.1 containing the galectin-1 gene. Iida, A., Ozaki, K., Tanaka, T., Nakamura, Y. J. Hum. Genet. (2005) [Pubmed]
  9. Genotype of galectin 2 (LGALS2) is associated with insulin-glucose profile in the British Women's Heart and Health Study. Christensen, M.B., Lawlor, D.A., Gaunt, T.R., Howell, M.W., Davey Smith, G., Ebrahim, S., Day, I.N. Diabetologia (2006) [Pubmed]
  10. Isolation of a cDNA clone, encoding a human beta-galactoside binding protein, overexpressed during glucocorticoid-induced cell death. Goldstone, S.D., Lavin, M.F. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  11. Biotransformation of tirilazad in human: 1. Cytochrome P450 3A-mediated hydroxylation of tirilazad mesylate in human liver microsomes. Wienkers, L.C., Steenwyk, R.C., Sanders, P.E., Pearson, P.G. J. Pharmacol. Exp. Ther. (1996) [Pubmed]
  12. Human galectin-2: expression profiling by RT-PCR/immunohistochemistry and its introduction as a histochemical tool for ligand localization. Saal, I., Nagy, N., Lensch, M., Lohr, M., Manning, J.C., Decaestecker, C., André, S., Kiss, R., Salmon, I., Gabius, H.J. Histol. Histopathol. (2005) [Pubmed]
  13. Multiple soluble beta-galactoside-binding lectins from human lung. Sparrow, C.P., Leffler, H., Barondes, S.H. J. Biol. Chem. (1987) [Pubmed]
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