LGALS8

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Lectin, galactoside-binding, soluble, 8 (galectin 8)
Identifiers
Symbol(s) LGALS8; Gal-8; PCTA-1; PCTA1; Po66-CBP
External IDs OMIM: 606099 MGI: 1928481 HomoloGene: 31386
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3964 56048
Ensembl ENSG00000116977 ENSMUSG00000057554
Uniprot O00214 Q8C6H0
Refseq NM_006499 (mRNA)
NP_006490 (protein)		 XM_983825 (mRNA)
XP_988919 (protein)
Location Chr 1: 234.75 - 234.78 Mb Chr 13: 12.49 - 12.52 Mb
Pubmed search [1] [2]

Lectin, galactoside-binding, soluble, 8 (galectin 8), also known as LGALS8, is a human gene.[1]

This gene encodes a member of the galectin family. Galectins are beta-galactoside-binding animal lectins with conserved carbohydrate recognition domains. The galectins have been implicated in many essential functions including development, differentiation, cell-cell adhesion, cell-matrix interaction, growth regulation, apoptosis, and RNA splicing. This gene is widely expressed in tumoral tissues and seems to be involved in integrin-like cell interactions. Alternatively spliced transcript variants encoding different isoforms have been identified.[1]

[edit] References

  1. ^ a b Entrez Gene: LGALS8 lectin, galactoside-binding, soluble, 8 (galectin 8).

[edit] Further reading

  • Bidon N, Brichory F, Bourguet P, et al. (2001). "Galectin-8: a complex sub-family of galectins (Review).". Int. J. Mol. Med. 8 (3): 245–50. PMID 11494049. 
  • Danguy A, Camby I, Kiss R (2002). "Galectins and cancer.". Biochim. Biophys. Acta 1572 (2-3): 285–93. PMID 12223276. 
  • Bidon-Wagner N, Le Pennec JP (2004). "Human galectin-8 isoforms and cancer.". Glycoconj. J. 19 (7-9): 557–63. doi:10.1023/B:GLYC.0000014086.38343.98. PMID 14758080. 
  • Hadari YR, Paz K, Dekel R, et al. (1995). "Galectin-8. A new rat lectin, related to galectin-4.". J. Biol. Chem. 270 (7): 3447–53. PMID 7852431. 
  • Su ZZ, Lin J, Shen R, et al. (1996). "Surface-epitope masking and expression cloning identifies the human prostate carcinoma tumor antigen gene PCTA-1 a member of the galectin gene family.". Proc. Natl. Acad. Sci. U.S.A. 93 (14): 7252–7. PMID 8692978. 
  • Bassen R, Brichory F, Caulet-Maugendre S, et al. (2000). "Expression of Po66-CBP, a type-8 galectin, in different healthy, tumoral and peritumoral tissues.". Anticancer Res. 19 (6B): 5429–33. PMID 10697573. 
  • Hadari YR, Arbel-Goren R, Levy Y, et al. (2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis.". J. Cell. Sci. 113 ( Pt 13): 2385–97. PMID 10852818. 
  • Gopalkrishnan RV, Roberts T, Tuli S, et al. (2000). "Molecular characterization of prostate carcinoma tumor antigen-1, PCTA-1, a human galectin-8 related gene.". Oncogene 19 (38): 4405–16. doi:10.1038/sj.onc.1203767. PMID 10980616. 
  • Bidon N, Brichory F, Hanash S, et al. (2001). "Two messenger RNAs and five isoforms for Po66-CBP, a galectin-8 homolog in a human lung carcinoma cell line.". Gene 274 (1-2): 253–62. PMID 11675018. 
  • Nagy N, Bronckart Y, Camby I, et al. (2002). "Galectin-8 expression decreases in cancer compared with normal and dysplastic human colon tissue and acts significantly on human colon cancer cell migration as a suppressor.". Gut 50 (3): 392–401. PMID 11839721. 
  • Maier C, Rösch K, Herkommer K, et al. (2003). "A candidate gene approach within the susceptibility region PCaP on 1q42.2-43 excludes deleterious mutations of the PCTA-1 gene to be responsible for hereditary prostate cancer.". Eur. Urol. 42 (3): 301–7. PMID 12234517. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Levy Y, Ronen D, Bershadsky AD, Zick Y (2003). "Sustained induction of ERK, protein kinase B, and p70 S6 kinase regulates cell spreading and formation of F-actin microspikes upon ligation of integrins by galectin-8, a mammalian lectin.". J. Biol. Chem. 278 (16): 14533–42. doi:10.1074/jbc.M207380200. PMID 12569102. 
  • Ideo H, Seko A, Ishizuka I, Yamashita K (2004). "The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity.". Glycobiology 13 (10): 713–23. doi:10.1093/glycob/cwg094. PMID 12851289. 
  • Nishi N, Shoji H, Seki M, et al. (2004). "Galectin-8 modulates neutrophil function via interaction with integrin alphaM.". Glycobiology 13 (11): 755–63. doi:10.1093/glycob/cwg102. PMID 12881409. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Arbel-Goren R, Levy Y, Ronen D, Zick Y (2005). "Cyclin-dependent kinase inhibitors and JNK act as molecular switches, regulating the choice between growth arrest and apoptosis induced by galectin-8.". J. Biol. Chem. 280 (19): 19105–14. doi:10.1074/jbc.M502060200. PMID 15753078. 
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