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.
Galectin-8 has recently been shown to have a role in cellular defence, against both bacterial cytosolic infection and vacuolar damage. Many intracellular bacteria, such as S. enterica serovar Typhimurium and S. flexneri prefer to replicate inside and outside of the vacuole safety respectively, yet these vacoles may become damaged, exposing bacteria to the host cell cytoplasm. It has been shown that the binding of galectin-8 to the damaged vacuole can recruit autophagy adaptors such as NDP52 leading to the formation of an autophagosome and subsequent bacterial destruction. As knockout experiments of galectin-8 leads to more successful cytosolic replication by S. enterica serovar Typhimurium, it is thought that galectin-8 acts as a danger receptor in defence against intracellular pathogens.
^ abcHadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y (July 2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis". J. Cell. Sci. 113 (Pt 13): 2385–97. PMID10852818.
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. PMID10697573.
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 (13): 2385–97. PMID10852818.
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. PMID10980616.
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. doi:10.1016/S0378-1119(01)00598-4. PMID11675018.
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. doi:10.1016/S0302-2838(02)00280-4. PMID12234517.
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. PMID12569102.
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. PMID12851289.
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. PMID12881409.
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. PMID15753078.