| Lectin, galactoside-binding, soluble, 8 | |||||||||||||
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 Rendering based on PDB 2YRO. |
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| Identifiers | |||||||||||||
| Symbols | LGALS8; Gal-8; PCTA-1; PCTA1; Po66-CBP | ||||||||||||
| External IDs | OMIM: 606099 MGI: 1928481 HomoloGene: 31386 ChEMBL: 5475 GeneCards: LGALS8 Gene | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 3964 | 56048 | |||||||||||
| Ensembl | ENSG00000116977 | ENSMUSG00000057554 | |||||||||||
| UniProt | O00214 | Q9JL15 | |||||||||||
| RefSeq (mRNA) | NM_006499.4 | NM_001199043.1 | |||||||||||
| RefSeq (protein) | NP_006490.3 | NP_001185972.1 | |||||||||||
| Location (UCSC) | Chr 1: 236.68 – 236.72 Mb |
Chr 13: 12.53 – 12.56 Mb |
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| PubMed search | [1] | [2] | |||||||||||
Galectin-8 is a protein of the galectin family that in humans is encoded by the LGALS8 gene.[1][2][3]
Contents |
Function [link]
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.[3]
Role in cellular defence [link]
Galectin-8 has recently been shown to have a role in cellular defence, against both bacterial cytosolic infection and vacuolar damage.[4] Many intracellular bacteria, such as S. enterica serovar Typhimurium and S. flexneri prefer to replicate in the safety of a vacuole, 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.[4] 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.[4][5]
Interactions [link]
Galectin-8 has been shown to interact with CD49d,[6] CD29[6] and CD49c.[6]
References [link]
- ^ Hadari YR, Paz K, Dekel R, Mestrovic T, Accili D, Zick Y (Mar 1995). "Galectin-8. A new rat lectin, related to galectin-4". J Biol Chem 270 (7): 3447–53. DOI:10.1074/jbc.270.7.3447. PMID 7852431.
- ^ Su ZZ, Lin J, Shen R, Fisher PE, Goldstein NI, Fisher PB (Aug 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. DOI:10.1073/pnas.93.14.7252. PMC 38969. PMID 8692978. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=38969.
- ^ a b "Entrez Gene: LGALS8 lectin, galactoside-binding, soluble, 8 (galectin 8)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3964.
- ^ a b c Thurston T et al. (February 2012). "Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion". Nature 482: 414–418. DOI:10.1038/nature10744. PMID 22246324.
- ^ Huang J & Brumell. (February 2012). "A sweet way of sensing danger". Nature 482: 316–317.
- ^ a b c Hadari 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. PMID 10852818.
Further reading [link]
- 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. DOI:10.1016/S0304-4165(02)00315-X. 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.
- 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 (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. DOI:10.1016/S0378-1119(01)00598-4. 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. DOI:10.1136/gut.50.3.392. PMC 1773143. PMID 11839721. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1773143.
- 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. 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. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- 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. PMC 528928. PMID 15489334. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- 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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