Galectin-8

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LGALS8
Protein LGALS8 PDB 2YRO.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases LGALS8, Gal-8, PCTA-1, PCTA1, Po66-CBP, galectin 8
External IDs MGI: 1928481 HomoloGene: 31386 GeneCards: LGALS8
RNA expression pattern
PBB GE LGALS8 208935 s at fs.png

PBB GE LGALS8 208934 s at fs.png

PBB GE LGALS8 208936 x at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006499
NM_201543
NM_201544
NM_201545

NM_001199043
NM_001291055
NM_001291057
NM_001291060
NM_018886

RefSeq (protein)

NP_006490
NP_963837
NP_963838
NP_963839

Location (UCSC) Chr 1: 236.52 – 236.55 Mb Chr 13: 12.44 – 12.46 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Galectin-8 is a protein of the galectin family that in humans is encoded by the LGALS8 gene.[3][4][5]

Function[edit]

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.[5]

Role in cellular defence[edit]

Galectin-8 has recently been shown to have a role in cellular defence, against both bacterial cytosolic infection and vacuolar damage.[6] 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.[6] 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.[6][7]

Interactions[edit]

Galectin-8 has been shown to interact with CD49d,[8] CD29[8] and CD49c.[8]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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. 
  4. ^ 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 38969Freely accessible. PMID 8692978. 
  5. ^ a b "Entrez Gene: LGALS8 lectin, galactoside-binding, soluble, 8 (galectin 8)". 
  6. ^ 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. PMC 3343631Freely accessible. PMID 22246324. 
  7. ^ Huang J & Brumell. (February 2012). "A sweet way of sensing danger". Nature. 482: 316–317. doi:10.1038/482316a. PMID 22337047. 
  8. ^ 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[edit]