GPVI

Glycoprotein VI (platelet), also known as GPVI, is a glycoprotein receptor for collagen which is expressed in platelets. In humans, glycoprotein VI is encoded by the GPVI gene.[5] GPVI was first cloned in 2000 by several groups including that of Martine Jandrot-Perrus from INSERM.

GP6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGP6, BDPLT11, GPIV, GPVI, glycoprotein VI platelet
External IDsOMIM: 605546 MGI: 1889810 HomoloGene: 9488 GeneCards: GP6
Gene location (Human)
Chr.Chromosome 19 (human)[1]
Band19q13.42Start55,013,705 bp[1]
End55,038,264 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

51206

243816

Ensembl

ENSMUSG00000078810

UniProt

Q9HCN6

P0C191

RefSeq (mRNA)

NM_016363
NM_001083899
NM_001256017

NM_001163014

RefSeq (protein)

NP_001077368
NP_001242946
NP_057447

NP_001156486

Location (UCSC)Chr 19: 55.01 – 55.04 MbChr 7: 4.36 – 4.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

Glycoprotein VI (GP6) is a 58-kD platelet membrane glycoprotein that plays a crucial role in the collagen-induced activation and aggregation of platelets. Upon injury to the vessel wall and subsequent damage to the endothelial lining, exposure of the subendothelial matrix to blood flow results in deposition of platelets. Collagen fibers are the most thrombogenic macromolecular components of the extracellular matrix, with collagen types I, III, and VI being the major forms found in blood vessels. Platelet interaction with collagen occurs as a 2-step procedure: (1) the initial adhesion to collagen is followed by (2) an activation step leading to platelet secretion, recruitment of additional platelets, and aggregation. In physiologic conditions, the resulting platelet plug is the initial hemostatic event limiting blood loss. However, exposure of collagen after rupture of atherosclerotic plaques is a major stimulus of thrombus formation associated with myocardial infarction or stroke.[6][7]

Complete or partial deficiency of GPVI in humans is a rare condition presenting as a mild bleeding disorder.

Interactions

GPVI has been shown to interact with LYN.[8]

See also

References

  1. ENSG00000274050, ENSG00000278670, ENSG00000276211, ENSG00000277439, ENSG00000278316, ENSG00000275633, ENSG00000274566, ENSG00000275931, ENSG00000276065 GRCh38: Ensembl release 89: ENSG00000088053, ENSG00000274050, ENSG00000278670, ENSG00000276211, ENSG00000277439, ENSG00000278316, ENSG00000275633, ENSG00000274566, ENSG00000275931, ENSG00000276065 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000078810 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Ezumi Y, Uchiyama T, Takayama H (Oct 2000). "Molecular cloning, genomic structure, chromosomal localization, and alternative splice forms of the platelet collagen receptor glycoprotein VI". Biochemical and Biophysical Research Communications. 277 (1): 27–36. doi:10.1006/bbrc.2000.3624. PMID 11027634.
  6. "Entrez Gene: GP6 glycoprotein VI (platelet)".
  7. Jandrot-Perrus M, Busfield S, Lagrue AH, Xiong X, Debili N, Chickering T, Le Couedic JP, Goodearl A, Dussault B, Fraser C, Vainchenker W, Villeval JL (Sep 2000). "Cloning, characterization, and functional studies of human and mouse glycoprotein VI: a platelet-specific collagen receptor from the immunoglobulin superfamily". Blood. 96 (5): 1798–807. doi:10.1182/blood.V96.5.1798. PMID 10961879.
  8. Suzuki-Inoue K, Tulasne D, Shen Y, Bori-Sanz T, Inoue O, Jung SM, Moroi M, Andrews RK, Berndt MC, Watson SP (Jun 2002). "Association of Fyn and Lyn with the proline-rich domain of glycoprotein VI regulates intracellular signaling". The Journal of Biological Chemistry. 277 (24): 21561–6. doi:10.1074/jbc.M201012200. PMID 11943772.

Further reading

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