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Protein GP6 PDB 2gi7.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases GP6, BDPLT11, GPIV, GPVI, glycoprotein VI platelet
External IDs OMIM: 605546 MGI: 1889810 HomoloGene: 9488 GeneCards: GP6
Gene location (Human)
Chromosome 19 (human)
Chr. Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for GP6
Genomic location for GP6
Band 19q13.42 Start 55,013,705 bp[1]
End 55,038,264 bp[1]
RNA expression pattern
PBB GE GP6 220336 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



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

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.


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.


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

See also[edit]


  1. ^ a b c 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. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000078810 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  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. 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[edit]

External links[edit]