Platelet glycoprotein VI

Last updated
GP6
Protein GP6 PDB 2gi7.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases GP6 , BDPLT11, GPIV, GPVI, glycoprotein VI platelet
External IDs OMIM: 605546 MGI: 1889810 HomoloGene: 9488 GeneCards: GP6
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 Mb Chr 7: 4.37 – 4.4 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Platelet glycoprotein VI (GPVI) is a glycoprotein receptor for collagen which is expressed in platelets. In humans, glycoprotein VI is encoded by the GP6 gene. [5] It was first cloned in 2000 by several groups including that of Martine Jandrot-Perrus from INSERM.

Function

GPVI 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

Related Research Articles

<span class="mw-page-title-main">Convulxin</span> Snake venom toxin

Convulxin is a snake venom toxin found in a tropical rattlesnake known as Crotalus durissus terrificus. It belongs to the family of hemotoxins, which destroy red blood cells or, as is the case with convulxin, induce blood coagulation.

<span class="mw-page-title-main">Lymphocyte cytosolic protein 2</span> Protein-coding gene in the species Homo sapiens

Lymphocyte cytosolic protein 2, also known as LCP2 or SLP-76, is a signal-transducing adaptor protein expressed in T cells and myeloid cells and is important in the signaling of T-cell receptors (TCRs). As an adaptor protein, SLP-76 does not have catalytic functions, primarily binding other signaling proteins to form larger signaling complexes. It is a key component of the signaling pathways of receptors with immunoreceptor tyrosine-based activation motifs (ITAMs) such as T-cell receptors, its precursors, and receptors for the Fc regions of certain antibodies. SLP-76 is expressed in T-cells and related lymphocytes like natural killer cells.

<span class="mw-page-title-main">Integrin alpha 2</span> Mammalian protein found in Homo sapiens

Integrin alpha-2, or CD49b, is a protein which in humans is encoded by the CD49b gene.

<span class="mw-page-title-main">LYN</span> Mammalian protein found in Homo sapiens

Tyrosine-protein kinase Lyn is a protein that in humans is encoded by the LYN gene.

<span class="mw-page-title-main">Integrin alpha 2b</span> Mammalian protein found in Homo sapiens

Integrin alpha-IIb is a protein that in humans is encoded by the ITGA2B gene. ITGA2B, also known as CD41, encodes integrin alpha chain 2b. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 2b undergoes post-translational cleavage to yield disulfide-linked light and heavy chains that join with beta 3 to form a fibrinogen receptor expressed in platelets that plays a crucial role in coagulation. Mutations that interfere with this role result in thrombasthenia. At least 38 disease-causing mutations in this gene have been discovered. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling.

<span class="mw-page-title-main">STX4</span> Protein-coding gene in the species Homo sapiens

Syntaxin-4 is a protein that in humans is encoded by the STX4 gene.

Platelet membrane glycoproteins are surface glycoproteins found on platelets (thrombocytes) which play a key role in hemostasis. When the blood vessel wall is damaged, platelet membrane glycoproteins interact with the extracellular matrix.

<span class="mw-page-title-main">GP1BA</span> Protein-coding gene in the species Homo sapiens

Platelet glycoprotein Ib alpha chain also known as glycoprotein Ib (platelet), alpha polypeptide or CD42b, is a protein that in humans is encoded by the GP1BA gene.

<span class="mw-page-title-main">Proteinase-activated receptor 1</span> Mammalian protein found in humans

Proteinase-activated receptor 1 (PAR1) also known as protease-activated receptor 1, coagulation factor II receptor and thrombin receptor is a protein that in humans is encoded by the F2R gene. PAR1 is a G protein-coupled receptor and one of four protease-activated receptors involved in the regulation of thrombotic response. Highly expressed in platelets and endothelial cells, PAR1 plays a key role in mediating the interplay between coagulation and inflammation, which is important in the pathogenesis of inflammatory and fibrotic lung diseases. It is also involved both in disruption and maintenance of endothelial barrier integrity, through interaction with either thrombin or activated protein C, respectively.

<span class="mw-page-title-main">CEACAM1</span> Mammalian protein found in Homo sapiens

Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) also known as CD66a, is a human glycoprotein, and a member of the carcinoembryonic antigen (CEA) gene family.

<span class="mw-page-title-main">INPP5D</span> Protein-coding gene in the species Homo sapiens

Src homology 2 (SH2) domain containing inositol polyphosphate 5-phosphatase 1(SHIP1) is an enzyme with phosphatase activity. SHIP1 is structured by multiple domain and is encoded by the INPP5D gene in humans. SHIP1 is expressed predominantly by hematopoietic cells but also, for example, by osteoblasts and endothelial cells. This phosphatase is important for the regulation of cellular activation. Not only catalytic but also adaptor activities of this protein are involved in this process. Its movement from the cytosol to the cytoplasmic membrane, where predominantly performs its function, is mediated by tyrosine phosphorylation of the intracellular chains of cell surface receptors that SHIP1 binds. Insufficient regulation of SHIP1 leads to different pathologies.

<span class="mw-page-title-main">Laminin, alpha 5</span> Protein-coding gene in the species Homo sapiens

Laminin subunit alpha-5 is a protein that in humans is encoded by the LAMA5 gene.

<span class="mw-page-title-main">F11 receptor</span> Protein-coding gene in the species Homo sapiens

Junctional adhesion molecule A is a protein that in humans is encoded by the F11R gene. It has also been designated as CD321.

<span class="mw-page-title-main">GP1BB</span> Protein-coding gene in the species Homo sapiens

Glycoprotein Ib (platelet), beta polypeptide (GP1BB) also known as CD42c, is a protein that in humans is encoded by the GP1BB gene.

<span class="mw-page-title-main">Glycoprotein IX</span> Protein-coding gene in the species Homo sapiens

Glycoprotein IX (platelet) (GP9) also known as CD42a (Cluster of Differentiation 42a), is a human gene.

<span class="mw-page-title-main">RHAG</span> Protein-coding gene in the species Homo sapiens

Rh-associated glycoprotein (RHAG) is an ammonia transporter protein that in humans is encoded by the RHAG gene. RHAG has also recently been designated CD241. Mutations in the RHAG gene can cause stomatocytosis.

<span class="mw-page-title-main">CD84</span> Protein found in humans

CD84 is a human protein encoded by the CD84 gene.

<span class="mw-page-title-main">GP5 (gene)</span> Protein-coding gene in the species Homo sapiens

Glycoprotein V (platelet) (GP5) also known as CD42d (Cluster of Differentiation 42d), is a human gene.

Collagen receptors are membrane proteins that bind the extracellular matrix protein collagen, the most abundant protein in mammals. They control mainly cell proliferation, migration and adhesion, coagulation cascade activation and they affect ECM structure by regulation of MMP.

<span class="mw-page-title-main">FCER1G</span> Protein-coding gene in the species Homo sapiens

Fc fragment of IgE, high affinity I, receptor for; gamma polypeptide is a protein that in humans is encoded by the FCER1G gene.

References

  1. 1 2 3 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. 1 2 3 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