Aliases for ITGB3 Gene
External Ids for ITGB3 Gene
Previous HGNC Symbols for ITGB3 Gene
Previous GeneCards Identifiers for ITGB3 Gene
The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in platelets. Integrins are known to participate in cell adhesion as well as cell-surface mediated signalling. [provided by RefSeq, Jul 2008]
GeneCards Summary for ITGB3 Gene
ITGB3 (Integrin, Beta 3 (Platelet Glycoprotein IIIa, Antigen CD61)) is a Protein Coding gene. Diseases associated with ITGB3 include fetal and neonatal alloimmune thrombocytopenia and thrombasthenia of glanzmann and naegeli, itgb3-related. Among its related pathways are PI3K-Akt signaling pathway and Ras signaling pathway. GO annotations related to this gene include identical protein binding and cell adhesion molecule binding. An important paralog of this gene is ITGB4.
UniProtKB/Swiss-Prot for ITGB3 Gene
Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets (By similarity). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposis sarcoma lesions.
Integrins are ubiquitously expressed adhesion molecules. They are cell-surface receptors that exist as heterodimers of alpha and beta subunits. At physiological conditions, integrins are highly glycosylated and contain a Ca2+ or Mg2+ ion, which is essential for ligand binding. Integrin receptors are critical for cell attachment to the extracellular matrix (ECM) and this is mediated through integrin-fibronectin, -vitronectin, -collagen and -laminin interactions. Intracellularly, integrins form adhesion complexes with proteins including talin, vinculin, paxillin and alpha-actinin. They also regulate kinases, such as focal adhesion kinase and Src family kinases, to mediate attachment to the actin cytoskeleton. Integrins also have a significant role in cell signaling and can activate protein kinases involved in the regulation of cell growth, division, survival, differentiation, migration and apoptosis. Glycoprotein II/IIIb (alphaIIbeta3) is an integrin receptor found on the surface of platelets. It is involved in the cross-linking of platelets with fibrin, and so has a vital role in blood clot formation.