• The 2C9.G2 monoclonal antibody specifically binds to the integrin β3 chain (CD61), which associates with the integrin αv chain (CD51) to form the vitronectin receptor, as well as the αIIb chain (CD41) to form the gpIIb/IIIa complex. (bdbiosciences.com)
  • Many epidemiological studies have evaluated associations of platelet glycoprotein receptor alpha2beta1 integrin (ITGA2) and glycoprotein IIIa (ITGB3) gene polymorphisms with diabetic retinopathy (DR), but the published data are inconclusive. (nih.gov)
  • The ITGB3 gene provides instructions for making the beta3 subunit of a receptor protein called integrin alphaIIb/beta3 (αIIbβ3), which is found on the surface of small cells called platelets. (medlineplus.gov)
  • Unlike Glanzmann thrombasthenia, this disorder results from a mutation in only one copy of the ITGB3 gene in each cell, and the mutations result in the formation of some integrin αIIbβ3 that is abnormally turned on (active), even when no clot is being formed. (medlineplus.gov)
  • Because the mutation that causes this disorder affects only one copy of the ITGB3 gene, some normal integrin is formed and normal platelets produced, which accounts for the mild signs and symptoms in affected individuals. (medlineplus.gov)
  • From NCBI Gene: The ITGB3 protein product is the integrin beta chain beta 3. (nih.gov)
  • Attachment of integrin αIIbβ3 from adjacent platelets to the same fibrinogen protein helps platelets cluster together (platelet cohesion) to form a blood clot. (medlineplus.gov)
  • Integrin αIIbβ3 can also bind other proteins on platelets and in the blood as well as proteins within the intricate lattice that forms in the space between cells (extracellular matrix) to ensure proper clot formation and promote wound healing. (medlineplus.gov)
  • The overactive integrin αIIbβ3 binds inappropriately to clotting proteins within the cell during the formation of platelets, causing the platelets to become misshapen and large. (medlineplus.gov)
  • Integrin beta 3 is found along with the alpha IIb chain in platelets. (nih.gov)
  • 7. The in-vitro effect of tirofiban, glycoprotein IIb/IIIa antagonist, on various responses of porcine blood platelets. (nih.gov)
  • 8. Involvement of activated integrin alpha2beta1 in the firm adhesion of platelets onto a surface of immobilized collagen under flow conditions. (nih.gov)
  • The beta3 subunit attaches (binds) to the alphaIIb subunit, which is produced from the ITGA2B gene, to form integrin αIIbβ3. (medlineplus.gov)
  • It is an integrin complex containing INTEGRIN ALPHAIIB and INTEGRIN BETA3 which recognizes the arginine-glycine-aspartic acid (RGD) sequence present on several adhesive proteins. (nih.gov)
  • An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. (bvsalud.org)
  • 12. Complementary roles of glycoprotein VI and alpha2beta1 integrin in collagen-induced thrombus formation in flowing whole blood ex vivo. (nih.gov)
  • Leukocyte-endothelial adhesion is also mediated by the binding of αvβ3 integrin or vitronectin receptor to CD31 (PECAM-1). (bdbiosciences.com)
  • 19. Differential integrin activity mediated by platelet collagen receptor engagement under flow conditions. (nih.gov)
  • Association of the platelet GPIIb/IIIa polymorphism with atherosclerotic plaque morphology: the Atherosclerosis Risk in Communities (ARIC) Study. (snpedia.com)
  • PMID 18045240 ] Immunologic and structural analysis of eight novel domain-deletion beta3 integrin peptides designed for detection of HPA-1 antibodies. (snpedia.com)
  • A shortage (deficiency) of functional integrin αIIbβ3 prevents sufficient binding of fibrinogen or other proteins, impairing the formation of blood clots. (medlineplus.gov)
  • Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. (nih.gov)
  • Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. (wikipedia.org)
  • 3. Distinct roles of GPVI and integrin alpha(2)beta(1) in platelet shape change and aggregation induced by different collagens. (nih.gov)
  • 10. Platelet adhesion to collagen and collagen-related peptide under flow: roles of the [alpha]2[beta]1 integrin, GPVI, and Src tyrosine kinases. (nih.gov)
  • CD41+Antigen at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Overview of all the structural information available in the PDB for UniProt: P08514 (Human Integrin alpha-IIb) at the PDBe-KB. (wikipedia.org)
  • The mutations that cause this disorder occur in both copies of the gene in each cell and impair the production or activity of the beta3 subunit, which disrupts the formation of functional integrin αIIbβ3. (medlineplus.gov)
  • Integrin alpha-IIb is a protein that in humans is encoded by the ITGA2B gene. (wikipedia.org)
  • ITGA2B, also known as CD41, encodes integrin alpha chain 2b. (wikipedia.org)
  • During clot formation, integrin αIIbβ3 binds to a protein called fibrinogen. (medlineplus.gov)
  • 5. Distinct but critical roles for integrin alphaIIbbeta3 in platelet lamellipodia formation on fibrinogen, collagen-related peptide and thrombin. (nih.gov)
  • Anti-αIIbß3 drugs like eptifibatide can engage the inactive integrin directly, inhibiting thrombosis but inadvertently impairing αIIbß3 hemostatic functions. (bvsalud.org)
  • In addition, interaction of the αvβ3 integrin with its ligands regulates the L-type Ca2+ channel in vascular smooth muscle cells, possibly mediating vasodilatory responses to injury. (bdbiosciences.com)
  • Integrins are known to participate in cell adhesion as well as cell-surface mediated signalling. (nih.gov)
  • PMID 22015659 ] Mean platelet volume and integrin alleles correlate with levels of integrins alpha(IIb)beta(3) and alpha(2)beta(1) in acute coronary syndrome patients and normal subjects. (snpedia.com)
  • A given chain may combine with multiple partners resulting in different integrins. (nih.gov)
  • 20. A defined peptide that inhibits the formation of the glycoprotein IIb and IIIa complex. (nih.gov)
  • These results advance our understanding of integrin structure and function and may guide development of safer inhibitors. (bvsalud.org)