Integrins are ubiquitously expressed adhesion molecules. They are cell-surface receptors that exist as heterodimers of α and β subunits. Under physiological conditions, integrins are highly glycosylated and contain a Ca2+ or Mg2+ ion, which is essential for ligand binding.
Integrin receptors 'integrate' the extracellular environment with the cell interior by binding both the extracellular matrix (ECM) and the cytoskeleton. They are critical for cell attachment to the ECM, which is mediated through integrin-fibronectin, -vitronectin, -collagen and -laminin interactions. Intracellularly, integrins form adhesion complexes with proteins including talin, vinculin, paxillin and α-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 (αIIbβ3) 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.View all products for Integrin Receptors »
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Literature for Integrin Receptors
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