Integrins: Structure, Function, and Biological Properties

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A family of cell adhesion receptors, termed integrins, has been defined that potentiate a wide variety of cell-cell and cell-matrix interactions. Integrins not only mediate cell adhesion events but are also involved in transmitting signals from the extracellular environment to the intracellular compartment. Integrins are heterodimeric molecules expressed on the cell surface that require divalent cations for functional activity. The integrin family is composed of at least 18 members based on the expression of 12α and 7β subunits. Depending on the α/β subunit pairing, the intact heterodimer can recognize either one or multiple ligands present in the extracellular matrix or on the surface of opposing cells. In some cases, a given β subunit such as β1 , can associate with multiple a subunits leading to cell adhesion to ligands, such as fibronectin, collagen, and laminin among others. The β2 integrins are restricted to leukocytes and primarily mediate cell-cell interactions that are important in immune recognition and inflammation. The β3 integrins include two members characterized by αIIβ expressed on platelets and a v expressed on a variety of cell types. The β3 integrins recognize fibrinogen, fibronectin, von Willebrand factor, and vitronectin among others.

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