Integrins are a large family of homologous transmembrane linker proteins that include collagen, fibronectin and laminin. They are a family of cell-surface proteins that mediated cell adhesion, a process that is essential for anchorage, and act as cues for cell migration and signals for growth and differentaition.1 In addition to their biological importance to fundamental cellular processes, integrins play a part in immune function, tissue repair, tumour invasion, and platelet aggregation.2 The integrins are a major family of adhesion receptors produced by most cell types and are a means by which the cell senses its immediate environment and responds to changes in extracellular matrix composition. dynamic family of receptors capable of translating information into and out of the cell.3 Each member of the integrin family consists of a non-covalently linked heterodimer of an a chain and a b chain, which are transmembrane proteins with short cytoplasmic tails. They are subdivided!
             according to the eight different b subunits, and more than 20 different ab combinations have been recognised. Different types of cells assemble and express different b complexes. Although most cells express diverse integrins, some are found only on specific cell types. Eg. The aIIbb3 integrin is found exclusively on megakaryocytes and platelets, and the b2 (CD18) integrin is detected only on leucocytes. Many integrins bind to extracellular-matrix proteins (fibronectin, various collagens, von Willebrand factor, and vitronectin) and take part in the mediation of interactions between cells and the extracellular matrix; other integrins bind to cell-membrane proteins (eg, intracellular adhesion molecules 1 and 2) and mediate cell-cell adhesion. Integrins also function a cell signal transducers, activating various intracellular signalling pathways when activated by matrix binding. A cell can regulate the activity of its integrins by altering either their matrix-bin...