CD29 (beta1 integrin subunit, GPIIa) forms non-covalently linked heterodimers with at least 6 different alpha chains (alpha1-alpha6, CD49a-f) determining the binding properties of beta1 (VLA) integrins. These integrins mediate cell adhesion to collagen, fibronectin, laminin and other extracellular matrix (ECM) components. This interaction hinders cell death, whereas disruption of anchorage to ECM leads to apoptosis. Decreased expression of most beta1 integrins correlates with acquiring multidrug resistance of tumour cells during selection in presence of antitumour drug. In platelets, translocation of intracellular pool of beta1 integrins to the plasma membrane following thrombin stimulation. These integrins are also up-regulated in leukocytes during emigration and extravascular migration and appear to be critically involved in regulating the immune cell trafficking from blood to tissue, as well as in regulating tissue damage and disease symptoms related to inflammatory bowel disease. Through a beta1 integrin-dependent mechanism, fibronectin and type I collagen enhance cytokine secretion of human airway smooth muscle in response to IL-1beta.
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