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- W43506750 abstract "We have investigated the intracellular signaling events generated during the interaction of integrins with extracellular matrix proteins in human endothelial cells (HEC). Within 30 s from adhesion to fibronectin, HEC showed increased tyrosine phosphorylation of a group of proteins with molecular mass of 100–130 and 70 kDa. Tyrosine phosphorylation of these proteins was triggered by several extracellular matrix ligands, including collagens type I and IV, laminin and vitronectin and could be mimicked by antibodies toα3βl,α5βl, andα6β1 integrin complexes. Among the tyrosine phosphoproteins regulated by integrins, we identified the focal adhesion tyrosine kinase pl25FAK. Inhibition of tyrosine phosphorylation with genistein during adhesion of HEC to fibronectin severly prevented the organization of focal adhesions and actin stress fibers, but did not inhibit adhesionper se. The role ofβi integrins in stimulating intracellular tyrosine phosphorylation was further investigated by analyzing a naturally occurring variant ofβ1 integrin(β1B) with a distinct cytoplasmic domain (Altruda et al., 1990).Β1B, expressed in Chinese hamster ovary (CHO) cells, formed heterodimers with theα3 andα5 subunits and bind fibronectin in a RGD-dependent manner (Balzac et al., 1993). Theα5β1B complex, however, did not stimulate tyrosine phosphorylation of the 100-130 kDa proteins and did not localize at focal adhesions. Moreover, cells expressingβ1B showed reduced migration in a Boyden chamber assay and poor spreading on fibronectin and laminin. This was not a generalized adhesive defect since cell spreading on vitronectin, aβ3 integrin-dependent adhesion, was unchanged. These data show thatβ1 integrin cytoplasmic domain is critical in the stimulation of intracellular protein tyrosine phosphorylation; this signalling, moreover, is important in the organization of actin stress fibers and in the control of cell spreading and migration on matrix proteins." @default.
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- W43506750 date "1995-01-01" @default.
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- W43506750 title "Role ofβ1 integrin cytoplasmic domain in signaling and cell adhesion" @default.
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- W43506750 doi "https://doi.org/10.1007/978-3-0348-9057-1_19" @default.
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