Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins
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منابع مشابه
Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins
The binding of urokinase plaminogen activator (uPA) to its cell surface receptor (uPAR; CD87) promotes cell adhesion by increasing the affinity of the receptor for both vitronectin (VN) and integrins. We provide evidence that plasminogen activator inhibitor (PAI)-1 can detach cells by disrupting uPAR-VN and integrin-VN interactions and that it does so by binding to the uPA present in uPA-uPAR-i...
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Negatively charged organochemical inactivators of the anti-proteolytic activity of plasminogen activator inhibitor-1 (PAI-1) convert it to inactive polymers. As investigated by native gel electrophoresis, the size of the PAI-1 polymers ranged from dimers to multimers of more than 20 units. As compared with native PAI-1, the polymers exhibited an increased resistance to temperature-induced unfol...
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We have described a monoclonal antibody that rounds and detaches chick skeletal myoblasts and myotubes from extracellular substrata. The antibody also inhibits the attachment of myogenic cells to a gelatin-coated substratum but has no detectable effect on myoblast fusion. The cellular response to antibody treatment varies with differentiation and cell type. Young myoblasts and myotubes are rapi...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2003
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.200208117