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• W2026458454 endingPage "2320" @default.
• W2026458454 startingPage "2314" @default.
• W2026458454 abstract "We have shown that a heptapeptide which resides in the middle part of vitronectin (VN) is responsible for binding to plasminogen activator inhibitor-1 (PAI-1). A single PAI-1 binding peptide was isolated from human VN after limited proteolysis with protease V8. The amino acid sequence of the fragment corresponded to residues Gly-115-Glu-121 of VN. A murine monoclonal antibody (JYV-1) raised against human VN bond to the same fragment and inhibited binding of PAI-1 to VN. A synthetic peptide (V-115), comprising residues Gly-115-Glu-121 of human VN, competed with VN for both PAI-1 and JYV-1 in a dose-dependent manner. Synthetic peptide V-111 (Ser-111-Glu-121) had a stronger inhibitory effect than V-115 on binding of PAI-1 or JYV-1 to VN. V-111 also inhibited the binding of human PAI-1 to mouse and rabbit VN. The functional half-life of PAI-1 activity was prolonged approximately 2-fold in the presence of V-111 (1 mM). This stabilizing effect of V-111 was equivalent to intact VN, although a 1000-fold higher molar concentration of V-111 over VN was required. These data indicated that VN residues Gly-115-Glu-121 contain a PAI-1 binding site." @default.
• W2026458454 created "2016-06-24" @default.
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• W2026458454 date "1993-03-09" @default.
• W2026458454 modified "2023-09-24" @default.
• W2026458454 title "Identification of the plasminogen activator inhibitor-1 binding heptapeptide in vitronectin" @default.
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• W2026458454 doi "https://doi.org/10.1021/bi00060a024" @default.
• W2026458454 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7680229" @default.
• W2026458454 hasPublicationYear "1993" @default.
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