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- W2041334951 abstract "Plasminogen activator inhibitor-1 (PAI-1) is a potential target for anti-thrombotic and anti-cancer therapy. It circulates in plasma in a complex with vitronectin (VN). We have studied biochemical mechanisms for PAI-1 neutralisation and its modulation by VN, using site-directed mutagenesis and limited proteolysis. We demonstrate that VN, besides delaying conversion of PAI-1 to the inactive latent form, also protects PAI-1 against cold- and detergent-induced substrate behaviour and counteracts conversion of PAI-1 to inert forms by certain amphipathic organochemical compounds. VN protection against cold- and detergent-induced substrate behaviour is associated with inhibition of the proteolytic susceptibility of beta-strand 5A. Alanine substitution of a lysine residue placed centrally in beta-strand 5A implied a VN-induced acceleration of latency transition, instead of the normal delay. This substitution not only protects PAI-1 against neutralisation, but also counteracts VN-induced protection against neutralisation. We conclude that beta-strand 5A plays a crucial role in VN-regulation of PAI-1 activity." @default.
- W2041334951 created "2016-06-24" @default.
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- W2041334951 date "2002-06-01" @default.
- W2041334951 modified "2023-09-26" @default.
- W2041334951 title "The role of β-strand 5A of plasminogen activator inhibitor-1 in regulation of its latency transition and inhibitory activity by vitronectin" @default.
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- W2041334951 doi "https://doi.org/10.1016/s0167-4838(02)00312-6" @default.
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