Open Access
Article
Biochemical properties of plasminogen activator inhibitor-1
Daniel Miotto Dupont1,Jeppe Buur Madsen1,Thomas Kristensen1,Julie Stove Bodker1,Grant Ellsworth Blouse1,Troels Wind1,Peter Andre Andreasen1
1
Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark
DOI: 10.2741/3312 Volume 14 Issue 4, pp.1337-1361
Published: 01 January 2009
(This article belongs to the Special Issue Urokinase-mediated plasminogen activation system)
Abstract

PAI-1 is a Mr ~50,000 glycoprotein, which is the primary physiological inhibitor of the two plasminogen activators uPA and tPA. PAI-1 belongs to the serpin protein family. Studies of PAI-1 have contributed significantly to the elucidation of the protease inhibitory mechanism of serpins, which is based on a metastable native state becoming stabilised by insertion of the RCL into the central beta-sheet A and formation of covalent complexes with target proteases. In PAI-1, this insertion can occur in the absence of the protease, resulting in generation of a so-called latent, inactive form of the protein. PAI-1, in its active state, also binds to the extracellular protein vitronectin. When in complex with its target proteases, it binds with high affinity to endocytosis receptors of the low density receptor family.

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Daniel Miotto Dupont, Jeppe Buur Madsen, Thomas Kristensen, Julie Stove Bodker, Grant Ellsworth Blouse, Troels Wind, Peter Andre Andreasen. Biochemical properties of plasminogen activator inhibitor-1. Frontiers in Bioscience-Landmark. 2009. 14(4); 1337-1361.