Biochemical properties of plasminogen activator inhibitor-1.
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.
Dupont
Daniel Miotto
DM
Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark.
Madsen
Jeppe Buur
JB
Kristensen
Thomas
T
Bodker
Julie Stove
JS
Blouse
Grant Ellsworth
GE
Wind
Troels
T
Andreasen
Peter Andre
PA
D001704:Biopolymers; D004705:Endocytosis; D006801:Humans; D017395:Plasminogen Activator Inhibitor 1 / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011973:Receptors, LDL / Q000378:metabolism
D001704:Biopolymers; D017395:Plasminogen Activator Inhibitor 1; D011973:Receptors, LDL