Plasminogen activator inhibitor type 1 (PAI-1) is the key regulator of the fibrinolytic
system, thereby acting as a potent mediator in thrombosis. Plasminogen activators
such as PAI-1 mediate the conversion of the inactive zymogen plasminogen to plasmin,
an active serine protease. As a member of the serpin superfamily, the highly conserved
structure of PAI-1 is critical for its regulatory function. This review elucidates
PAI-1 structure, function, and genetic architecture, and then discusses intracellular
and extracellular functions that have broad implications for proliferative signaling
and cell death, angiogenesis, cellular transit, and emerging roles in cancer biology.
By understanding the complex and elaborate mechanism of PAI-1 in the fibrinolytic
system and as a biomarker, PAI-1 may have broad implications across many disease states
not related to its historical roles in fibrinolysis and thrombosis.
Keywords
PAI-1 - extracellular matrix - genetics - fibrinolytic system - cell migration - cell
proliferation
Bibliographical Record
Jacob Wortley, Justin Vu, Neha Soogoor, Mebeli Becerra, Mohanakrishnan Sathyamoorthy.
A Contemporary Review of Plasminogen Activator Inhibitor Type 1: Structure, Function,
Genetic Architecture, and Intracellular/Extracellular Roles. TH Open 2025; 09: a26984219.
DOI: 10.1055/a-2698-4219