Summary
Although plasminogen activator inhibitor 1 (PAI-1) is one of the primary regulators
of the fibrinolytic system, it also has dramatic effects on cell adhesion, detachment
and migration. PAI-1 also differs from other serine protease inhibitors (serpins)
in that it is a trace protein in plasma, it has a short half-life in vivo, its synthesis is highly regulated, and it binds to the adhesive glycoprotein vitronectin
(VN) with high affinity and specificity. These unique and diverse properties of PAI-1
probably account for the many observations in the literature that correlate abnormalities
in PAI-1 gene expression with a variety of pathological conditions. In this review,
we discuss the discovery, origin, properties and regulation of PAI-1, and then speculate
about its potential role in vascular disease, fibrosis, obesity and the metabolic
syndrome, and cancer.
Keywords
PAI-1 - vascular disease - fibrosis - obesity - cancer