title: Historical analysis of PAI-1 from its discovery to its potential role in cell motility and disease.
abstract: 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.
authors.affiliation: Department of Cellular Biology, Division of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
authors.forename: Claudia
authors.initials: C
authors.lastname: Dellas
authors.forename: David J
authors.initials: DJ
authors.lastname: Loskutoff
mesh_terms: D002465:Cell Movement; D004194:Disease / Q000209:etiology*; D005786:Gene Expression Regulation; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D017395:Plasminogen Activator Inhibitor 1 / Q000235:genetics / Q000266:history* / Q000502:physiology
chemical_list: D017395:Plasminogen Activator Inhibitor 1