4.6 Review

PAI-1, progress in understanding the clinical problem and its aetiology

Journal

BRITISH JOURNAL OF HAEMATOLOGY
Volume 157, Issue 3, Pages 291-298

Publisher

WILEY
DOI: 10.1111/j.1365-2141.2012.09074.x

Keywords

PAI-1; Serpine1; haemostasis; pathophysiology

Categories

Funding

  1. Japan Society for the Promotion of Science (JSPS) KAKENHI [20890093, 22790247]
  2. Japan Science and Technology Agency (JST) [AS232Z01751F]
  3. Uehara Memorial Foundation
  4. Grants-in-Aid for Scientific Research [22590826, 22790247, 20890093, 21590230, 24590273] Funding Source: KAKEN

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Plasminogen activator inhibitor-1 (PAI-1, also known as SERPINE1) is a member of the serine protease inhibitor (SERPIN) superfamily and is the primary physiological regulator of urokinase-type plasminogen activator (uPA) and tissue-type plasminogen activator (tPA) activity. Although the principal function of PAI-1 is the inhibition of fibrinolysis, PAI-1 possesses pleiotropic functions besides haemostasis. In the quarter century since its discovery, a number of studies have focused on improving our understanding of PAI-1 functions in vivo and in vitro. The use of Serpine1-deficient mice has particularly enhanced our understanding of the functions of PAI-1 in various physiological and pathophysiological conditions. In this review, the results of recent studies on PAI-1 and its role in clinical conditions are discussed.

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