Interactions between type 1 plasminogen activator inhibitor, extracellular matrix and vitronectin

Cell Differ Dev. 1990 Dec 2;32(3):287-92. doi: 10.1016/0922-3371(90)90041-t.

Abstract

Regulation of plasminogen activation is a key process in controlling proteolytic events in the extracellular matrix (ECM) and this regulation is achieved through the action of specific plasminogen activator (PA) inhibitors (PAIs). Type I PAI (PAI-1) is the physiological inhibitor both of urinary-type PA (u-PA) and tissue-type PA (t-PA) (Loskutoff et al., 1989) and is a major component of the ECM of cultured cells. This inhibitor may protect ECM constituents against cellular proteases and thus influence the cell migration and tissue destruction that occurs during development, inflammation and tumor metastasis. In this review, we discuss the properties of PAI-1 and the evidence that the binding of PAI-1 to ECM is mediated by serum-derived vitronectin (Vn).

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Cattle
  • Cells, Cultured
  • Endothelium, Vascular / cytology
  • Enzyme Activation
  • Extracellular Matrix / metabolism*
  • Extracellular Matrix Proteins / metabolism
  • Glycoproteins / physiology*
  • Plasminogen Activators / metabolism
  • Plasminogen Inactivators / metabolism*
  • Protein Binding
  • Urokinase-Type Plasminogen Activator / metabolism
  • Vitronectin

Substances

  • Extracellular Matrix Proteins
  • Glycoproteins
  • Plasminogen Inactivators
  • Vitronectin
  • Plasminogen Activators
  • Urokinase-Type Plasminogen Activator