Plasminogen receptors in the mediation of pericellular proteolysis

Cell Differ Dev. 1990 Dec 2;32(3):293-8. doi: 10.1016/0922-3371(90)90042-u.

Abstract

A wide variety of cells bind plasminogen with very high capacity, with similar affinity and recognize the same structural features within the plasminogen molecule. As a consequence of binding to cell surfaces, plasminogen is more readily activated to plasmin. Plasmin remains cell-bound where it can degrade matrix constituents and is protected from inactivation by alpha 2-antiplasmin. Thus, the functional consequence of plasminogen binding to cells is pericellular proteolysis, permitting cell migration. Both proteins and nonprotein cell-surface constituents function as plasminogen binding sites. Gangliosides exhibit the appropriate properties of the non-protein plasminogen receptors.

Publication types

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

MeSH terms

  • Binding Sites
  • Cell Movement / physiology*
  • Extracellular Matrix Proteins / metabolism*
  • Fibrinolysin / metabolism*
  • Gangliosides / metabolism
  • Humans
  • Protein Binding
  • Receptors, Cell Surface / physiology*
  • Receptors, Urokinase Plasminogen Activator
  • alpha-2-Antiplasmin / metabolism

Substances

  • Extracellular Matrix Proteins
  • Gangliosides
  • PLAUR protein, human
  • Receptors, Cell Surface
  • Receptors, Urokinase Plasminogen Activator
  • alpha-2-Antiplasmin
  • Fibrinolysin