Plasminogen receptors in the mediation of pericellular proteolysis

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 α₂-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.