Plasminogen receptors in the mediation of pericellular proteolysis.
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.
Plow
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Committee on Vascular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.
Miles
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D001665:Binding Sites; D002465:Cell Movement / Q000502:physiology*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism*; D005732:Gangliosides / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000502:physiology*; D055293:Receptors, Urokinase Plasminogen Activator; D000979:alpha-2-Antiplasmin / Q000378:metabolism
D016326:Extracellular Matrix Proteins; D005732:Gangliosides; C524898:PLAUR protein, human; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D000979:alpha-2-Antiplasmin; D005341:Fibrinolysin