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Receptor-mediated endocytosis of plasminogen activators and activator/inhibitor complexes

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Recent findings have elucidated the mechanism for clearance from the extracellular space of the two types of plasminogen activators, urokinase-type plasminogen activator (u-PA) and tissue-type plasminogen activator (t-PA), and their type-1 inhibitor (PAI-1). Activator/PAI-1 complexes and uncomplexed t-PA bind to the multi-ligand receptors alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein (alpha 2MR) and epithelial glycoprotein 330 (gp330). These receptors mediate endocytosis and degradation of u-PA/PAI-1 complex bound to the glycosyl phosphatidyl inositol-anchored urokinase receptor (u-PAR) on cell surfaces, and participate, in cooperation with other receptors, in hepatic clearance of activator/PAI-1 complexes and uncomplexed t-PA from blood plasma. The alpha 2MR- and gp330-mediated endocytosis of a ligand (u-PA/PAI-1 complex) initially bound to another receptor (u-PAR) is a novel kind of interaction between membrane receptors. Binding to alpha 2MR and gp330 is a novel kind of molecular recognition of serine proteinases and serpins.
Original languageEnglish
JournalF E B S Letters
Pages (from-to)239-45
Number of pages7
Publication statusPublished - 1994

    Research areas

  • Amino Acid Sequence, Animals, Endocytosis, Heymann Nephritis Antigenic Complex, Humans, Low Density Lipoprotein Receptor-Related Protein-1, Membrane Glycoproteins, Molecular Sequence Data, Plasminogen Activators, Plasminogen Inactivators, Receptors, Immunologic

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