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Receptor‐mediated endocytosis of plasminogen activators and activator/inhibitor complexes
Author(s) -
Andreasen Peter A.,
Sottrup-Jensen Lars,
Kjøller Lars,
Nykjær Anders,
Moestrup Søren K.,
Petersen Claus Munch,
Gliemann Jørgen
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80276-9
Subject(s) - plasminogen activator , receptor , endocytosis , chemistry , urokinase , microbiology and biotechnology , activator (genetics) , glycoprotein , plasminogen activator inhibitor 1 , ldl receptor , biochemistry , biology , endocrinology , lipoprotein , genetics , cholesterol
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 multiligand receptors α 2 macroglubulin receptor/low density lipoprotein receptor‐related protein (α 2 MR) 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 α 2 MR‐ 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 α 2 MR and gp330 is a novel kind of molecular recognition of serine proteinases and serpins.