Receptor-mediated endocytosis of plasminogen activators and activator/inhibitor complexes
Autor: | Lars Kjøller, Jørgen Gliemann, Peter A. Andreasen, Claus Munch Petersen, Anders Nykjaer, Lars Sottrup-Jensen, Søren K. Moestrup |
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Rok vydání: | 1994 |
Předmět: |
Molecular Sequence Data
Heymann Nephritis Antigenic Complex Biophysics Plasminogen activator Biology Endocytosis Biochemistry Plasminogen Activators Structural Biology Cell surface receptor α2-Macroglobulin Genetics Animals Humans Amino Acid Sequence Receptors Immunologic Receptor Molecular Biology Serpin Membrane Glycoproteins T-plasminogen activator Activator (genetics) Cell Biology Receptor-mediated endocytosis Urokinase receptor Plasminogen Inactivators Proteolysis Serine proteinase Low Density Lipoprotein Receptor-Related Protein-1 Glycosyl phosphatidyl inositol |
Zdroj: | FEBS Letters. 338:239-245 |
ISSN: | 0014-5793 |
DOI: | 10.1016/0014-5793(94)80276-9 |
Popis: | 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. |
Databáze: | OpenAIRE |
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