Print page Print page
Switch language
The Capital Region of Denmark - a part of Copenhagen University Hospital

Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosyl-phosphatidylinositol

Research output: Contribution to journalJournal articleResearchpeer-review

  1. Tumor cell MT1-MMP is dispensable for osteosarcoma tumor growth, bone degradation and lung metastasis

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Chylomicronemia From GPIHBP1 Autoantibodies Successfully Treated With Rituximab: A Case Report

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Chylomicronemia from GPIHBP1 autoantibodies

    Research output: Contribution to journalReviewResearchpeer-review

  4. Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

    Research output: Contribution to journalJournal articleResearchpeer-review

  5. ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain

    Research output: Contribution to journalEditorialResearchpeer-review

View graph of relations

The cellular receptor for human urokinase-type plasminogen activator (u-PAR) is shown by several independent criteria to be a true member of a family of integral membrane proteins, anchored to the plasma membrane exclusively by a COOH-terminal glycosyl-phosphatidylinositol moiety. 1) Amino acid analysis of u-PAR after micropurification by affinity chromatography and N-[2-hydroxy-1,1-bis(hydroxymethyl)-ethyl]glycine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of 2-3 mol of ethanolamine/mol protein. 2) Membrane-bound u-PAR is efficiently released from the surface of human U937 cells by trace amounts of purified bacterial phosphatidylinositol-specific phospholipase C. This soluble form of u-PAR retains the binding specificity toward both u-PA and its amino-terminal fragment holding the receptor-binding domain. 3) Treatment of purified u-PAR with phosphatidylinositol-specific phospholipase C or mild alkali completely alters the hydrophobic properties of the receptor as judged by temperature-induced detergent-phase separation and charge-shift electrophoresis. 4) Biosynthetic labeling of u-PAR was obtained with [3H]ethanolamine and myo-[3H]inositol. 5) Finally, comparison of amino acid compositions derived from cDNA sequence and amino acid analysis shows that a polypeptide of medium hydrophobicity is excised from the COOH terminus of the nascent u-PAR. A similar proteolytic processing has been reported for other proteins that are linked to the plasma membrane by a glycosyl-phosphatidylinositol membrane anchor.

Original languageEnglish
JournalThe journal of biological chemistry
Issue number3
Pages (from-to)1926-33
Number of pages8
Publication statusPublished - 25 Jan 1991

    Research areas

  • Amino Acids, Ethanolamine, Ethanolamines, Glycolipids, Glycosylphosphatidylinositols, Humans, In Vitro Techniques, Membrane Glycoproteins, Molecular Weight, Phosphatidylinositol Diacylglycerol-Lyase, Phosphatidylinositols, Phosphoinositide Phospholipase C, Phosphoric Diester Hydrolases, Polysaccharides, Protein Processing, Post-Translational, Receptors, Cell Surface, Receptors, Urokinase Plasminogen Activator, Solubility, Tumor Cells, Cultured, Urokinase-Type Plasminogen Activator

ID: 46434591