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

Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis

Research output: Contribution to journalJournal articleResearchpeer-review

  1. FoxO3A promotes metabolic adaptation to hypoxia by antagonizing Myc function

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Plasminogen activation independent of uPA and tPA maintains wound healing in gene-deficient mice

    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. The collagen receptor uPARAP/Endo180 regulates collectins through unique structural elements in its FNII domain

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Cellular uptake of collagens and implications for immune cell regulation in disease

    Research output: Contribution to journalReviewResearchpeer-review

  4. TAFI deficiency causes maladaptive vascular remodeling after hemophilic joint bleeding

    Research output: Contribution to journalJournal articleResearchpeer-review

  5. CCL2/MCP-1 signaling drives extracellular matrix turnover by diverse macrophage subsets

    Research output: Contribution to journalJournal articleResearchpeer-review

View graph of relations

The surface receptor for urokinase plasminogen activator (uPAR) has been recognized in recent years as a key molecule in regulating plasminogen mediated extracellular proteolysis. Surface plasminogen activation controls the connections between cells, basement membrane and extracellular matrix, and therefore the capacity of cells to migrate and invade neighboring tissues. We have isolated a 1.4 kb cDNA clone coding for the entire human uPAR. An oligonucleotide synthesized on the basis of the N-terminal sequence of the purified protein was used to screen a cDNA library made from SV40 transformed human fibroblasts [Okayama and Berg (1983) Mol. Cell Biol., 3, 280-289]. The cDNA encodes a protein of 313 amino acids, preceded by a 21 residue signal peptide. A hydrophobicity plot suggests the presence of a membrane spanning domain close to the C-terminus. The cDNA hybridizes to a 1.4 kb mRNA from human cells, a size very close to that of the cloned cDNA. Expression of the uPAR cDNA in mouse cells confirms that the clone is complete and expresses a functional uPA binding protein, located on the cell surface and with properties similar to the human uPAR. Caseinolytic plaque assay, immunofluorescence analysis, direct binding studies and cross-linking experiments show that the transfected mouse LB6 cells specifically bind human uPA, which in turn activates plasminogen. The Mr of the mature human receptor expressed in mouse cells is approximately 55,000, in accordance with the naturally occurring, highly glycosylated human uPAR. The Mr calculated on the basis of the cDNA sequence, approximately 35,000, agrees well with that of the deglycosylated receptor.

Original languageEnglish
JournalE M B O Journal
Volume9
Issue number2
Pages (from-to)467-74
Number of pages8
ISSN0261-4189
Publication statusPublished - Feb 1990

    Research areas

  • Amino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Cloning, Molecular, Enzyme Precursors, Fluorescent Antibody Technique, Gene Expression, Gene Library, Humans, Kinetics, L Cells (Cell Line), Mice, Molecular Sequence Data, Oligonucleotide Probes, Plasminogen Activators, RNA, Receptors, Cell Surface, Receptors, Urokinase Plasminogen Activator, Transfection

ID: 46434371