The urokinase plasminogen activator receptor in blood from healthy individuals and patients with cancer

The cell surface plasminogen activation system functions in promoting tumor dissemination, and is facilitated by a glycolipid anchored three domain receptor for urokinase. This receptor can also be found in a soluble form (suPAR) in extracts of tumors, as well as in plasma from both healthy individuals and cancer patients. The suPAR in plasma consists of the intact three domain protein, but neither the precise mechanism of its release from cell surfaces, nor its biological function are understood. Increased levels of plasma suPAR have been found in patients with cancers of the lung, breast, ovary, and colon, and recent data now indicates that the level of the molecule is related to patient prognosis.

[1]  N. Brünner,et al.  The level of urokinase-type plasminogen activator receptor is increased in serum of ovarian cancer patients. , 1998, Cancer research.

[2]  K. Preissner,et al.  Vitronectin concentrates proteolytic activity on the cell surface and extracellular matrix by trapping soluble urokinase receptor-urokinase complexes. , 1998, Blood.

[3]  K. Preissner,et al.  The intact urokinase receptor is required for efficient vitronectin binding: receptor cleavage prevents ligand interaction , 1997, FEBS letters.

[4]  T. Plesner,et al.  Structure, Function and Expression on Blood and Bone Marrow Cells of the Urokinase‐Type Plasminogen Activator Receptor, uPAR , 1997, Stem cells.

[5]  H. Nielsen,et al.  ELISA determination of soluble urokinase receptor in blood from healthy donors and cancer patients. , 1997, Clinical chemistry.

[6]  M. Duffy,et al.  The urokinase‐type plasminogen activator system in cancer metastasis: A review , 1997, International journal of cancer.

[7]  F. Blasi,et al.  Recycling of the urokinase receptor upon internalization of the uPA:serpin complexes , 1997, The EMBO journal.

[8]  N. Brünner,et al.  Elevated plasma levels of urokinase plasminogen activator receptor in non-small cell lung cancer patients. , 1997, European journal of cancer.

[9]  M. Schmitt,et al.  Epitope-mapped monoclonal antibodies as tools for functional and morphological analyses of the human urokinase receptor in tumor tissue. , 1997, The American journal of pathology.

[10]  K. Preissner,et al.  The Urokinase-receptor (CD87) Is Expressed in Cells of the Megakaryoblastic Lineage , 1997, Thrombosis and Haemostasis.

[11]  N. Brünner,et al.  Plasminogen activator inhibitor type 1 in cytosolic tumor extracts predicts prognosis in low-risk breast cancer patients. , 1997, Clinical cancer research : an official journal of the American Association for Cancer Research.

[12]  D. Loskutoff,et al.  Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release? , 1996, The Journal of cell biology.

[13]  K. Ulm,et al.  Clinical relevance of urokinase plasminogen activator, its receptor, and its inhibitor in patients with renal cell carcinoma , 1996, Cancer.

[14]  M. Fernö,et al.  Urokinase plasminogen activator, a strong independent prognostic factor in breast cancer, analysed in steroid receptor cytosols with a luminometric immunoassay. , 1996, European journal of cancer.

[15]  F. Blasi,et al.  Proteolytic cleavage of the urokinase receptor substitutes for the agonist‐induced chemotactic effect. , 1996, The EMBO journal.

[16]  Y. DeClerck,et al.  Cooperation between matrix metalloproteinases and the plasminogen activator-plasmin system in tumor progression. , 1996, Enzyme & protein.

[17]  H. Allgayer,et al.  Individual development and uPA–receptor expression of disseminated tumour cells in bone marrow: A reference to early systemic disease in solid cancer , 1995, Nature Medicine.

[18]  N. Brünner,et al.  Prognostic significance of the receptor for urokinase plasminogen activator in breast cancer. , 1995, Clinical cancer research : an official journal of the American Association for Cancer Research.

[19]  M. Duffy,et al.  Urokinase plasminogen activator and urokinase plasminogen activator receptor in breast cancer , 1995, International journal of cancer.

[20]  N. Brünner,et al.  Plasminogen activator inhibitor type 1 in cancer: therapeutic and prognostic implications. , 1995, Biological chemistry Hoppe-Seyler.

[21]  N. E. Hansen,et al.  The receptor for urokinase plasminogen activator is present in plasma from healthy donors and elevated in patients with paroxysmal nocturnal haemoglobinuria , 1995, British journal of haematology.

[22]  N. Brünner,et al.  The urokinase receptor. Protein structure and role in plasminogen activation and cancer invasion , 1995 .

[23]  S. Rosenberg,et al.  Identification of the urokinase receptor as an adhesion receptor for vitronectin. , 1994, The Journal of biological chemistry.

[24]  H. Kobayashi,et al.  Impact of urokinase-type plasminogen activator and its inhibitor type 1 on prognosis in cervical cancer of the uterus. , 1994, Cancer research.

[25]  P. Dettmar,et al.  Urokinase (uPA) and PAI-1 predict survival in advanced ovarian cancer patients (FIGO III) after radical surgery and platinum-based chemotherapy. , 1994, Gynecologic oncology.

[26]  N. Brünner,et al.  A cleaved form of the receptor for urokinase‐type plasminogen activator in invasive transplanted human and murine tumors , 1994, International journal of cancer.

[27]  N. Brünner,et al.  Prognostic impact of urokinase, urokinase receptor, and type 1 plasminogen activator inhibitor in squamous and large cell lung cancer tissue. , 1994, Cancer research.

[28]  J. Foekens,et al.  Plasminogen activator inhibitor-1 and prognosis in primary breast cancer. , 1994, Journal of clinical oncology : official journal of the American Society of Clinical Oncology.

[29]  K. Ulm,et al.  Both the cytosols and detergent extracts of breast cancer tissues are suited to evaluate the prognostic impact of the urokinase-type plasminogen activator and its inhibitor, plasminogen activator inhibitor type 1. , 1994, Cancer research.

[30]  U. Weidle,et al.  Recombinant soluble urokinase receptor as a scavenger for urokinase‐type plasminogen activator (uPA) , 1994, FEBS letters.

[31]  N. Brünner,et al.  Urokinase and plasminogen activator inhibitor type 1 in pulmonary adenocarcinoma. , 1994, Cancer research.

[32]  F. Jänicke,et al.  A ligand-free, soluble urokinase receptor is present in the ascitic fluid from patients with ovarian cancer. , 1993, The Journal of clinical investigation.

[33]  A. Vaheri,et al.  Distribution and lateral mobility of the urokinase-receptor complex at the cell surface. , 1993, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[34]  N. Brünner,et al.  High levels of urokinase-type plasminogen activator and its inhibitor PAI-1 in cytosolic extracts of breast carcinomas are associated with poor prognosis. , 1993, Cancer research.

[35]  J. Foekens,et al.  Prognostic value of urokinase-type plasminogen activator in 671 primary breast cancer patients. , 1992, Cancer research.

[36]  L. Lund,et al.  Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain. , 1992, The Journal of biological chemistry.

[37]  A. Vaheri,et al.  Alpha 2-macroglobulin restricts plasminogen activation to the surface of RC2A leukemia cells. , 1991, Cell regulation.

[38]  F. Jänicke,et al.  Clinical Relevance of the Urokinase-Type and Tissue-Type Plasminogen Activators and of Their Type 1 Inhibitor in Breast Cancer , 1991, Seminars in thrombosis and hemostasis.

[39]  F. Blasi,et al.  The ligand-binding domain of the cell surface receptor for urokinase-type plasminogen activator. , 1991, The Journal of biological chemistry.

[40]  F. Blasi,et al.  Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosyl-phosphatidylinositol. , 1991, The Journal of biological chemistry.

[41]  A. Vaheri,et al.  Directed plasminogen activation at the surface of normal and malignant cells. , 1991, Advances in cancer research.

[42]  M. Cubellis,et al.  Receptor‐mediated internalization and degradation of urokinase is caused by its specific inhibitor PAI‐1. , 1990, The EMBO journal.

[43]  M. Schmitt,et al.  UROKINASE-TYPE PLASMINOGEN ACTIVATOR ANTIGEN AND EARLY RELAPSE IN BREAST CANCER , 1989, The Lancet.

[44]  O. Sigurdardottir,et al.  Stability of Plasminogen Activator Inhibitor 1 (PAI-1) , 1989, Thrombosis and Haemostasis.

[45]  A. Vaheri,et al.  Activation of pro-urokinase and plasminogen on human sarcoma cells: a proteolytic system with surface-bound reactants , 1989, The Journal of cell biology.

[46]  E. Ruoslahti,et al.  Interaction of plasminogen activator inhibitor (PAI-1) with vitronectin. , 1989, The Journal of biological chemistry.

[47]  M. Scully,et al.  Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. Potentiation by U937 monocytes. , 1989, The Journal of biological chemistry.

[48]  L. Lund,et al.  One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity. , 1988, The Journal of biological chemistry.

[49]  H. Moses,et al.  Proteolytic activation of latent transforming growth factor-beta from fibroblast-conditioned medium , 1988, The Journal of cell biology.

[50]  E. Plow,et al.  Plasminogen receptors: Ubiquitous sites for cellular regulation of fibrinolysis , 1988 .

[51]  K. Danø,et al.  Plasminogen activators, tissue degradation, and cancer. , 1985, Advances in cancer research.

[52]  K. Danø,et al.  Plasminogen activator released as inactive proenzyme from murine cells transformed by sarcoma virus. , 2005, European Journal of Biochemistry.

[53]  J. Zeuthen,et al.  Purification of zymogen to plasminogen activator from human glioblastoma cells by affinity chromatography with monoclonal antibody. , 1982, Biochemistry.

[54]  K. Alitalo,et al.  Pericellular matrix in malignant transformation. , 1982, Advances in cancer research.

[55]  L. Liotta,et al.  Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane. , 1981, Cancer research.

[56]  Z. Werb,et al.  Endogenous activation of latent collagenase by rheumatoid synovial cells. Evidence for a role of plasminogen activator. , 1977, The New England journal of medicine.

[57]  R. Johnson.  Letter: Primary non-function in cadaver kidney transplants. , 1975, Lancet.