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Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells

Academic Article
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Overview

authors

  • Miles, Lindsey
  • Plow, E. F.

publication date

  • October 1987

journal

  • Thrombosis and Haemostasis  Journal

abstract

  • Glu-plasminogen binds to platelets; the monocytoid line, U937, and the human fetal fibroblast line, GM1380 bind both plasminogen and its activator, urokinase. This study assesses the interaction of these fibrinolytic proteins with circulating human blood cells. Plasminogen bound minimally to red cells but bound saturably and reversibly to monocytes, granulocytes and lymphocytes with apparent Kd values of 0.9-1.4 microM. The interactions were of high capacity with 1.6 to 49 X 10(5) sites/cell and involved the lysine binding sites of plasminogen. Both T cells and non-rosetting lymphocytes and two B cell lines saturably bound plasminogen. Urokinase bound saturably to granulocytes, monocytes, non-rosetting lymphocytes and a B cell line, but minimally to T cells, platelets and red cells. Therefore, plasminogen binding sites of high capacity, of similar affinities, and with common recognition specificities are expressed by many peripheral blood cells. Urokinase receptors are also widely distributed, but less so than plasminogen binding sites. The binding of plasminogen and/or urokinase to these cells may lead to generation of cell-associated proteolytic activity which contributes to a variety of cellular functions.

subject areas

  • Blood Cells
  • Cell Membrane
  • Erythrocytes
  • Fibrinolysis
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Leukocytes
  • Plasminogen
  • Receptors, Cell Surface
  • Receptors, Urokinase Plasminogen Activator
  • Urokinase-Type Plasminogen Activator
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Identity

International Standard Serial Number (ISSN)

  • 0340-6245

PubMed ID

  • 2829380
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Additional Document Info

start page

  • 936

end page

  • 942

volume

  • 58

issue

  • 3

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