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Murine lymphoid procoagulant activity induced by bacterial lipopolysaccharide and immune-complexes is a monocyte prothrombinase

Academic Article
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Overview

authors

  • Schwartz, B. S.
  • Levy, G. A.
  • Fair, D. S.
  • Edgington, Thomas

publication date

  • 1982

journal

  • Journal of Experimental Medicine  Journal

abstract

  • Murine lymphoid cells respond rapidly to bacterial lipopolysaccharide or antigen-antibody complexes to initiate or accelerate the blood coagulation pathways. The monocyte or macrophage has been identified as the cellular source, although lymphocyte collaboration is required for the rapid induction of the procoagulant response. This procoagulant activity is identified in the present study as a direct prothrombin activator, i.e., a prothrombinase. Studies with plasmas deficient in single coagulation factors demonstrate that the induced murine procoagulant activity effector molecule does not require factors XII, VIII, VII, X, or V, but does require prothrombin to transform fibrinogen to fibrin. This enzyme(s) produces limited proteolysis of prothrombin to yield thrombin or thrombinlike products that are functionally capable of converting fibrinogen to fibrin. The prothrombinase is undetectable in freshly isolated Murine lymphoid cells respond rapidly to bacterial lipopolysaccharide or antigen-antibody complexes to initiate or accelerate the blood coagulation pathways. The monocyte or macrophage has been identified as the cellular source, although lymphocyte collaboration is required for the rapid induction of the procoagulant response. This procoagulant activity is identified in the present study as a direct prothrombin activator, i.e., a prothrombinase. Studies with plasmas deficient in single coagulation factors demonstrate that the induced murine procoagulant activity effector molecule does not require factors XII, VIII, VII, X, or V, but does require prothrombin to transform fibrinogen to fibrin. This enzyme(s) produces limited proteolysis of prothrombin to yield thrombin or thrombinlike products that are functionally capable of converting fibrinogen to fibrin. The prothrombinase is undetectable in freshly isolated

subject areas

  • Animals
  • Antigen-Antibody Complex
  • Blood Coagulation
  • Blood Coagulation Factors
  • Calcium
  • Enzyme Precursors
  • Humans
  • Lipopolysaccharides
  • Male
  • Membrane Proteins
  • Mice
  • Mice, Inbred C3H
  • Monocytes
  • Plasminogen Activators
  • Prothrombin
  • Thromboplastin
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Identity

International Standard Serial Number (ISSN)

  • 0022-1007

Digital Object Identifier (DOI)

  • 10.1084/jem.155.5.1464

PubMed ID

  • 7200121
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Additional Document Info

start page

  • 1464

end page

  • 1479

volume

  • 155

issue

  • 5

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