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PMID: 7200121 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

The Journal of experimental medicine ·Vol. 155 ·No. 5 ·1982-05-01 ·Pages 1464-79

Schwartz BS, Levy GA, Fair DS, Edgington TS

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

MeSH Terms
Animals Antigen-Antibody Complex/metabolism Blood Coagulation/drug effects Blood Coagulation Factors Calcium/pharmacology Enzyme Precursors/biosynthesis Humans Lipopolysaccharides/pharmacology Male Membrane Proteins/metabolism Mice Mice, Inbred C3H Monocytes/enzymology Plasminogen Activators/metabolism Prothrombin/metabolism Thromboplastin/metabolism
Chemicals
Antigen-Antibody Complex Blood Coagulation Factors Enzyme Precursors Lipopolysaccharides Membrane Proteins Prothrombin Thromboplastin Plasminogen Activators Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schwartz B S
Levy G A
Fair D S
Edgington T S
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45 references, click to expand
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Article Info
Journal
The Journal of experimental medicine
Abbr.
J Exp Med
ISSN
0022-1007
DOI
10.1084/jem.155.5.1464
Published
1982-05-01
Pages
1464-79
Language
English
Region
United States
NLM ID
2985109R
PMCID
PMC2186684
Subset
IM
Grants
NCI NIH HHS · CA-28166 · United States
NHLBI NIH HHS · HL-07195 · United States
NHLBI NIH HHS · HL-16411 · United States
External Links
PubMed source DOI: 10.1084/jem.155.5.1464 PMC Full Text View journal details
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