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细菌脂多糖和免疫复合物诱导的小鼠淋巴样促凝活性是一种单核细胞凝血酶原酶。

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

作者信息

Schwartz B S, Levy G A, Fair D S, Edgington T S

出版信息

J Exp Med. 1982 May 1;155(5):1464-79. doi: 10.1084/jem.155.5.1464.

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

摘要

小鼠淋巴细胞对细菌脂多糖或抗原 - 抗体复合物反应迅速,可启动或加速血液凝固途径。单核细胞或巨噬细胞已被确定为细胞来源,尽管促凝反应的快速诱导需要淋巴细胞协作。在本研究中,这种促凝活性被确定为一种直接的凝血酶原激活剂,即凝血酶原酶。对缺乏单一凝血因子的血浆进行的研究表明,诱导的小鼠促凝活性效应分子不需要因子 XII、VIII、VII、X 或 V,但确实需要凝血酶原将纤维蛋白原转化为纤维蛋白。这种酶对凝血酶原进行有限的蛋白水解,产生凝血酶或类似凝血酶的产物,这些产物在功能上能够将纤维蛋白原转化为纤维蛋白。在新鲜分离的细胞中检测不到凝血酶原酶。小鼠淋巴细胞对细菌脂多糖或抗原 - 抗体复合物反应迅速,可启动或加速血液凝固途径。单核细胞或巨噬细胞已被确定为细胞来源,尽管促凝反应的快速诱导需要淋巴细胞协作。在本研究中,这种促凝活性被确定为一种直接的凝血酶原激活剂,即凝血酶原酶。对缺乏单一凝血因子的血浆进行的研究表明,诱导的小鼠促凝活性效应分子不需要因子 XII、VIII、VII、X 或 V,但确实需要凝血酶原将纤维蛋白原转化为纤维蛋白。这种酶对凝血酶原进行有限的蛋白水解,产生凝血酶或类似凝血酶的产物,这些产物在功能上能够将纤维蛋白原转化为纤维蛋白。在新鲜分离的细胞中检测不到凝血酶原酶。

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