凝血酶原片段对凝血酶原合成的诱导作用。
Induction of prothrombin synthesis by prothrombin fragments.
作者信息
Graves C B, Munns T W, Carlisle T L, Grant G A, Strauss A W
出版信息
Proc Natl Acad Sci U S A. 1981 Aug;78(8):4772-6. doi: 10.1073/pnas.78.8.4772.
The mechanisms by which blood levels of prothrombin (PT) are regulated in the vitamin K-sufficient state are unknown. We have studied PT synthesis by Reuber H-35 rat hepatoma cells exposed to vitamin K and [3H]leucine in serum-free cultures. Administration to the culture system of exogenous bovine PT and rat PT was characterized by increases in endogenous PT synthesis and secretion of 2- and 3-fold, respectively. This induction required endogenous proteolytic degradation of PT. Studies conducted with bovine PT fragment 1 (residues 1-156) demonstrated up to 5-fold increases in PT synthesis. This induction was dose dependent and saturable. Addition of bovine PT chymotryptic fragments to the cells indicated that the NH2-terminal peptide of prothrombin (residues 1-42) contained the requisite structural elements for the induction. Peptide-bound gamma-carboxyglutamate residues were required for the observed stimulation of PT synthesis. These results suggest that PT synthesis might be regulated physiologically by the products formed during its normal turnover and consumption during blood coagulation.
在维生素K充足状态下，凝血酶原（PT）血液水平的调节机制尚不清楚。我们研究了在无血清培养中，暴露于维生素K和[3H]亮氨酸的鲁伯H-35大鼠肝癌细胞的PT合成。向培养系统中添加外源性牛PT和大鼠PT的特征分别是内源性PT合成增加2倍和分泌增加3倍。这种诱导需要PT的内源性蛋白水解降解。用牛PT片段1（第1-156位氨基酸残基）进行的研究表明PT合成增加了5倍。这种诱导是剂量依赖性的且具有饱和性。向细胞中添加牛PT胰凝乳蛋白酶片段表明，凝血酶原的NH2末端肽（第1-42位氨基酸残基）包含诱导所需的结构元件。观察到的PT合成刺激需要肽结合的γ-羧基谷氨酸残基。这些结果表明，PT合成可能在生理上受其在血液凝固过程中正常周转和消耗期间形成的产物调节。
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