Induction of prothrombin synthesis by prothrombin fragments.
- 1 August 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (8) , 4772-4776
- https://doi.org/10.1073/pnas.78.8.4772
Abstract
The mechanisms by which blood levels of prothrombin (PT) are regulated in the vitamin K-sufficient state are unknown. PT synthesis by Reuber H-35 rat hepatoma cells exposed to vitamin K and [3H]leucine in serum-free cultures was studied. 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. PT synthesis might be regulated physiologically by the products formed during its normal turnover and consumption during blood coagulation.This publication has 19 references indexed in Scilit:
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