Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments.

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Rat factor X is synthesized as a single chain precursor inducible by prothrombin fragments.

Factor X in plasma is a gamma-carboxylated two-chain glycoprotein which, in activated form, plays a pivotal role in blood coagulation. We have utilized purified rat Factor X antibody, coupled to Sepharose, to isolate and characterize Factor X in rat liver, plasma, and hepatoma cells. Rat factor X is synthesized as a single chain precursor (Mr = 63,000). It is this form which undergoes vitamin K...

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Induction of prothrombin synthesis by prothrombin fragments.

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-...

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Human hepatoma cells secrete single chain factor X, prothrombin, and antithrombin III.

The human hepatoma cell line, Hep G2, was analyzed for the ability to synthesize and secrete several coagulation proteins. Using specific radioimmunoassays, factor X, prothrombin, and antithrombin III were present in 8-day culture supernatants at 62, 405, and 1,220 ng/mL, respectively. Factor IX was not detected, either in supernatants or in cell extracts. Intrinsically labeled factor X was sec...

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Lyt-2 glycoprotein is synthesized as a single molecular species

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The activation of factor X and prothrombin by recombinant factor VIIa in vivo is mediated by tissue factor.

The human coagulation system continuously generates very small quantities of Factor Xa and thrombin. Current evidence suggests that basal level activation of the hemostatic mechanism occurs via Factor VIIa-dependent activation of Factor X, but direct proof has not been available for the participation of tissue factor in this pathway. To examine this issue, we infused relatively high concentrati...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1982

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)33629-9