Skip to main content
NCBI home page
British Journal of Experimental Pathology logoLink to British Journal of Experimental Pathology
. 1984 Dec;65(6):691–700.

Synthesis and turnover of prothrombin during experimental inflammation in rats.

A Koj, E Regoeczi, P A Chindemi, J Gauldie
PMCID: PMC2041002  PMID: 6208926

Abstract

The response of prothrombin to inflammatory reactions was investigated in rats. Inflammation was induced by the administration of either subcutaneous turpentine or intraperitoneal endotoxin, and its effects were studied 24 h and 48 h later. Albumin and alpha 1-acute-phase globulin served as the controls. There were only insignificant changes in plasma prothrombin concentration during inflammation which contrasts sharply with a decrease in circulating albumin by approximately 25% and an increase in alpha 1-acute-phase globulin by 300-400%. These changes were paralleled by similar changes in the incorporation of [3H]lysine into these proteins during the incubation of liver slices from rats that had been pretreated with the phlogistic agents. Prothrombin catabolism, studied using 131I-prothrombin, was increased by approximately 20%; albumin turnover, studied simultaneously with 125I-albumin, was not significantly affected, though the capillary transfer rate of albumin was significantly elevated 48 h after the induction of inflammation. It is concluded that rat prothrombin is not an acute-phase protein.

Full text

PDF
691

Images in this article

695Fig. 1
on p.695

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Edwards K., Fleischer B., Dryburgh H., Fleischer S., Schreiber G. The distribution of albumin precursor protein and albumin in liver. Biochem Biophys Res Commun. 1976 Sep 7;72(1):310–318. doi: 10.1016/0006-291x(76)90995-5. [DOI] [PubMed] [Google Scholar]
  2. Grant G. A., Suttie J. W. Rat prothrombin: purification, characterization, and activation. Arch Biochem Biophys. 1976 Oct;176(2):650–662. doi: 10.1016/0003-9861(76)90209-5. [DOI] [PubMed] [Google Scholar]
  3. Kaplan A. P., Silverberg M., Dunn J. T., Ghebrehiwet B. Interaction of the clotting, kinin-forming, complement, and fibrinolytic pathways in inflammation. Ann N Y Acad Sci. 1982;389:25–38. doi: 10.1111/j.1749-6632.1982.tb22123.x. [DOI] [PubMed] [Google Scholar]
  4. Kasperczyk H., Koj A. Ethionine-dependent inhibition of acute-phase plasma protein synthesis in the rat. Br J Exp Pathol. 1983 Jun;64(3):277–285. [PMC free article] [PubMed] [Google Scholar]
  5. Koj A. Comparison of synthesis and secretion of plasma albumin, fibrinogen and alpha 2-macroglobulin by slices of Morris hepatomas and rat liver. Br J Exp Pathol. 1980 Jun;61(3):332–338. [PMC free article] [PubMed] [Google Scholar]
  6. Koj A., Dubin A., Kasperczyk H., Bereta J., Gordon A. H. Changes in the blood level and affinity to concanavalin A of rat plasma glycoproteins during acute inflammation and hepatoma growth. Biochem J. 1982 Sep 15;206(3):545–553. doi: 10.1042/bj2060545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Koj A., Regoeczi E. Effect of experimental inflammation on the synthesis and distribution of antithrombin III and alpha1-antitrypsin in rabbits. Br J Exp Pathol. 1978 Oct;59(5):473–481. [PMC free article] [PubMed] [Google Scholar]
  8. McDuffie F. C., Giffin C., Niedringhaus R., Mann K. G., Owen C. A., Jr, Bowie E. J., Peterson J., Clark G., Hunder G. G. Prothrombin, thrombin and prothrombin fragments in plasma of normal individuals and of patients with laboratory evidence of disseminated intravascular coagulation. Thromb Res. 1979;16(5-6):759–773. doi: 10.1016/0049-3848(79)90219-6. [DOI] [PubMed] [Google Scholar]
  9. Miletich J. P., Broze G. J., Jr, Majerus P. W. The synthesis of sulfated dextran beads for isolation of human plasma coagulation factors II, IX, and X. Anal Biochem. 1980 Jul 1;105(2):304–310. doi: 10.1016/0003-2697(80)90462-5. [DOI] [PubMed] [Google Scholar]
  10. Murtiashaw M. H., Baynes J. W., Thorpe S. R. Albumin catabolism in diabetic rats. Arch Biochem Biophys. 1983 Aug;225(1):256–262. doi: 10.1016/0003-9861(83)90028-0. [DOI] [PubMed] [Google Scholar]
  11. Olson J. P., Miller L. L., Troup S. B. Synthesis of clotting factors by the isolated perfused rat liver. J Clin Invest. 1966 May;45(5):690–701. doi: 10.1172/JCI105384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Owen C. A., Jr, Mann K. G., McDuffie F. C. The turnover in normal dogs of prothrombin and its fragments; effect of induced intravascular coagulation. Thromb Haemost. 1979 Aug 31;42(2):548–555. [PubMed] [Google Scholar]
  13. Regoeczi E. Iodogen-catalyzed iodination of transferrin. Int J Pept Protein Res. 1983 Oct;22(4):422–433. doi: 10.1111/j.1399-3011.1983.tb02111.x. [DOI] [PubMed] [Google Scholar]
  14. Regoeczi E., Taylor P., Hatton M. W., Wong K. L., Koj A. Distinction between binding and endocytosis of human asialo-transferrin by the rat liver. Biochem J. 1978 Jul 15;174(1):171–178. doi: 10.1042/bj1740171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sellers A. L., Katz J., Bonorris G., Okuyama S. Determination of extravascular albumin in the rat. J Lab Clin Med. 1966 Aug;68(2):177–185. [PubMed] [Google Scholar]
  16. Shah D. V., Suttie J. W., Grant G. A. A rat liver protein with potential thrombin activity: properties and partial purification. Arch Biochem Biophys. 1973 Nov;159(1):483–491. doi: 10.1016/0003-9861(73)90478-5. [DOI] [PubMed] [Google Scholar]
  17. Takeda Y. Studies of the metabolism and distribution of prothrombin in healthy men with homologous 125 I-prothrombin. Thromb Diath Haemorrh. 1972 Jul 31;27(3):472–489. [PubMed] [Google Scholar]
  18. van Oosterom A. T., Mattie H., Hermens W. T., Veltkamp J. J. The influence of the thyroid function on the metabolic rate of prothrombin, factor VII, and factor X in the rat. Thromb Haemost. 1976 Jun 30;35(3):607–619. [PubMed] [Google Scholar]

Articles from British journal of experimental pathology are provided here courtesy of Wiley

RESOURCES