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Gene Review

F2  -  coagulation factor II

Rattus norvegicus

Synonyms: Coagulation factor II, Prothrombin
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High impact information on F2

  • To clarify the role of MAP kinase activation in insulin action, we compared the activation of the enzyme in Rat-1 cells transfected with wild-type (Hirc) and mutant insulin receptors in which the 2 carboxyl-terminal tyrosines were substituted with phenylalanine (Y/F2) [1].
  • Warfarin appears to induce the factor X precursor-specific but not the prothrombin precursor-specific binding proteins, which suggests a new mechanism for the action of warfarin [2].
  • Rat liver microsomes contain a vitamin K-dependent carboxylase activity that converts specific glutamyl residues of microsomal prothrombin precursor to gamma-carboxyglutamic acid residues [3].
  • In the present study we have monitored the intracellular prothrombin precursor in the secretory pathway of liver cells to determine the effect that the propeptide has on Ca(2+)-dependent folding of the protein [4].
  • It is also shown that the prothrombin precursor acquires negative charges in the Golgi apparatus that do not result from addition of sugars in late processing [5].

Biological context of F2


Anatomical context of F2

  • The distribution of vitamin K epoxidase activity in rough and smooth microsomes has been studied and compared to the prothrombin precursor and vitamin K-dependent carboxylase activity [7].

Associations of F2 with chemical compounds


  1. Mutation of the two carboxyl-terminal tyrosines in the insulin receptor results in enhanced activation of mitogen-activated protein kinase. Pang, L., Milarski, K.L., Ohmichi, M., Takata, Y., Olefsky, J.M., Saltiel, A.R. J. Biol. Chem. (1994) [Pubmed]
  2. Early processing of prothrombin and factor X by the vitamin K-dependent carboxylase. Wallin, R., Martin, L.F. J. Biol. Chem. (1988) [Pubmed]
  3. Vitamin K-dependent carboxylase. Development of a peptide substrate. Suttie, J.W., Hageman, J.M. J. Biol. Chem. (1976) [Pubmed]
  4. Intracellular maturation of the gamma-carboxyglutamic acid (Gla) region in prothrombin coincides with release of the propeptide. Wallin, R., Stanton, C., Hutson, S.M. Biochem. J. (1993) [Pubmed]
  5. Processing of prothrombin in the secretory pathway. Stanton, C., Taylor, R., Wallin, R. Biochem. J. (1991) [Pubmed]
  6. Effect of dienogest on bleeding time, coagulation, fibrinolysis, and platelet aggregation in female rats. Nobukata, H., Katsuki, Y., Ishikawa, T., Inokuma, M., Shibutani, Y. Toxicol. Lett. (1999) [Pubmed]
  7. Vitamin K epoxidase activity of rough and smooth microsomes from rat liver. Egeberg, K., Helgeland, L. Biochim. Biophys. Acta (1980) [Pubmed]
  8. Vertical profile of dioxin-like and estrogenic potencies in a sediment core from Tokyo Bay, Japan. Kannan, K., Yamashita, N., Villeneuve, D.L., Hashimoto, S., Miyazaki, A., Giesy, J.P. Cent. Eur. J. Public Health (2000) [Pubmed]
  9. Synthesis of peptide analogues of prothrombin precursor sequence 5-9. Substrate specificity of vitamin K dependent carboxylase. Rich, D.H., Lehrman, S.R., Kawai, M., Goodman, H.L., Suttie, J.W. J. Med. Chem. (1981) [Pubmed]
  10. Vitamin K-dependent carboxylase: effect of endogenous microsomal protein precursors on the rate of exogenous substrate carboxylation. Shah, D.V., Suttie, J.W. Proc. Soc. Exp. Biol. Med. (1983) [Pubmed]
  11. Effect of sodium tauroursodeoxycholate (UR-906) on liver dysfunction in bile duct-ligated rats. Ishizaki, K., Kinbara, S., Miyazawa, N., Takeuchi, Y., Hirabayashi, N., Kasai, H., Araki, T. Eur. J. Pharmacol. (1997) [Pubmed]
  12. Instrumental and bioanalytical measures of persistent organochlorines in blue mussel (Mytilus edulis) from Korean coastal waters. Khim, J.S., Villeneuve, D.L., Kannan, K., Hu, W.Y., Giesy, J.P., Kang, S.G., Song, K.J., Koh, C.H. Arch. Environ. Contam. Toxicol. (2000) [Pubmed]
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