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

• Danazol increased the fibrinogen level, coagulation factor II, V, VII, VIII, IX, X, XI, and XII activities, and antithrombin III activity, but had no influence on the platelet aggregation at repeated doses of 10 and 100 mg/kg per day for 4 weeks [6].
• The drug increased the fibrinogen level, coagulation factor II and V activities, and antithrombin III activity, but had no effect on fibrinolysis or on platelet aggregation at repeated doses of 1 and 10 mg/kg per day for 4 weeks [6].

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

• PAH concentrations were correlated with dioxin-like activities measured in F2 [8].
• Synthesis of peptide analogues of prothrombin precursor sequence 5-9. Substrate specificity of vitamin K dependent carboxylase [9].
• Rat liver microsomes contain a Triton X-100 solubilizable vitamin K-dependent carboxylase activity that converts specific glutamyl residues of a microsomal prothrombin precursor to gamma-carboxyglutamyl residues [10].
• Furthermore, UR-906 significantly suppressed the decreases in plasma coagulation factor II and X activities [11].
• Fraction 2 (F-2), which contained hexachlorocyclohexanes, chlordanes, p,p'-DDD, and p,p'-DDT, generally elicited significant dioxin-like activity compared to control, whereas Fraction 1 (F-1), which contained PCBs, p,p'-DDE, and hexachlorobenzene, did not [12].

References