The metabolic functions and mechanism of action of vitamin K

References

• Dam H. Cholesterinstoffwechsel in Hühnereiern und Hühnchen. Biochem Z 1929; 215: 475–92
   Google Scholar
• MacCorquodale D. W., Cheney L. C., Binkley S. B., Holcomb W. F., McKee R. W., Thayer S. A., Doisy E. A. The constitution and synthesis of vitamin K2. J Biol Chem 1939; 131: 357–70
   Google Scholar
• Suttie J. W. Vitamin K. The Fat-Soluble Vitamins, A. T. Diplock. William Heinemann Ltd, London 1985; 225–311
   Google Scholar
• Sakano T., Nagaoka T., Morimoto A., Hirauchi K. Measurement of K vitamins in human and animal feces by HPLC with fluorometric detection. Chem Pharm Bull 1986; 34: 4322–6
   PubMed Web of Science ®Google Scholar
• Olson R. E. The function and metabolism of vitamin K. Ann Rev Nutr 1984; 4: 281–337
   PubMed Web of Science ®Google Scholar
• Campbell H. A., Link K. P. Studies on the hemorrhagic sweet clover disease IV. The isolation and crystallization of the hemorrhagic agent. J Biol Chem 1941; 138: 21–33
   Google Scholar
• Ganrot P. O., Niléhn J-E. Plasma prothrombin during treatment with dicumarol. II. Demonstration of an abnormal prothrombin fraction. Scand J Clin Lab Invest 1968; 22: 23–8
   PubMed Web of Science ®Google Scholar
• Stenflo J., Fernlund P., Egan W., Roepstorff P. Vitamin K-dependent modifications of glutamic acid residues in prothrombin. Proc Natl Acad Sci USA 1974; 71: 2730–3
   PubMed Web of Science ®Google Scholar
• Nelsestuen G. L., Zytkovicz T. H., Howard J. B. The mode of action of vitamin K. Identification of γ-carboxyglutamic acid as a component of prothrombin. J Biol Chem 1974; 249: 6347–50
   PubMed Web of Science ®Google Scholar
• Jackson C. M., Nemerson Y. Blood coagulation. Ann Rev Biochem 1980; 49: 765–811
   PubMed Web of Science ®Google Scholar
• Furie B., Furie B. C. The molecular basis of blood coagulation. Cell 1988; 53: 505–18
   PubMed Web of Science ®Google Scholar
• Strickland D. K., Kessler C. M. Biochemical and functional properties of protein C and protein S. Clin Chim Acta 1987; 170: 1–24
   PubMed Web of Science ®Google Scholar
• Højrup P., Jensen M. S., Petersen T. E. Amino acid sequence of bovine protein Z: a vitamin K-dependent serine protease homolog. FEBS Lett 1985; 184: 333–8
   PubMed Web of Science ®Google Scholar
• Price P. A. Vitamin K-dependent formation of bone Gla protein (osteocalcin) and its function. Vitamins and Hormones Vol 42, D. B. McCormick. Academic Press, Orlando 1985; 65–108
   Google Scholar
• Lian J. B. Osteocalcin: Functional studies and postulated role in bone resorption. Current Advances in Vitamin K Research, J. W. Suttie. Elsevier Science Publishing Co, New York 1988; 245–57
   Google Scholar
• Price P. A. Bone Gla protein and matrix Gla protein: Identification of the probable structures involved in substrate recognition by the γ-carboxylase and discovery of tissue differences in vitamin K metabolism. Current Advances in Vitamin K Research, J. W. Suttie. Elsevier Science Publishing Co, New York 1988; 259–73
   Google Scholar
• Levy R. J., Howard S. L., Oshry L. J. Carboxyglutamic acid (Gla) containing proteins of human calcified atherosclerotic plaque solubilized by EDTA. Atherosclerosis 1986; 59: 155–60
   PubMed Web of Science ®Google Scholar
• van Haarlem L. JM, Soute B. AM, Hemker H. C., Vermeer C. Characterization of Gla-containing proteins from calcified human atherosclerotic plaques. Current Advances in Vitamin K Research, J. W. Suttie. Elsevier Science Publishing Co, New York 1988; 287–92
   Google Scholar
• Nakagawa Y., Abram V., Parks J. H., Lau H. S-H, Kawooya J. K., Coe F. L. Urine glycoprotein crystal growth inhibitors. Evidence for a molecular abnormality in calcium oxalate nephrolithiasis. J Clin Invest 1985; 76: 1455–62
   PubMed Web of Science ®Google Scholar
• Nakagawa Y., Ahmed M. A., Hall S. L., Deganello S., Coe F. L. Isolation from human calcium oxalate renal stones of nephrocalcin, a glycoprotein inhibitor of calcium oxalate crystal growth. Evidence that nephrocalcin from patients with calcium oxalate nephrolithiasis is deficient in γ-carboxyglutamic acid. J Clin Invest 1987; 79: 1782–7
   PubMed Web of Science ®Google Scholar
• Soute B. AM, Müller-Esterl W., de Boer-van den Berg M. AG, Ulrich M., Vermeer C. Discovery of a γ-carboxyglutamic acid-containing protein in human spermatozoa. FEBS Lett 1985; 190: 137–41
   PubMed Web of Science ®Google Scholar
• Rannels S. R., Gallaher K. J., Wallin R., Rannels D. E. Vitamin K-dependent carboxylation of pulmonary surfactant-associated proteins. Proc Natl Acad Sci USA 1987; 84: 5952–6
   PubMed Web of Science ®Google Scholar
• Vitamin K metabolism and vitamin K-dependent proteins, J. W. Suttie. University Park Press, Baltimore 1981; 592
   Google Scholar
• McIntosh J. M., Olivera B. M., Cruz L. J., Gray W. R. γ-Carboxyglutamate in a neuroactive toxin. J Biol Chem 1984; 259: 14343–6
   PubMed Web of Science ®Google Scholar
• Esmon C. T., Sadowski J. A., Suttie J. W. A new carboxylation reaction. The vitamin K-dependent incorporation of H14CO3 into prothrombin. J Biol Chem 1975; 250: 4744–8
   PubMed Web of Science ®Google Scholar
• Matschiner J. T., Bell R. G., Amelotti J. M., Knauer J. T. Isolation and characterization of a new metabolite of phylloquinone in the rat. Biochim Biophys Acta 1970; 201: 309–15
   PubMed Web of Science ®Google Scholar
• Zimmerman A., Matschiner J. T. Biochemical basis of hereditary resistance to warfarin in the rat. Biochem Pharmacol 1974; 23: 1033–40
   PubMed Web of Science ®Google Scholar
• Suttie J. W. Vitamin K-dependent carboxylase. Ann Rev Biochem 1985; 54: 459–77
   PubMed Web of Science ®Google Scholar
• van Haarlem L. JM, Ulrich M. MW, Hemker H. C., Soute B. AM, Vermeer C. Isolation and partial characterization of vitamin K-dependent carboxylase from bovine aortae. Biochem J 1987; 245: 251–5
   PubMed Web of Science ®Google Scholar
• de Boer-van den Berg M. AG, Verstijnen C. PHJ, Vermeer C. Vitamin K-dependent carboxylase in skin. J Invest Dermatol 1986; 87: 377–80
   PubMed Web of Science ®Google Scholar
• Uotila L., Suttie J. W. Characterization of vitamin K-dependent carboxylase from the livers of the adult ox and dicoumarol-treated calf. Biochem J 1982; 201: 249–58
   PubMed Web of Science ®Google Scholar
• Suttie J. W., Hageman J. M., Lehrman S. R., Rich D. H. Vitamin K-dependent carboxylase: development of a peptide substrate. J Biol Chem 1976; 251: 5827–30
   PubMed Web of Science ®Google Scholar
• Ulrich M. W., Furie B., Jacobs M. R., Vermeer C., Furie B. C. Vitamin K-dependent carboxylation. A synthetic peptide based upon the γ-carboxylation recognition site sequence of the prothrombin propeptide is an active substrate for the carboxylase in vitro. J Biol Chem 1988; 263: 9697–702
   PubMed Web of Science ®Google Scholar
• Hubbard B. R., Jacobs M., Ulrich M. MW, Walsh C., Furie B., Furie B. C. Vitamin K-dependent carboxylation. In vivo modification of synthetic peptides containing the γ-carboxylation recognition site. J Biol Chem 1989; 264: 14145–50
   PubMed Web of Science ®Google Scholar
• Uotila L. Vitamin K-dependent carboxylase from calf liver: studies on the steady-state kinetic mechanism. Arch Biochem Biophys 1988; 264: 135–43
   PubMed Web of Science ®Google Scholar
• McTigue J. J., Suttie J. W. Oxygen dependence of vitamin K-dependent carboxylase and vitamin K epoxidase. FEBS Lett 1986; 200: 71–5
   PubMed Web of Science ®Google Scholar
• Jones J. P., Gardner E. J., Cooper T. G., Olson R. E. Vitamin K-dependent carboxylation of peptide-bound glutamate. The active species of “CO2” utilized by the membrane-bound preprothrombin carboxylase. J Biol Chem 1977; 252: 7738–42
   PubMed Web of Science ®Google Scholar
• Uotila L. Inhibition of vitamin K-dependent carboxylase by vitamin E and its derivatives. Current Advances in Vitamin K Research, J. W. Suttie. Elsevier Science Publishing Co, New York 1988; 59–64
   Google Scholar
• Guibé E., Decottignies-Le Maréchal P., Le Maréchal P., Azerad R. Vitamin K-dependent carboxylation: inhibition by a peptide containing 4-methylene glutamic acid. FEBS Lett 1984; 177: 265–8
   PubMed Web of Science ®Google Scholar
• De Metz M., Vermeer C., Soute B. AM, van Scharrenburg G. JM, Slotboom A. J., Hemker H. C. Partial purification of bovine liver vitamin K-dependent carboxylase by immunospecific adsorption onto antifactor X. FEBS Lett 1981; 123: 215–8
   PubMed Web of Science ®Google Scholar
• Friedman P. A., Shia M. A., Gallop P. M., Griep A. E. Vitamin K-dependent γ-carbon-hydrogen bond cleavage and nonmandatory concurrent carboxylation of peptide-bound glutamic acid residues. Proc Natl Acad Sci USA 1979; 76: 3126–9
   PubMed Web of Science ®Google Scholar
• Cheung A. Y., Wood G. M., Funakawa S., Grossman C. P., Suttie J. W. Vitamin K-dependent carboxylase: substrates, products and inhibitors. Current Advances in Vitamin K Research, J. W. Suttie. Elsevier Science Publishing Co, New York 1988; 3–16
   Google Scholar
• Wood G., Suttie J. W. Vitamin K-dependent carboxylase. Stoichiometry of vitamin K epoxide formation, γ-carboxyglutamyl formation, and γ-glutamyl-3H cleavage. J Biol Chem 1988; 263: 3234–9
   PubMed Web of Science ®Google Scholar
• Hildebrandt E. F., Preusch P. C., Patterson J. L., Suttie J. W. Solubilization and characterization of vitamin K epoxide reductase from normal and warfarinresistant rat microsomes. Arch Biochem Biophys 1984; 228: 480–92
   PubMed Web of Science ®Google Scholar
• Hazelett S. E., Preusch P. C. Tissue distribution and warfarin sensitivity of vitamin K epoxide reductase. Biochem Pharmacol 1988; 37: 929–34
   PubMed Web of Science ®Google Scholar
• van Haarlem L. JM, Soute B. AM, Vermeer C. Vitamin K-dependent carboxylase. Possible role of thioredoxin in the reduction of vitamin K metabolites in liver. FEBS Lett 1987; 222: 353–7
   PubMed Web of Science ®Google Scholar
• Silverman R. B., Nandi D. L. Reduced thioredoxin: a possible physiological cofactor for vitamin K epoxide reductase. Further support for an active site disulfide. Biochem Biophys Res Commun 1988; 155: 1248–54
   PubMed Web of Science ®Google Scholar
• Fasco M. J., Principe L. M. R and S-Warfarin inhibition of vitamin K and vitamin K 2,3-epoxide reductase activities in the rat. J Biol Chem 1982; 257: 4894–901
   PubMed Web of Science ®Google Scholar
• Fasco M. J., Principe L. M., Walsh W. A., Friedman P. A. Warfarin inhibition of vitamin K 2,3-epoxide reductase in rat liver microsomes. Biochemistry 1983; 22: 5655–60
   PubMed Web of Science ®Google Scholar
• Wallin R. Vitamin K antagonism of coumarin anticoagulation. A dehydrogenase pathway in rat liver is responsible for the antagonistic effect. Biochem J 1986; 236: 685–93
   PubMed Web of Science ®Google Scholar