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Volumn 135, Issue 2, 2005, Pages 233-238

Activities of hepatic cytosolic and mitochondrial forms of serine hydroxymethyltransferase and hepatic glycine concentration are affected by vitamin B-6 intake in rats

Author keywords

One carbon metabolism; Rat; Serine hydroxymethyltransferase; Vitamin B 6

Indexed keywords

APOENZYME; GLYCINE; GLYCINE HYDROXYMETHYLTRANSFERASE; ISOENZYME; METHYLENETETRAHYDROFOLIC ACID; PYRIDOXAL 5 PHOSPHATE; PYRIDOXINE; SERINE; TETRAHYDROFOLIC ACID;

EID: 13244252239     PISSN: 00223166     EISSN: None     Source Type: Journal    
DOI: 10.1093/jn/135.2.233     Document Type: Article
Times cited : (41)

References (47)
  • 2
    • 0025954883 scopus 로고
    • Compartmentation of folate-mediated one-carbon metabolism in eukaryotes
    • Appling, D. (1991) Compartmentation of folate-mediated one-carbon metabolism in eukaryotes. FASEB J. 5: 2645-2651.
    • (1991) FASEB J. , vol.5 , pp. 2645-2651
    • Appling, D.1
  • 3
    • 0024511031 scopus 로고
    • Interaction of folylpolyglutamates with enzymes in one-carbon metabolism
    • Schirch, V. & Strong, W. B. (1989) Interaction of folylpolyglutamates with enzymes in one-carbon metabolism. Arch. Biochem. Biophys. 269: 371-380.
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 371-380
    • Schirch, V.1    Strong, W.B.2
  • 4
    • 0032515921 scopus 로고    scopus 로고
    • Molecular cloning characterization and alternative splicing of the human cytoplasmic serine hydroxymethyltransferase gene
    • Girgis, S., Nasrallah, I. M., Suh, J. R., Oppenheim, E., Zanetti, K. A., Mastri, M. G. & Stover, P. (1998) Molecular cloning characterization and alternative splicing of the human cytoplasmic serine hydroxymethyltransferase gene. Gene 210: 315-324.
    • (1998) Gene , vol.210 , pp. 315-324
    • Girgis, S.1    Nasrallah, I.M.2    Suh, J.R.3    Oppenheim, E.4    Zanetti, K.A.5    Mastri, M.G.6    Stover, P.7
  • 5
    • 0018160479 scopus 로고
    • Interaction of pyridoxal 5′-phosphate with apo-serine hydroxymethyltransferase
    • Jones, C. & Priest, D. (1978) Interaction of pyridoxal 5′-phosphate with apo-serine hydroxymethyltransferase. Biochem. Biophys. Acta 526: 369-374.
    • (1978) Biochem. Biophys. Acta , vol.526 , pp. 369-374
    • Jones, C.1    Priest, D.2
  • 6
    • 0034015564 scopus 로고    scopus 로고
    • Vitamin B-6 deficiency in rats reduces hepatic serine hydroxymethyl-transferase and cystathionine beta-synthase activities and rate of in vivo protein turnover, homocysteine remethylation, and transsulfuration
    • Martinez, M., Cuskelly, G. J., Williamson, J., Toth, J. P. & Gregory, J. F. (2000) Vitamin B-6 deficiency in rats reduces hepatic serine hydroxymethyl-transferase and cystathionine beta-synthase activities and rate of in vivo protein turnover, homocysteine remethylation, and transsulfuration. J. Nutr. 130: 1151-1123.
    • (2000) J. Nutr. , vol.130 , pp. 1151-1123
    • Martinez, M.1    Cuskelly, G.J.2    Williamson, J.3    Toth, J.P.4    Gregory, J.F.5
  • 7
    • 0027223085 scopus 로고
    • Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization
    • Garrow, T., Brenner, A. A., Whitehead, M., Cen, X., Duncan, R., Korenberg, J. & Shane, B. (1993) Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J. Biol. Chem. 268: 11910-11916.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11910-11916
    • Garrow, T.1    Brenner, A.A.2    Whitehead, M.3    Cen, X.4    Duncan, R.5    Korenberg, J.6    Shane, B.7
  • 8
    • 0028084927 scopus 로고
    • The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and analysis of the evolutionary relationships among SHMTs
    • Usha, R., Savithri, H. S. & Rao, N. A. (1994) The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and analysis of the evolutionary relationships among SHMTs. Biochim. Biophys. Acta 1204: 75-83.
    • (1994) Biochim. Biophys. Acta , vol.1204 , pp. 75-83
    • Usha, R.1    Savithri, H.S.2    Rao, N.A.3
  • 9
    • 0026063520 scopus 로고
    • 5-Formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase
    • Stover, P. & Schirch, V. (1991) 5-Formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase. J. Biol. Chem. 266: 1543-1550.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1543-1550
    • Stover, P.1    Schirch, V.2
  • 10
    • 0030030729 scopus 로고    scopus 로고
    • Evidence for intracellular partitioning of serine and glycine metabolism in Chinese hamster ovary cells
    • Narkewicz, M., Sauls, S. D., Tjoa, S. S., Teng, C. & Fennessey, P. V. (1996) Evidence for intracellular partitioning of serine and glycine metabolism in Chinese hamster ovary cells. Biochem. J. 313: 991-996.
    • (1996) Biochem. J. , vol.313 , pp. 991-996
    • Narkewicz, M.1    Sauls, S.D.2    Tjoa, S.S.3    Teng, C.4    Fennessey, P.V.5
  • 11
    • 0030589008 scopus 로고    scopus 로고
    • Role of cytosolic serine hydrox-methyltransferase in one-carbon metabolism in Neurospora crassa
    • Jeong, S. S. & Schirch, V. (1996) Role of cytosolic serine hydrox-methyltransferase in one-carbon metabolism in Neurospora crassa. Arch. Biochem. Biophys. 335: 333-341.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 333-341
    • Jeong, S.S.1    Schirch, V.2
  • 12
    • 0034613194 scopus 로고    scopus 로고
    • Regulation of the balance of one-carbon metabolism in Saccharomyces cerevisiae
    • Piper, M., Hong, S. P., Ball, E. & Dawes, I. W. (2000) Regulation of the balance of one-carbon metabolism in Saccharomyces cerevisiae. J. Biol. Chem. 275: 30987-30995.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30987-30995
    • Piper, M.1    Hong, S.P.2    Ball, E.3    Dawes, I.W.4
  • 13
    • 0030862155 scopus 로고    scopus 로고
    • Role of mitochondrial and cytoplasmic serine hydroxymethyltransferase isozymes in do novo purine synthesis in Saccharomyces cerevisiae
    • Kastanos, E., Woldman, Y. & Appling, D. (1997) Role of mitochondrial and cytoplasmic serine hydroxymethyltransferase isozymes in do novo purine synthesis in Saccharomyces cerevisiae. Biochemistry 36: 14956-14964.
    • (1997) Biochemistry , vol.36 , pp. 14956-14964
    • Kastanos, E.1    Woldman, Y.2    Appling, D.3
  • 14
    • 0037064008 scopus 로고    scopus 로고
    • Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses
    • Herbig, K., Chiang, E., Lee, L., Hills, J., Shane, B. & Stover, P. (2002) Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses. J. Biol. Chem. 277: 38381-38389.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38381-38389
    • Herbig, K.1    Chiang, E.2    Lee, L.3    Hills, J.4    Shane, B.5    Stover, P.6
  • 16
    • 13244290814 scopus 로고    scopus 로고
    • Vitamin B-6 intake and smoking status influence lymphocyte serine hydroxymethyltransferase (SHMT) activity in healthy adults
    • Hansen, C., Shultz, T., Hunt, K., Hardin, K., Leklem, J., Huang, A. & Ames, B. (2003) Vitamin B-6 intake and smoking status influence lymphocyte serine hydroxymethyltransferase (SHMT) activity in healthy adults. FASEB J. A277.
    • (2003) FASEB J.
    • Hansen, C.1    Shultz, T.2    Hunt, K.3    Hardin, K.4    Leklem, J.5    Huang, A.6    Ames, B.7
  • 17
    • 0037657458 scopus 로고    scopus 로고
    • Hydrolytic activity toward pyridoxine-5′-β-D-glucoside in rat intestinal mucosa is not increased by vitamin B-6 deficiency: Effect of basal diet composition and pyridoxine intake
    • Mackey, A., Lieu, S., Carmen, C. & Gregory, J. F. (2003) Hydrolytic activity toward pyridoxine-5′-β-D-glucoside in rat intestinal mucosa is not increased by vitamin B-6 deficiency: effect of basal diet composition and pyridoxine intake. J. Nutr. 133: 1362-1367.
    • (2003) J. Nutr. , vol.133 , pp. 1362-1367
    • Mackey, A.1    Lieu, S.2    Carmen, C.3    Gregory, J.F.4
  • 18
    • 0017375321 scopus 로고
    • Report of the American Institute of Nutrition ad hoc committee on standards for nutritional studies
    • American Institute of Nutrition (1977) Report of the American Institute of Nutrition ad hoc committee on standards for nutritional studies. J. Nutr. 107: 1340-1348.
    • (1977) J. Nutr. , vol.107 , pp. 1340-1348
  • 19
    • 0027386062 scopus 로고
    • AIN-93 purified diets for laboratory rodents: Final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet
    • Reeves, P., Rossow, K. & Lindlauf, J. (1993) AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet. J. Nutr. 123: 1923-1931.
    • (1993) J. Nutr. , vol.123 , pp. 1923-1931
    • Reeves, P.1    Rossow, K.2    Lindlauf, J.3
  • 20
    • 0003721552 scopus 로고
    • National Academy Press, Washington, DC
    • Subcomittee on Laboratory Animal Nutrition, Committee on Animal Nutrition, Board on Agriculture & National Research Council (1995) Nutrient Requirements of Laboratory Animals, 4th revised ed. National Academy Press, Washington, DC.
    • (1995) Nutrient Requirements of Laboratory Animals, 4th Revised Ed.
  • 21
    • 0021968758 scopus 로고
    • Stability of pyridoxal 5′-phosphate semicarbazone: Application in plasma vitamin B-6 analysis and population surveys of vitamin B-6 nutritional status
    • Ubbink, J., Serfontein, W. J. & de Villiers, L. S. (1985) Stability of pyridoxal 5′-phosphate semicarbazone: application in plasma vitamin B-6 analysis and population surveys of vitamin B-6 nutritional status. J. Chromatogr. 342: 277-284.
    • (1985) J. Chromatogr. , vol.342 , pp. 277-284
    • Ubbink, J.1    Serfontein, W.J.2    De Villiers, L.S.3
  • 22
    • 0019805266 scopus 로고
    • Dansylation of amino acids for high-performance liquid chromatography analysis
    • Tapuhi, Y., Schmidt, D. E., Under, W. & Karger, B. L. (1981) Dansylation of amino acids for high-performance liquid chromatography analysis. Anal. Biochem. 115: 123-129.
    • (1981) Anal. Biochem. , vol.115 , pp. 123-129
    • Tapuhi, Y.1    Schmidt, D.E.2    Under, W.3    Karger, B.L.4
  • 23
    • 0031253248 scopus 로고    scopus 로고
    • (Graham, J. M. & Rickwood, D., eds.). Oxford University Press, Oxford, UK
    • Graham, J. M. (1997) Subcellular Fractionation-A Practical Approach (Graham, J. M. & Rickwood, D., eds.), pp. 1-29. Oxford University Press, Oxford, UK.
    • (1997) Subcellular Fractionation - A Practical Approach , pp. 1-29
    • Graham, J.M.1
  • 24
    • 0031573430 scopus 로고    scopus 로고
    • Determination of serine hydroxymethyltransferase and reduced folate pools in tissue extracts
    • Kim, D., Fratte, S. D., Jeong, S. S. & Schirch, V. (1997) Determination of serine hydroxymethyltransferase and reduced folate pools in tissue extracts. Anal. Biochem. 253: 201-209.
    • (1997) Anal. Biochem. , vol.253 , pp. 201-209
    • Kim, D.1    Fratte, S.D.2    Jeong, S.S.3    Schirch, V.4
  • 25
    • 0031035739 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene
    • Stover, P., Chen, L. H., Suh, J. R., Stover, D. M., Keyomarsi, K. & Shane, B. (1997) Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene. J. Biol. Chem. 272: 1842-1848.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1842-1848
    • Stover, P.1    Chen, L.H.2    Suh, J.R.3    Stover, D.M.4    Keyomarsi, K.5    Shane, B.6
  • 27
    • 84961031476 scopus 로고
    • Biochemistry of dystrophic muscle. Mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase
    • Pennington, R. (1961) Biochemistry of dystrophic muscle. Mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase. Biochem. J. 80: 649-654.
    • (1961) Biochem. J. , vol.80 , pp. 649-654
    • Pennington, R.1
  • 29
    • 10544236654 scopus 로고
    • Pyridoxine and related compounds
    • (Sebrell, W. & Harris, R., eds.). Academic Press, New York, NY
    • Sherrnan, H. (1954) Pyridoxine and related compounds. In: Vitamins (Sebrell, W. & Harris, R., eds.), pp. 265-276. Academic Press, New York, NY.
    • (1954) Vitamins , pp. 265-276
    • Sherrnan, H.1
  • 30
    • 0025542986 scopus 로고
    • Subtle abnormalities of gait detected early in vitamin B-6 deficiency in aged and weanling rats with hind gait analysis
    • Schaeffer, M., Cochary, E. & Sadowski, J. (1990) Subtle abnormalities of gait detected early in vitamin B-6 deficiency in aged and weanling rats with hind gait analysis. J. Am. Coll. Nutr. 9: 120-127.
    • (1990) J. Am. Coll. Nutr. , vol.9 , pp. 120-127
    • Schaeffer, M.1    Cochary, E.2    Sadowski, J.3
  • 31
    • 0029126266 scopus 로고
    • Tissue B-6 vitamer concentrations in rats fed excess vitamin B-6
    • Schaeffer, M. C., Gretz, D., Mahuren, J. D. & Coburn, S. P. (1995) Tissue B-6 vitamer concentrations in rats fed excess vitamin B-6. J. Nutr. 125: 2370-2378.
    • (1995) J. Nutr. , vol.125 , pp. 2370-2378
    • Schaeffer, M.C.1    Gretz, D.2    Mahuren, J.D.3    Coburn, S.P.4
  • 32
    • 0024250996 scopus 로고
    • Metabolic utilization of pyridoxine-β-glucoside in rats: Influence of vitamin B-6 status and route of administration
    • Trumbo, P. R. & Gregory, J. F. (1988) Metabolic utilization of pyridoxine-β-glucoside in rats: influence of vitamin B-6 status and route of administration. J. Nutr. 118: 1336-1342.
    • (1988) J. Nutr. , vol.118 , pp. 1336-1342
    • Trumbo, P.R.1    Gregory, J.F.2
  • 33
    • 0030848948 scopus 로고    scopus 로고
    • Elevations of serum cystathionine and total homocysteine in pyridoxine-, folate-, and cobalamin-deficient rats
    • Stabler, S. P., Sampson, D. A., Wang, L.-P. & Allen, R. H. (1997) Elevations of serum cystathionine and total homocysteine in pyridoxine-, folate-, and cobalamin-deficient rats. J. Nutr. Biochem. 8: 279-289.
    • (1997) J. Nutr. Biochem. , vol.8 , pp. 279-289
    • Stabler, S.P.1    Sampson, D.A.2    Wang, L.-P.3    Allen, R.H.4
  • 34
    • 0034086911 scopus 로고    scopus 로고
    • The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase
    • Snell, K., Baumann, U., Byrne, P., Chave, K. J., Renwick, S., Sanders, P. & Whithouse, S. K. (2000) The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase. Adv. Enzyme Regul. 40: 353-403.
    • (2000) Adv. Enzyme Regul. , vol.40 , pp. 353-403
    • Snell, K.1    Baumann, U.2    Byrne, P.3    Chave, K.J.4    Renwick, S.5    Sanders, P.6    Whithouse, S.K.7
  • 35
    • 0030800643 scopus 로고    scopus 로고
    • The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase
    • Jagath, J. R., Sharma, B., Rao, N. A. & Savithri, H. S. (1997) The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase. J. Biol. Chem. 272: 24355-24362.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24355-24362
    • Jagath, J.R.1    Sharma, B.2    Rao, N.A.3    Savithri, H.S.4
  • 37
    • 0025193689 scopus 로고
    • Vitamin B-6 influences glucocorticoid receptor-dependant gene expression
    • Allgood, V., Powell-Oliver, F. & Cidlowski, J. (1990) Vitamin B-6 influences glucocorticoid receptor-dependant gene expression. J. Biol. Chem. 265: 12424-12433.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12424-12433
    • Allgood, V.1    Powell-Oliver, F.2    Cidlowski, J.3
  • 38
    • 0027340420 scopus 로고
    • Vitamin B-6 deficiency causes activation of RNA polymerase and general enhancement of gene expression in rat liver
    • Oka, T., Komori, N., Kuwahata, M., Sassa, T., Suzuki, I., Okada, M. & Natori, Y. (1993) Vitamin B-6 deficiency causes activation of RNA polymerase and general enhancement of gene expression in rat liver. FEBS Lett. 331: 162-164.
    • (1993) FEBS Lett. , vol.331 , pp. 162-164
    • Oka, T.1    Komori, N.2    Kuwahata, M.3    Sassa, T.4    Suzuki, I.5    Okada, M.6    Natori, Y.7
  • 39
    • 0028979709 scopus 로고
    • Vitamin B-6 modulates expression of albumin gene by inactivating tissue-specific DNA-binding protein in rat liver
    • Oka, T., Komori, N., Kuwahata, M., Okada, M. & Natori, Y. (1995) Vitamin B-6 modulates expression of albumin gene by inactivating tissue-specific DNA-binding protein in rat liver. Biochom. J. 309: 243-248.
    • (1995) Biochom. J. , vol.309 , pp. 243-248
    • Oka, T.1    Komori, N.2    Kuwahata, M.3    Okada, M.4    Natori, Y.5
  • 40
    • 0028176274 scopus 로고
    • Effect of vitamin B-6 deficiency on the expression of glycogen phosphorylase mRNA in rat liver and skeletal muscle
    • Oka, T., Komori, N., Kuwahata, M., Suzuki, I., Okada, M. & Natori, Y. (1994) Effect of vitamin B-6 deficiency on the expression of glycogen phosphorylase mRNA in rat liver and skeletal muscle. Experientia 50: 127-129.
    • (1994) Experientia , vol.50 , pp. 127-129
    • Oka, T.1    Komori, N.2    Kuwahata, M.3    Suzuki, I.4    Okada, M.5    Natori, Y.6
  • 41
    • 4644359527 scopus 로고    scopus 로고
    • Vitamin B-6
    • (Rucker, R., Suttie, J., McCormick, D. & Machlin, L., eds.). Dekker, New York, NY
    • Leklem, J. (2001) Vitamin B-6. In: Handbook of Vitamins, 3rd ed. (Rucker, R., Suttie, J., McCormick, D. & Machlin, L., eds.), pp. 339-396. Dekker, New York, NY.
    • (2001) Handbook of Vitamins, 3rd Ed. , pp. 339-396
    • Leklem, J.1
  • 43
    • 13244272891 scopus 로고    scopus 로고
    • Dietary vitamin B6 restriction does not a ter rates of homocysteine remethylation or synthesis in healthy young women and men
    • in press
    • Davis, S. R., Scneer, J. B., Quinlivan, E. P., Coats, B. S., Stacpoole, P. W. & Gregory, J. F. (2004) Dietary vitamin B6 restriction does not a ter rates of homocysteine remethylation or synthesis in healthy young women and men. Am. J. Clin. Nutr. (in press).
    • (2004) Am. J. Clin. Nutr.
    • Davis, S.R.1    Scneer, J.B.2    Quinlivan, E.P.3    Coats, B.S.4    Stacpoole, P.W.5    Gregory, J.F.6
  • 44
    • 0033865194 scopus 로고    scopus 로고
    • Nutritional aspects and possible pathological mechanisms of hyperhomocysteinaemia: An independent risk factor for vascular disease
    • McKinley, M. (2000) Nutritional aspects and possible pathological mechanisms of hyperhomocysteinaemia: an independent risk factor for vascular disease. Proc. Nutr. Soc. 59: 221-237.
    • (2000) Proc. Nutr. Soc. , vol.59 , pp. 221-237
    • McKinley, M.1
  • 45
    • 0032771346 scopus 로고    scopus 로고
    • Homocysteine metabolism
    • Selhub, J. (1999) Homocysteine metabolism. Annu. Rev. Nutr. 19: 217-246.
    • (1999) Annu. Rev. Nutr. , vol.19 , pp. 217-246
    • Selhub, J.1
  • 46
    • 0343068972 scopus 로고
    • Free amino acids in plasma and tissues of rats fed a vitamin B-6 deficient diet
    • Swendseid, M., Villalobos, J. & Friedrich, B. (1964) Free amino acids in plasma and tissues of rats fed a vitamin B-6 deficient diet. J. Nutr. 82: 206-208.
    • (1964) J. Nutr. , vol.82 , pp. 206-208
    • Swendseid, M.1    Villalobos, J.2    Friedrich, B.3
  • 47
    • 0022944532 scopus 로고
    • Effect of vitamin B-6 deficiency on plasma amino acid levels in chronically azotemic rats
    • Wolfson, M., Laidlaw, S., Flugel-Link, R., Strong, C., Salusky, E. & Kopple, J. (1986) Effect of vitamin B-6 deficiency on plasma amino acid levels in chronically azotemic rats. J. Nutr. 116: 1865-1872.
    • (1986) J. Nutr. , vol.116 , pp. 1865-1872
    • Wolfson, M.1    Laidlaw, S.2    Flugel-Link, R.3    Strong, C.4    Salusky, E.5    Kopple, J.6


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