메뉴 건너뛰기




Volumn 45, Issue 1, 2004, Pages 17-31

PPARα controls the intracellular coenzyme A concentration via regulation of PANK1α gene expression

Author keywords

Fatty acid oxidation; Liver; Pantothenate; Pantothenate kinase; Peroxisome proliferator activator receptor

Indexed keywords

BEZAFIBRATE; COENZYME A; COMPLEMENTARY DNA; MESSENGER RNA; PANTOTHENATE KINASE; PANTOTHENIC ACID; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR AGONIST; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; CELL RECEPTOR; PHOSPHOTRANSFERASE; THIOL DERIVATIVE; TRANSCRIPTION FACTOR;

EID: 0842304656     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: 10.1194/jlr.M300279-JLR200     Document Type: Article
Times cited : (53)

References (75)
  • 1
    • 0002562806 scopus 로고
    • Metabolism of coenzyme A
    • D. M. Greenburg, editor. Academic Press, Inc., New York
    • Abiko, Y. 1975. Metabolism of coenzyme A. In Metabolic Pathways. D. M. Greenburg, editor. Academic Press, Inc., New York. 1-25.
    • (1975) Metabolic Pathways , pp. 1-25
    • Abiko, Y.1
  • 2
    • 0000991019 scopus 로고    scopus 로고
    • Biosynthesis of pantothenic acid and coenzyme A
    • F. C. Neidhardt, R. Curtiss, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger, editors. American Society for Microbiology, Washington, D.C.
    • Jackowski, S. 1996. Biosynthesis of pantothenic acid and coenzyme A. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. F. C. Neidhardt, R. Curtiss, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger, editors. American Society for Microbiology, Washington, D.C. 687-694.
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , pp. 687-694
    • Jackowski, S.1
  • 5
    • 0023664065 scopus 로고
    • Regulation of pantothenate kinase by coenzyme A and its thioesters
    • Vallari, D. S., S. Jackowski, and C. O. Rock. 1987. Regulation of pantothenate kinase by coenzyme A and its thioesters. J. Biol. Chem. 262: 2468-2471.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2468-2471
    • Vallari, D.S.1    Jackowski, S.2    Rock, C.O.3
  • 6
    • 0019812065 scopus 로고
    • Regulation of coenzyme A biosynthesis
    • Jackowski, S., and C. O. Rock. 1981. Regulation of coenzyme A biosynthesis. J. Bacteriol. 148: 926-932.
    • (1981) J. Bacteriol. , vol.148 , pp. 926-932
    • Jackowski, S.1    Rock, C.O.2
  • 7
    • 0020491113 scopus 로고
    • Rate-limiting step and control of coenzyme A synthesis in cardiac muscle
    • Robishaw, J. D., D. A. Berkich, and J. R. Neely. 1982. Rate-limiting step and control of coenzyme A synthesis in cardiac muscle. J. Biol. Chem. 257: 10967-10972.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10967-10972
    • Robishaw, J.D.1    Berkich, D.A.2    Neely, J.R.3
  • 8
    • 0033954772 scopus 로고    scopus 로고
    • Pantothenate kinase regulation of the intracellular concentration of coenzyme A
    • Rock, C. O., R. B. Calder, M. A. Karim, and S. Jackowski. 2000. Pantothenate kinase regulation of the intracellular concentration of coenzyme A. J. Biol. Chem. 275: 1377-1383.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1377-1383
    • Rock, C.O.1    Calder, R.B.2    Karim, M.A.3    Jackowski, S.4
  • 9
    • 0037193667 scopus 로고    scopus 로고
    • The murine Pank1 gene encodes two differentially regulated pantothenate kinase isozymes
    • Rock, C. O., M. A. Karim, Y-M. Zhang, and S. Jackowski. 2002. The murine Pank1 gene encodes two differentially regulated pantothenate kinase isozymes. Gene. 291: 35-43.
    • (2002) Gene , vol.291 , pp. 35-43
    • Rock, C.O.1    Karim, M.A.2    Zhang, Y.-M.3    Jackowski, S.4
  • 11
    • 0037322485 scopus 로고    scopus 로고
    • An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria
    • Hortnagel, K., H. Prokisch, and T. Meitinger. 2003. An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria. Hum. Mol. Genet. 12: 321-327.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 321-327
    • Hortnagel, K.1    Prokisch, H.2    Meitinger, T.3
  • 12
    • 0037062571 scopus 로고    scopus 로고
    • HARP syndrome is allelic with pantothenate kinase-associated neurodegeneration
    • Ching, K. H., S. K. Westaway, J. Gitschier, J. J. Higgins, and S. J. Hayflick. 2002. HARP syndrome is allelic with pantothenate kinase-associated neurodegeneration. Neurology. 58: 1673-1674.
    • (2002) Neurology , vol.58 , pp. 1673-1674
    • Ching, K.H.1    Westaway, S.K.2    Gitschier, J.3    Higgins, J.J.4    Hayflick, S.J.5
  • 13
    • 0020540019 scopus 로고
    • Effects of hypolipidemic drugs on hepatic CoA
    • Halvorsen, O. 1983. Effects of hypolipidemic drugs on hepatic CoA. Biochem. Pharmacol. 32: 1126-1128.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 1126-1128
    • Halvorsen, O.1
  • 14
    • 0018777097 scopus 로고
    • Increased biosynthesis of CoA in the liver of rats treated with clofibrate
    • Skrede, S., and O. Halvorsen. 1979. Increased biosynthesis of CoA in the liver of rats treated with clofibrate. Eur. J. Biochem. 98: 223-229.
    • (1979) Eur. J. Biochem. , vol.98 , pp. 223-229
    • Skrede, S.1    Halvorsen, O.2
  • 15
    • 0015595662 scopus 로고
    • The effect of acute and prolonged ethanol treatment on the contents of coenzyme A, carnitine and their derivatives in rat liver
    • Kondrup, J., and N. Grunnet. 1973. The effect of acute and prolonged ethanol treatment on the contents of coenzyme A, carnitine and their derivatives in rat liver. Biochem. J. 132: 373-379.
    • (1973) Biochem. J. , vol.132 , pp. 373-379
    • Kondrup, J.1    Grunnet, N.2
  • 16
    • 0022497626 scopus 로고
    • Effects of thyroid state and fasting on the concentrations of CoA and malonyl-CoA in rat liver
    • Lund, H., J. A. Stakkestad, and S. Skrede. 1986. Effects of thyroid state and fasting on the concentrations of CoA and malonyl-CoA in rat liver. Biochim. Biophys. Acta. 876: 685-687.
    • (1986) Biochim. Biophys. Acta , vol.876 , pp. 685-687
    • Lund, H.1    Stakkestad, J.A.2    Skrede, S.3
  • 17
    • 0017347219 scopus 로고
    • Effects of clofibrate on ethanol-induced modifications in liver and adipose tissue metabolism: Role of hepatic redox state and hormonal mechanisms
    • Savolainen, M.J., V. P. Jauhonen, and I. E. Hassinen. 1977. Effects of clofibrate on ethanol-induced modifications in liver and adipose tissue metabolism: role of hepatic redox state and hormonal mechanisms. Biochem. Pharmacol. 26: 425-431.
    • (1977) Biochem. Pharmacol. , vol.26 , pp. 425-431
    • Savolainen, M.J.1    Jauhonen, V.P.2    Hassinen, I.E.3
  • 18
    • 0018225585 scopus 로고
    • The relationship between metabolic state and total CoA content of rat liver and heart
    • Smith, C. M., M. L. Cano, and J. Potyraj. 1978. The relationship between metabolic state and total CoA content of rat liver and heart. J. Nutr. 108: 854-862.
    • (1978) J. Nutr. , vol.108 , pp. 854-862
    • Smith, C.M.1    Cano, M.L.2    Potyraj, J.3
  • 19
    • 0018868147 scopus 로고
    • Regulation of coenzyme A biosynthesis by glucagon and glucocorticoid in adult rat liver parenchymal cells
    • Smith, C. M., and C. R. Savage, Jr. 1980. Regulation of coenzyme A biosynthesis by glucagon and glucocorticoid in adult rat liver parenchymal cells. Biochem. J. 188: 175-184.
    • (1980) Biochem. J. , vol.188 , pp. 175-184
    • Smith, C.M.1    Savage Jr., C.R.2
  • 21
    • 0000302176 scopus 로고
    • Regulation of coenzyme A synthesis in heart muscle: Effects of diabetes and fasting
    • Reibel, D. K., B. W. Wyse, D. A. Berkich, and J. R. Neely. 1981. Regulation of coenzyme A synthesis in heart muscle: effects of diabetes and fasting. Am. J. Physiol. 240: H606-H611.
    • (1981) Am. J. Physiol. , vol.240
    • Reibel, D.K.1    Wyse, B.W.2    Berkich, D.A.3    Neely, J.R.4
  • 22
    • 0023712250 scopus 로고
    • Effects of ciprofibrate and 2-[5-(4-chlorophenyl)pentyl]oxirane-2-carboxylate (POCA) on the distribution of carnitine and CoA and their acyl-esters and on enzyme activities in rats
    • Bhuiyan, A. K. M. J., K. Bartlett, H. S. A. Sherratt, and L. Agius. 1988. Effects of ciprofibrate and 2-[5-(4-chlorophenyl)pentyl]oxirane-2-carboxylate (POCA) on the distribution of carnitine and CoA and their acyl-esters and on enzyme activities in rats. Biochem. J. 253: 337-343.
    • (1988) Biochem. J. , vol.253 , pp. 337-343
    • Bhuiyan, A.K.M.J.1    Bartlett, K.2    Sherratt, H.S.A.3    Agius, L.4
  • 23
    • 0018290370 scopus 로고
    • Clofibrate-induced increase in coenzyme A concentration in rat tissues
    • Voltti, H., M. J. Savolainen, V. P. Jauhonen, and I. E. Hassinen. 1979. Clofibrate-induced increase in coenzyme A concentration in rat tissues. Biochem. J. 182: 95-102.
    • (1979) Biochem. J. , vol.182 , pp. 95-102
    • Voltti, H.1    Savolainen, M.J.2    Jauhonen, V.P.3    Hassinen, I.E.4
  • 24
    • 0030602866 scopus 로고    scopus 로고
    • The peroxisome proliferator activated receptors (PPARS) and their effects on lipid metabolism and adipocyte differentiation
    • Schoonjans, K., B. Staels, and J. Auwerx. 1996. The peroxisome proliferator activated receptors (PPARS) and their effects on lipid metabolism and adipocyte differentiation. Biochim. Biophys. Acta. 1302: 93-109.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 93-109
    • Schoonjans, K.1    Staels, B.2    Auwerx, J.3
  • 25
    • 0029609755 scopus 로고
    • PPAR: A mediator of peroxisome proliferator action
    • Green, S. 1995. PPAR: a mediator of peroxisome proliferator action. Mutat. Res. 333: 101-109.
    • (1995) Mutat. Res. , vol.333 , pp. 101-109
    • Green, S.1
  • 26
    • 0029994543 scopus 로고    scopus 로고
    • Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression
    • Schoonjans, K., B. Staels, and J. Auwerx. 1996. Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression. J. Lipid Res. 37: 907-925.
    • (1996) J. Lipid Res. , vol.37 , pp. 907-925
    • Schoonjans, K.1    Staels, B.2    Auwerx, J.3
  • 27
    • 0028033268 scopus 로고
    • The peroxisome proliferator-activated receptor regulates mitochondrial fatty acid oxidative enzyme gene expression
    • Gulick, T., S. Cresci, T. Caira, D. D. Moore, and D. P. Kelly. 1994. The peroxisome proliferator-activated receptor regulates mitochondrial fatty acid oxidative enzyme gene expression. Proc. Natl. Acad. Sci. USA. 91: 11012-11016.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11012-11016
    • Gulick, T.1    Cresci, S.2    Caira, T.3    Moore, D.D.4    Kelly, D.P.5
  • 28
    • 0026541591 scopus 로고
    • The mouse peroxisome proliferator activated receptor recognizes a response element in the 5′ flanking sequence of the rat acyl CoA oxidase gene
    • Tugwood, J. D., I. Issemann, R. G. Anderson, K. R. Bundell, W. L. McPheat, and S. Green. 1992. The mouse peroxisome proliferator activated receptor recognizes a response element in the 5′ flanking sequence of the rat acyl CoA oxidase gene. EMBO J. 11: 433-439.
    • (1992) EMBO J. , vol.11 , pp. 433-439
    • Tugwood, J.D.1    Issemann, I.2    Anderson, R.G.3    Bundell, K.R.4    McPheat, W.L.5    Green, S.6
  • 29
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors
    • Kliewer, S. A., K. Umesono, D.J. Noonan, R. A. Heyman, and R. M. Evans. 1992. Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors. Nature. 358: 771-774.
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Noonan, D.J.3    Heyman, R.A.4    Evans, R.M.5
  • 31
    • 0004595467 scopus 로고    scopus 로고
    • Human pantothenate kinase 1 (PANK1) gene: Characterization of the cDNAs, structural organization and mapping of the locus to chromosome 10q23.2-23.31
    • Karim, M. A., V. A. Valentine, and S. Jackowski. 2000. Human pantothenate kinase 1 (PANK1) gene: characterization of the cDNAs, structural organization and mapping of the locus to chromosome 10q23.2-23.31 (Abstract). Am. J. Hum. Genet. 67: 185.
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 185
    • Karim, M.A.1    Valentine, V.A.2    Jackowski, S.3
  • 32
    • 0000155229 scopus 로고    scopus 로고
    • CsCl purification of RNA from cultured cells
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl, editors. John Wiley & Sons, New York
    • Kingston, R. E. 1998. CsCl purification of RNA from cultured cells. In Current Protocols in Molecular Biology. F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl, editors. John Wiley & Sons, New York. 4.2.3-4.2.9.
    • (1998) Current Protocols in Molecular Biology , pp. 423-429
    • Kingston, R.E.1
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0019432469 scopus 로고
    • A simple method of reducing the fading of immunofluorescence during microscopy
    • Johnson, G. D., and G. M. C. Araujo. 1981. A simple method of reducing the fading of immunofluorescence during microscopy. J. Immunol. Methods. 43: 349-350.
    • (1981) J. Immunol. Methods , vol.43 , pp. 349-350
    • Johnson, G.D.1    Araujo, G.M.C.2
  • 35
    • 0035122485 scopus 로고    scopus 로고
    • Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase
    • Vigneri, P., and J. Y. J. Wang. 2001. Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase. Nat. Med. 7: 228-234.
    • (2001) Nat. Med. , vol.7 , pp. 228-234
    • Vigneri, P.1    Wang, J.Y.J.2
  • 36
    • 0033602117 scopus 로고    scopus 로고
    • Variation of liver-type fatty acid binding protein content in the human hepatoma cell line HepG2 by peroxisome proliferators and antisense RNA affects the rate of fatty acid uptake
    • Wolfrum, C., C. Buhlmann, B. Rolf, T. Borchers, and F. Spener. 1999. Variation of liver-type fatty acid binding protein content in the human hepatoma cell line HepG2 by peroxisome proliferators and antisense RNA affects the rate of fatty acid uptake. Biochim. Biophys. Acta. 1437: 194-201.
    • (1999) Biochim. Biophys. Acta , vol.1437 , pp. 194-201
    • Wolfrum, C.1    Buhlmann, C.2    Rolf, B.3    Borchers, T.4    Spener, F.5
  • 37
    • 0031909536 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of fibric acid derivatives (fibrates)
    • Miller, D. B., and J. D. Spence. 1998. Clinical pharmacokinetics of fibric acid derivatives (fibrates). Clin. Pharmacokinet. 34: 155-162.
    • (1998) Clin. Pharmacokinet. , vol.34 , pp. 155-162
    • Miller, D.B.1    Spence, J.D.2
  • 38
  • 39
    • 0034671583 scopus 로고    scopus 로고
    • The human cytochrome P4501A1 mRNA is rapidly degraded in HepG2 cells
    • Lekas, P., K. L. Tin, and R. D. Prokipcak. 2000. The human cytochrome P4501A1 mRNA is rapidly degraded in HepG2 cells. Arch. Biochem. Biophys. 384: 311-318.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 311-318
    • Lekas, P.1    Tin, K.L.2    Prokipcak, R.D.3
  • 40
    • 0033546734 scopus 로고    scopus 로고
    • The AU-rich 3′ untranslated region of human MDR1 mRNA is an inefficient mRNA destabilizer
    • Prokipcak, R. D., A. Raouf, and C. Lee. 2000. The AU-rich 3′ untranslated region of human MDR1 mRNA is an inefficient mRNA destabilizer. Arch. Biochem. Biophys. 261: 627-634.
    • (2000) Arch. Biochem. Biophys. , vol.261 , pp. 627-634
    • Prokipcak, R.D.1    Raouf, A.2    Lee, C.3
  • 41
    • 0034737576 scopus 로고    scopus 로고
    • Cloning and characterization of a functional peroxisome proliferator activator receptor-γ-responsive element in the promoter of the CAP gene
    • Baumann, C. A., N. Chokshi, A. R. Saltiel, and V. Ribon. 2000. Cloning and characterization of a functional peroxisome proliferator activator receptor-γ-responsive element in the promoter of the CAP gene. J. Biol. Chem. 275: 9131-9135.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9131-9135
    • Baumann, C.A.1    Chokshi, N.2    Saltiel, A.R.3    Ribon, V.4
  • 43
    • 0034681335 scopus 로고    scopus 로고
    • Glucose regulation of mouse S14 gene expression in hepatocytes
    • Koo, S. H., and H. C. Towle. 2000. Glucose regulation of mouse S14 gene expression in hepatocytes. J. Biol. Chem. 275: 5200-5207.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5200-5207
    • Koo, S.H.1    Towle, H.C.2
  • 44
    • 0037040185 scopus 로고    scopus 로고
    • Mechanism for fatty acid 'spareing' effect on glucose-induced transcription
    • Kawaguchi, R., K. Osatomi, H. Yamashita, T. Kabashima, and K. Uyeda. 2002. Mechanism for fatty acid 'spareing' effect on glucose-induced transcription. J. Biol. Chem. 277: 3829-3835.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3829-3835
    • Kawaguchi, R.1    Osatomi, K.2    Yamashita, H.3    Kabashima, T.4    Uyeda, K.5
  • 45
    • 0029094172 scopus 로고
    • Two CACGTG motifs with proper spacing dictate the carbohydrate regulation of hepatic gene transcription
    • Shih, H. M., Z. Liu, and H. C. Towle. 1995. Two CACGTG motifs with proper spacing dictate the carbohydrate regulation of hepatic gene transcription. J. Biol. Chem. 270: 21991-21997.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21991-21997
    • Shih, H.M.1    Liu, Z.2    Towle, H.C.3
  • 46
    • 0037031836 scopus 로고    scopus 로고
    • ChREBP rather than USF2 regulates glucose stimulation of endogenous L-pyruvate kinase expression in insulin-secreting cells
    • Wang, H., and C. B. Wollheim. 2002. ChREBP rather than USF2 regulates glucose stimulation of endogenous L-pyruvate kinase expression in insulin-secreting cells. J. Biol. Chem. 277: 32746-32752.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32746-32752
    • Wang, H.1    Wollheim, C.B.2
  • 48
    • 0037166338 scopus 로고    scopus 로고
    • Role of sterol regulatory element-binding protein 1 in regulation of renal lipid metabolism and glomerulosclerosis in diabetes mellitus
    • Sun, L., N. Halaihel, W. Zhang, T. Roger, and M. Levi. 2002. Role of sterol regulatory element-binding protein 1 in regulation of renal lipid metabolism and glomerulosclerosis in diabetes mellitus. J. Biol. Chem. 277: 18919-18927.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18919-18927
    • Sun, L.1    Halaihel, N.2    Zhang, W.3    Roger, T.4    Levi, M.5
  • 49
    • 0036013438 scopus 로고    scopus 로고
    • Characterizatgion of the human PPARα promoter: Identification of a functional nuclear receptor response element
    • Torra, I. P., Y. Jamshidi, D. M. Flavell, J-C. Fruchart, and B. Staels. 2002. Characterizatgion of the human PPARα promoter: identification of a functional nuclear receptor response element. Mol. Endocrinol 16: 1013-1028.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 1013-1028
    • Torra, I.P.1    Jamshidi, Y.2    Flavell, D.M.3    Fruchart, J.-C.4    Staels, B.5
  • 50
    • 0034680797 scopus 로고    scopus 로고
    • Glucose down-regulates the expression of the peroxisome proliferator-activated receptor-alpha gene in the pancreatic beta cell
    • Roduit, R., J. Morin, F. Masse, L. Segall, E. Roche, C. B. Newgard, F. Assimacopoulos-Jeannet, and M. Prentki. 2000. Glucose down-regulates the expression of the peroxisome proliferator-activated receptor-alpha gene in the pancreatic beta cell. J. Biol. Chem. 275: 35799-35806.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35799-35806
    • Roduit, R.1    Morin, J.2    Masse, F.3    Segall, L.4    Roche, E.5    Newgard, C.B.6    Assimacopoulos-Jeannet, F.7    Prentki, M.8
  • 51
    • 0026265115 scopus 로고
    • Pantothenic acid in health and disease
    • Tahiliani, A. G., and C. J. Beinlich. 1991. Pantothenic acid in health and disease. Vitam. Horm. 46: 165-228.
    • (1991) Vitam. Horm. , vol.46 , pp. 165-228
    • Tahiliani, A.G.1    Beinlich, C.J.2
  • 52
    • 0035958960 scopus 로고    scopus 로고
    • Identification of peroxisome proliferator-responsive human genes by elevated expression of the peroxisome proliferator-activated receptor α in HepG2 cells
    • Hsu, M. H., U. Savas, K.J. Griffin, and E. F. Johnson. 2001. Identification of peroxisome proliferator-responsive human genes by elevated expression of the peroxisome proliferator-activated receptor α in HepG2 cells. J. Biol. Chem. 276: 27950-27958.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27950-27958
    • Hsu, M.H.1    Savas, U.2    Griffin, K.J.3    Johnson, E.F.4
  • 53
    • 0037853313 scopus 로고    scopus 로고
    • Role of feedback regulation of pantothenate kinase (CoaA) in the control of coenzyme A levels in Escherichia coli
    • Rock, C. O., H-W. Park, and S. Jackowski. 2003. Role of feedback regulation of pantothenate kinase (CoaA) in the control of coenzyme A levels in Escherichia coli. J. Bacteriol. 185: 3410-3415.
    • (2003) J. Bacteriol. , vol.185 , pp. 3410-3415
    • Rock, C.O.1    Park, H.-W.2    Jackowski, S.3
  • 55
    • 0021858568 scopus 로고
    • Pantothenate transport in Escherichia coli
    • Vallari, D. S., and C. O. Rock. 1985. Pantothenate transport in Escherichia coli. J. Bacteriol. 162: 1156-1161.
    • (1985) J. Bacteriol. , vol.162 , pp. 1156-1161
    • Vallari, D.S.1    Rock, C.O.2
  • 56
    • 0022851228 scopus 로고
    • Pantothenate-sodium cotransport in renal brush-border membranes
    • Barbarat, B., and R. A. Podevin. 1986. Pantothenate-sodium cotransport in renal brush-border membranes. J. Biol. Chem. 261: 14455-14460.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14455-14460
    • Barbarat, B.1    Podevin, R.A.2
  • 57
    • 0026778799 scopus 로고
    • Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene of Escherichia coli
    • Song, W-J., and S. Jackowski. 1992. Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene of Escherichia coli. J. Bacteriol. 174: 6411-6417.
    • (1992) J. Bacteriol. , vol.174 , pp. 6411-6417
    • Song, W.-J.1    Jackowski, S.2
  • 58
    • 0033578920 scopus 로고    scopus 로고
    • Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli
    • Geerlof, A., A. Lewendon, and W. V. Shaw. 1999. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J. Biol. Chem. 274: 27105-27111.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27105-27111
    • Geerlof, A.1    Lewendon, A.2    Shaw, W.V.3
  • 59
    • 0017824474 scopus 로고
    • Coenzyme A and carnitine distribution in normal and ischemic hearts
    • Idell-Wenger, J., L. Grotyohann, and J. R. Neely. 1978. Coenzyme A and carnitine distribution in normal and ischemic hearts. J. Biol. Chem. 253: 4310-4318.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4310-4318
    • Idell-Wenger, J.1    Grotyohann, L.2    Neely, J.R.3
  • 60
    • 0018337607 scopus 로고
    • Assay of citric acid cycle intermediates and related compounds-uptake with tissue metabolite levels and intracellular distribution
    • Williamson, J., and B. Corkey. 1979. Assay of citric acid cycle intermediates and related compounds-uptake with tissue metabolite levels and intracellular distribution. Methods Enzymol. 55: 200-222.
    • (1979) Methods Enzymol. , vol.55 , pp. 200-222
    • Williamson, J.1    Corkey, B.2
  • 61
    • 0022458178 scopus 로고
    • Changes in CoA pools in hepatic peroxisomes of the rat under various conditions
    • Horie, S., M. Isobe, and T. Suga. 1986. Changes in CoA pools in hepatic peroxisomes of the rat under various conditions. J. Biochem. 99: 1345-1352.
    • (1986) J. Biochem. , vol.99 , pp. 1345-1352
    • Horie, S.1    Isobe, M.2    Suga, T.3
  • 62
  • 63
    • 0030724442 scopus 로고    scopus 로고
    • Mitochondrial, but not peroxisomal, β-oxidation of fatty acids is conserved in coenzyme A-deficient rat liver
    • Youssef, J. A., W. O. Song, and M. Z. Badr. 1997. Mitochondrial, but not peroxisomal, β-oxidation of fatty acids is conserved in coenzyme A-deficient rat liver. Mol. Cell. Biochem. 175: 37-42.
    • (1997) Mol. Cell. Biochem. , vol.175 , pp. 37-42
    • Youssef, J.A.1    Song, W.O.2    Badr, M.Z.3
  • 64
    • 0034693059 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae PCD1 gene encodes a peroxisomal nudix hydrolase active toward coenzyme A and its derivatives
    • Cartwright, J. L., L. Gasmi, D. G. Spiller, and A. G. McLennan. 2000. The Saccharomyces cerevisiae PCD1 gene encodes a peroxisomal nudix hydrolase active toward coenzyme A and its derivatives. J. Biol. Chem. 275: 32925-32930.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32925-32930
    • Cartwright, J.L.1    Gasmi, L.2    Spiller, D.G.3    McLennan, A.G.4
  • 65
    • 0035397652 scopus 로고    scopus 로고
    • The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives
    • Gasmi, L., and A. G. McLennan. 2001. The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives. Biochem. J. 357: 33-38.
    • (2001) Biochem. J. , vol.357 , pp. 33-38
    • Gasmi, L.1    McLennan, A.G.2
  • 67
    • 0026317374 scopus 로고
    • Hallervorden-Spatz syndrome and brain iron metabolism
    • Swaiman, K. F. 1991. Hallervorden-Spatz syndrome and brain iron metabolism. Arch. Neurol. 48: 1285-1293.
    • (1991) Arch. Neurol. , vol.48 , pp. 1285-1293
    • Swaiman, K.F.1
  • 69
    • 0026590705 scopus 로고
    • Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease
    • Connor, J. R., B. S. Snyder, J. L. Beard, R. E. Fine, and E. J. Mufson. 1992. Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease. J. Neurosci. Res. 31: 327-335.
    • (1992) J. Neurosci. Res. , vol.31 , pp. 327-335
    • Connor, J.R.1    Snyder, B.S.2    Beard, J.L.3    Fine, R.E.4    Mufson, E.J.5
  • 70
    • 0025821265 scopus 로고
    • Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia
    • Dexter, D. T., A. Carayon, F. Javoy-Agid, Y. Agid, F. R. Wells, S. E. Daniel, A. J. Lees, P. Jenner, and C. D. Marsden. 1991. Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia. Brain. 114: 1953-1975.
    • (1991) Brain , vol.114 , pp. 1953-1975
    • Dexter, D.T.1    Carayon, A.2    Javoy-Agid, F.3    Agid, Y.4    Wells, F.R.5    Daniel, S.E.6    Lees, A.J.7    Jenner, P.8    Marsden, C.D.9
  • 71
    • 0020842362 scopus 로고
    • A bifunctional enzyme complex in coenzyme A biosynthesis: Purification of 4′ pantetheine phosphate adenylyltransferase and dephospho-CoA kinase
    • Worrall, D. M., and P. K. Tubbs. 1983. A bifunctional enzyme complex in coenzyme A biosynthesis: purification of 4′ pantetheine phosphate adenylyltransferase and dephospho-CoA kinase. J. Biochem. (Tokyo). 215: 153-157.
    • (1983) J. Biochem. (Tokyo) , vol.215 , pp. 153-157
    • Worrall, D.M.1    Tubbs, P.K.2
  • 72
    • 0020727375 scopus 로고
    • Mitochondrial pantetheinephosphate adenylytransferase and dephospho-CoA kinase
    • Skrede, S., and O. Halvorsen. 1983. Mitochondrial pantetheinephosphate adenylytransferase and dephospho-CoA kinase. Eur. J. Biochem. 131: 57-63.
    • (1983) Eur. J. Biochem. , vol.131 , pp. 57-63
    • Skrede, S.1    Halvorsen, O.2
  • 73
    • 0023664895 scopus 로고
    • A transport system for coenzyme A in isolated rat heart mitochondria
    • Tahiliani, A. G., and J. R. Neely. 1987. A transport system for coenzyme A in isolated rat heart mitochondria. J. Biol. Chem. 262: 11607-11610.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11607-11610
    • Tahiliani, A.G.1    Neely, J.R.2
  • 74
    • 0024457069 scopus 로고
    • Dependence of mitochondrial coenzyme A uptake on the membrane electrical gradient
    • Tahiliani, A. G. 1989. Dependence of mitochondrial coenzyme A uptake on the membrane electrical gradient. J. Biol. Chem. 264: 18426-18432.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18426-18432
    • Tahiliani, A.G.1
  • 75
    • 0021762952 scopus 로고
    • Transport of coenzyme A in plant mitochondria
    • Neuburger, M., D. A. Day, and R. Douce. 1984. Transport of coenzyme A in plant mitochondria. Arch. Biochem. Biophys. 229: 253-258.
    • (1984) Arch. Biochem. Biophys. , vol.229 , pp. 253-258
    • Neuburger, M.1    Day, D.A.2    Douce, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.