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Volumn 14, Issue 3, 2007, Pages 291-302

Chemical Knockout of Pantothenate Kinase Reveals the Metabolic and Genetic Program Responsible for Hepatic Coenzyme A Homeostasis

Author keywords

CHEMBIOL; DNA; SIGNALING

Indexed keywords

4 AMINOBUTYRIC ACID; CARNITINE; COENZYME A; DRUG DERIVATIVE; NOOTROPIC AGENT; PANTOGAB; PANTOTHENATE KINASE; PANTOTHENIC ACID; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 33947241895     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2007.01.013     Document Type: Article
Times cited : (97)

References (55)
  • 2
    • 0019812065 scopus 로고
    • Regulation of coenzyme A biosynthesis
    • Jackowski S., and Rock C.O. Regulation of coenzyme A biosynthesis. J. Bacteriol. 148 (1981) 926-932
    • (1981) J. Bacteriol. , vol.148 , pp. 926-932
    • Jackowski, S.1    Rock, C.O.2
  • 3
    • 0020491113 scopus 로고
    • Rate-limiting step and control of coenzyme A synthesis in cardiac muscle
    • Robishaw J.D., Berkich D.A., and Neely J.R. Rate-limiting step and control of coenzyme A synthesis in cardiac muscle. J. Biol. Chem. 257 (1982) 10967-10972
    • (1982) J. Biol. Chem. , vol.257 , pp. 10967-10972
    • Robishaw, J.D.1    Berkich, D.A.2    Neely, J.R.3
  • 4
    • 0033954772 scopus 로고    scopus 로고
    • Pantothenate kinase regulation of the intracellular concentration of coenzyme A
    • Rock C.O., Calder R.B., Karim M.A., and Jackowski S. Pantothenate kinase regulation of the intracellular concentration of coenzyme A. J. Biol. Chem. 275 (2000) 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
  • 5
    • 0026778799 scopus 로고
    • Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene of Escherichia coli
    • Song W.-J., and Jackowski S. Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene of Escherichia coli. J. Bacteriol. 174 (1992) 6411-6417
    • (1992) J. Bacteriol. , vol.174 , pp. 6411-6417
    • Song, W.-J.1    Jackowski, S.2
  • 6
    • 25444432519 scopus 로고    scopus 로고
    • Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters
    • Zhang Y.-M., Rock C.O., and Jackowski S. Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters. J. Biol. Chem. 280 (2005) 32594-32601
    • (2005) J. Biol. Chem. , vol.280 , pp. 32594-32601
    • Zhang, Y.-M.1    Rock, C.O.2    Jackowski, S.3
  • 7
    • 0037193667 scopus 로고    scopus 로고
    • The murine Pank1 gene encodes two differentially regulated pantothenate kinase isozymes
    • Rock C.O., Karim M.A., Zhang Y.-M., and Jackowski S. The murine Pank1 gene encodes two differentially regulated pantothenate kinase isozymes. Gene 291 (2002) 35-43
    • (2002) Gene , vol.291 , pp. 35-43
    • Rock, C.O.1    Karim, M.A.2    Zhang, Y.-M.3    Jackowski, S.4
  • 8
    • 0028104163 scopus 로고
    • Kinetics and regulation of pantothenate kinase from Escherichia coli
    • Song W.-J., and Jackowski S. Kinetics and regulation of pantothenate kinase from Escherichia coli. J. Biol. Chem. 269 (1994) 27051-27058
    • (1994) J. Biol. Chem. , vol.269 , pp. 27051-27058
    • Song, W.-J.1    Jackowski, S.2
  • 9
    • 0023664065 scopus 로고
    • Regulation of pantothenate kinase by coenzyme A and its thioesters
    • Vallari D.S., Jackowski S., and Rock C.O. Regulation of pantothenate kinase by coenzyme A and its thioesters. J. Biol. Chem. 262 (1987) 2468-2471
    • (1987) J. Biol. Chem. , vol.262 , pp. 2468-2471
    • Vallari, D.S.1    Jackowski, S.2    Rock, C.O.3
  • 10
    • 0020130867 scopus 로고
    • Regulation of the biosynthesis of CoA at the level of pantothenate kinase
    • Halvorsen O., and Skrede S. Regulation of the biosynthesis of CoA at the level of pantothenate kinase. Eur. J. Biochem. 124 (1982) 211-215
    • (1982) Eur. J. Biochem. , vol.124 , pp. 211-215
    • Halvorsen, O.1    Skrede, S.2
  • 11
    • 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., Park H.-W., and Jackowski S. Role of feedback regulation of pantothenate kinase (CoaA) in the control of coenzyme A levels in Escherichia coli. J. Bacteriol. 185 (2003) 3410-3415
    • (2003) J. Bacteriol. , vol.185 , pp. 3410-3415
    • Rock, C.O.1    Park, H.-W.2    Jackowski, S.3
  • 13
    • 0842304656 scopus 로고    scopus 로고
    • PPARα controls the intracellular coenzyme A concentration via regulation of PANK1α gene expression
    • Ramaswamy G., Karim M.A., Murti K.G., and Jackowski S. PPARα controls the intracellular coenzyme A concentration via regulation of PANK1α gene expression. J. Lipid Res. 45 (2004) 17-31
    • (2004) J. Lipid Res. , vol.45 , pp. 17-31
    • Ramaswamy, G.1    Karim, M.A.2    Murti, K.G.3    Jackowski, S.4
  • 14
    • 0037322485 scopus 로고    scopus 로고
    • An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria
    • Hörtnagel K., Prokisch H., and Meitinger T. An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria. Hum. Mol. Genet. 12 (2003) 321-327
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 321-327
    • Hörtnagel, K.1    Prokisch, H.2    Meitinger, T.3
  • 16
    • 33644864274 scopus 로고    scopus 로고
    • Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration
    • Zhang Y.-M., Rock C.O., and Jackowski S. Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration. J. Biol. Chem. 281 (2006) 107-114
    • (2006) J. Biol. Chem. , vol.281 , pp. 107-114
    • Zhang, Y.-M.1    Rock, C.O.2    Jackowski, S.3
  • 17
    • 0018290370 scopus 로고
    • Clofibrate-induced increase in coenzyme A concentration in rat tissues
    • Voltti H., Savolainen M.J., Jauhonen V.P., and Hassinen I.E. Clofibrate-induced increase in coenzyme A concentration in rat tissues. Biochem. J. 182 (1979) 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
  • 18
    • 0018868147 scopus 로고
    • Regulation of coenzyme A biosynthesis by glucagon and glucocorticoid in adult rat liver parenchymal cells
    • Smith C.M., and Savage Jr. C.R. Regulation of coenzyme A biosynthesis by glucagon and glucocorticoid in adult rat liver parenchymal cells. Biochem. J. 188 (1980) 175-184
    • (1980) Biochem. J. , vol.188 , pp. 175-184
    • Smith, C.M.1    Savage Jr., C.R.2
  • 19
    • 0018225585 scopus 로고
    • The relationship between metabolic state and total CoA content of rat liver and heart
    • Smith C.M., Cano M.L., and Potyraj J. The relationship between metabolic state and total CoA content of rat liver and heart. J. Nutr. 108 (1978) 854-862
    • (1978) J. Nutr. , vol.108 , pp. 854-862
    • Smith, C.M.1    Cano, M.L.2    Potyraj, J.3
  • 20
    • 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 Grunnet N. The effect of acute and prolonged ethanol treatment on the contents of coenzyme A, carnitine and their derivatives in rat liver. Biochem. J. 132 (1973) 373-379
    • (1973) Biochem. J. , vol.132 , pp. 373-379
    • Kondrup, J.1    Grunnet, N.2
  • 21
    • 0022497626 scopus 로고
    • Effects of thyroid state and fasting on the concentrations of CoA and malonyl-CoA in rat liver
    • Lund H., Stakkestad J.A., and Skrede S. Effects of thyroid state and fasting on the concentrations of CoA and malonyl-CoA in rat liver. Biochim. Biophys. Acta 876 (1986) 685-687
    • (1986) Biochim. Biophys. Acta , vol.876 , pp. 685-687
    • Lund, H.1    Stakkestad, J.A.2    Skrede, S.3
  • 22
    • 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., Jauhonen V.P., and Hassinen I.E. Effects of clofibrate on ethanol-induced modifications in liver and adipose tissue metabolism: role of hepatic redox state and hormonal mechanisms. Biochem. Pharmacol. 26 (1977) 425-431
    • (1977) Biochem. Pharmacol. , vol.26 , pp. 425-431
    • Savolainen, M.J.1    Jauhonen, V.P.2    Hassinen, I.E.3
  • 23
    • 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., Bartlett K., Sherratt H.S.A., and Agius L. 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 (1988) 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
  • 24
    • 0018777097 scopus 로고
    • Increased biosynthesis of CoA in the liver of rats treated with clofibrate
    • Skrede S., and Halvorsen O. Increased biosynthesis of CoA in the liver of rats treated with clofibrate. Eur. J. Biochem. 98 (1979) 223-229
    • (1979) Eur. J. Biochem. , vol.98 , pp. 223-229
    • Skrede, S.1    Halvorsen, O.2
  • 25
    • 0020540019 scopus 로고
    • Effects of hypolipidemic drugs on hepatic CoA
    • Halvorsen O. Effects of hypolipidemic drugs on hepatic CoA. Biochem. Pharmacol. 32 (1983) 1126-1128
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 1126-1128
    • Halvorsen, O.1
  • 27
    • 0000302176 scopus 로고
    • Regulation of coenzyme A synthesis in heart muscle: effects of diabetes and fasting
    • Reibel D.K., Wyse B.W., Berkich D.A., and Neely J.R. Regulation of coenzyme A synthesis in heart muscle: effects of diabetes and fasting. Am. J. Physiol. 240 (1981) H606-H611
    • (1981) Am. J. Physiol. , vol.240
    • Reibel, D.K.1    Wyse, B.W.2    Berkich, D.A.3    Neely, J.R.4
  • 28
    • 1842504252 scopus 로고    scopus 로고
    • Mitochondrial localization of human PANK2 and hypotheses of secondary iron accumulation in pantothenate kinase-associated neurodegeneration
    • Johnson M.A., Kuo Y.M., Westaway S.K., Parker S.M., Ching K.H., Gitschier J., and Hayflick S.J. Mitochondrial localization of human PANK2 and hypotheses of secondary iron accumulation in pantothenate kinase-associated neurodegeneration. Ann. N Y Acad. Sci. 1012 (2004) 282-298
    • (2004) Ann. N Y Acad. Sci. , vol.1012 , pp. 282-298
    • Johnson, M.A.1    Kuo, Y.M.2    Westaway, S.K.3    Parker, S.M.4    Ching, K.H.5    Gitschier, J.6    Hayflick, S.J.7
  • 29
    • 12744280679 scopus 로고    scopus 로고
    • Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused by abnormal processing, stability, and catalytic activity of mutant pantothenate kinase 2
    • Kotzbauer P.T., Truax A.C., Trojanowski J.Q., and Lee V.M.Y. Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused by abnormal processing, stability, and catalytic activity of mutant pantothenate kinase 2. J. Neurosci. 25 (2005) 689-698
    • (2005) J. Neurosci. , vol.25 , pp. 689-698
    • Kotzbauer, P.T.1    Truax, A.C.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 32
    • 0027536871 scopus 로고
    • Glucose counterregulation: prevention and correction of hypoglycemia in humans
    • Cryer P.E. Glucose counterregulation: prevention and correction of hypoglycemia in humans. Am. J. Physiol. 264 (1993) E149-E155
    • (1993) Am. J. Physiol. , vol.264
    • Cryer, P.E.1
  • 33
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: a practical and powerful approach to multiple testing
    • Benjamini Y., and Hochberg Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc. [Ser. B] 57 (1995) 289-300
    • (1995) J. R. Stat. Soc. [Ser. B] , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 34
    • 27544473473 scopus 로고    scopus 로고
    • Quantitative trait loci analysis using the false discovery rate
    • Benjamini Y., and Yekutieli D. Quantitative trait loci analysis using the false discovery rate. Genetics 171 (2005) 783-790
    • (2005) Genetics , vol.171 , pp. 783-790
    • Benjamini, Y.1    Yekutieli, D.2
  • 36
    • 4444311812 scopus 로고    scopus 로고
    • Carnitine acyltransferases and their influence on CoA pools in health and disease
    • Ramsay R.R., and Zammit V.A. Carnitine acyltransferases and their influence on CoA pools in health and disease. Mol. Aspects Med. 25 (2004) 475-493
    • (2004) Mol. Aspects Med. , vol.25 , pp. 475-493
    • Ramsay, R.R.1    Zammit, V.A.2
  • 38
    • 0036370558 scopus 로고    scopus 로고
    • Mouse models for disorders of mitochondrial fatty acid β-oxidation
    • Schuler A.M., and Wood P.A. Mouse models for disorders of mitochondrial fatty acid β-oxidation. ILAR J. 43 (2002) 57-65
    • (2002) ILAR J. , vol.43 , pp. 57-65
    • Schuler, A.M.1    Wood, P.A.2
  • 39
    • 0036125848 scopus 로고    scopus 로고
    • Acylcarnitine profiles in fibroblasts from patients with respiratory chain defects can resemble those from patients with mitochondrial fatty acid β-oxidation disorders
    • Sim K.G., Carpenter K., Hammond J., Christodoulou J., and Wilcken B. Acylcarnitine profiles in fibroblasts from patients with respiratory chain defects can resemble those from patients with mitochondrial fatty acid β-oxidation disorders. Metabolism 51 (2002) 366-371
    • (2002) Metabolism , vol.51 , pp. 366-371
    • Sim, K.G.1    Carpenter, K.2    Hammond, J.3    Christodoulou, J.4    Wilcken, B.5
  • 40
    • 0036062553 scopus 로고    scopus 로고
    • Strategies for the diagnosis of mitochondrial fatty acid β-oxidation disorders
    • Sim K.G., Hammond J., and Wilcken B. Strategies for the diagnosis of mitochondrial fatty acid β-oxidation disorders. Clin. Chim. Acta 323 (2002) 37-58
    • (2002) Clin. Chim. Acta , vol.323 , pp. 37-58
    • Sim, K.G.1    Hammond, J.2    Wilcken, B.3
  • 41
    • 0035397652 scopus 로고    scopus 로고
    • The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives
    • Gasmi L., and McLennan A.G. The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives. Biochem. J. 357 (2001) 33-38
    • (2001) Biochem. J. , vol.357 , pp. 33-38
    • Gasmi, L.1    McLennan, A.G.2
  • 42
    • 30744471923 scopus 로고    scopus 로고
    • Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity
    • Ofman R., Speijer D., Leen R., and Wanders R.J. Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity. Biochem. J. 393 (2006) 537-543
    • (2006) Biochem. J. , vol.393 , pp. 537-543
    • Ofman, R.1    Speijer, D.2    Leen, R.3    Wanders, R.J.4
  • 43
    • 33947226983 scopus 로고
    • A double-blind controlled study of Ca hopantenate and placebo in conformity to a rating list for the evaluation of the abnormal behaviors in children (III)
    • Task Force for Evaluation of Children's Behaviors
    • Task Force for Evaluation of Children's Behaviors. A double-blind controlled study of Ca hopantenate and placebo in conformity to a rating list for the evaluation of the abnormal behaviors in children (III). Rinsho Hyoka 2 (1974) 375-384
    • (1974) Rinsho Hyoka , vol.2 , pp. 375-384
  • 44
    • 0025923570 scopus 로고
    • Acute encephalopathy with hepatic steatosis induced by pantothenic acid antagonist, calcium hopantenate, in dogs
    • Noda S., Haratake J., Sasaki A., Ishii N., Umezaki H., and Horie A. Acute encephalopathy with hepatic steatosis induced by pantothenic acid antagonist, calcium hopantenate, in dogs. Liver 11 (1991) 134-142
    • (1991) Liver , vol.11 , pp. 134-142
    • Noda, S.1    Haratake, J.2    Sasaki, A.3    Ishii, N.4    Umezaki, H.5    Horie, A.6
  • 45
    • 0024324069 scopus 로고
    • Metabolic acidosis and hypoglycemia during calcium hopantenate administration-report on 5 patients
    • Ohsuga S., Ohsuga H., Takeoka T., Ikeda A., and Shinohara Y. Metabolic acidosis and hypoglycemia during calcium hopantenate administration-report on 5 patients. Rinsho Shinkeigaku 29 (1989) 741-746
    • (1989) Rinsho Shinkeigaku , vol.29 , pp. 741-746
    • Ohsuga, S.1    Ohsuga, H.2    Takeoka, T.3    Ikeda, A.4    Shinohara, Y.5
  • 46
    • 0025318678 scopus 로고
    • Urinary organic acids in elderly Japanese patients with ketosis and encephalopathy who have taken panto-yl-γ-aminobutyrate, calcium salt (calcium hopantenate, HOPA)
    • Nakanishi T., Funahashi S., Shimizu A., and Hayashi A. Urinary organic acids in elderly Japanese patients with ketosis and encephalopathy who have taken panto-yl-γ-aminobutyrate, calcium salt (calcium hopantenate, HOPA). Clin. Chim. Acta 188 (1990) 85-90
    • (1990) Clin. Chim. Acta , vol.188 , pp. 85-90
    • Nakanishi, T.1    Funahashi, S.2    Shimizu, A.3    Hayashi, A.4
  • 47
    • 0025355832 scopus 로고
    • Mass spectrometric identification of 2-hydroxydodecanedioic acid and its homologues in urine from patients with hopantenate therapy during clinical episode
    • Matsumoto M., Kuhara T., Inoue Y., Shinka T., Matsumoto I., and Kajita M. Mass spectrometric identification of 2-hydroxydodecanedioic acid and its homologues in urine from patients with hopantenate therapy during clinical episode. Biomed. Environ. Mass Spectrom. 19 (1990) 171-175
    • (1990) Biomed. Environ. Mass Spectrom. , vol.19 , pp. 171-175
    • Matsumoto, M.1    Kuhara, T.2    Inoue, Y.3    Shinka, T.4    Matsumoto, I.5    Kajita, M.6
  • 48
    • 0026023966 scopus 로고
    • Abnormal fatty acid metabolism in patients in hopantenate therapy during clinical episodes
    • Matsumoto M., Kuhara T., Inoue Y., Shinka T., and Matsumoto I. Abnormal fatty acid metabolism in patients in hopantenate therapy during clinical episodes. J. Chromatogr. 562 (1991) 139-145
    • (1991) J. Chromatogr. , vol.562 , pp. 139-145
    • Matsumoto, M.1    Kuhara, T.2    Inoue, Y.3    Shinka, T.4    Matsumoto, I.5
  • 49
    • 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. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 50
    • 0028146621 scopus 로고
    • Coordination of membrane phospholipid synthesis with the cell cycle
    • Jackowski S. Coordination of membrane phospholipid synthesis with the cell cycle. J. Biol. Chem. 269 (1994) 3858-3867
    • (1994) J. Biol. Chem. , vol.269 , pp. 3858-3867
    • Jackowski, S.1
  • 53
    • 0023818508 scopus 로고
    • A radioisotopic assay of picomolar concentrations of coenzyme A in liver tissue
    • Knights K.M., and Drew R. A radioisotopic assay of picomolar concentrations of coenzyme A in liver tissue. Anal. Biochem. 168 (1988) 94-99
    • (1988) Anal. Biochem. , vol.168 , pp. 94-99
    • Knights, K.M.1    Drew, R.2


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