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Volumn 7, Issue 7, 2012, Pages

Germline deletion of pantothenate kinases 1 and 2 reveals the key roles for CoA in postnatal metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A DESATURASE; ARACHIDONIC ACID; COENZYME A; DOCOSAHEXAENOIC ACID; KETONE; LINOLEIC ACID; MYRISTIC ACID; OLEIC ACID; PALMITIC ACID; PALMITOLEIC ACID; PANTOTHENATE KINASE; PANTOTHENATE KINASE 1; PANTOTHENATE KINASE 2; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STEARIC ACID; TRIACYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 84864005176     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040871     Document Type: Article
Times cited : (62)

References (42)
  • 2
    • 0037193667 scopus 로고    scopus 로고
    • The murine Pank1 gene encodes two differentially regulated pantothenate kinase isozymes
    • Rock CO, Karim MA, Zhang Y-M, Jackowski S, (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
  • 3
    • 0034935036 scopus 로고    scopus 로고
    • A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome
    • Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, et al. (2001) A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet 28: 345-349.
    • (2001) Nat Genet , vol.28 , pp. 345-349
    • Zhou, B.1    Westaway, S.K.2    Levinson, B.3    Johnson, M.A.4    Gitschier, J.5
  • 4
    • 25444432519 scopus 로고    scopus 로고
    • Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters
    • Zhang Y-M, Rock CO, Jackowski S, (2005) Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters. J Biol Chem 280: 32594-32601.
    • (2005) J Biol Chem , vol.280 , pp. 32594-32601
    • Zhang, Y.-M.1    Rock, C.O.2    Jackowski, S.3
  • 5
    • 67349203977 scopus 로고    scopus 로고
    • Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces cerevisiae: identification of a conditional mutation in the pantothenate kinase gene CAB1
    • Olzhausen J, Schubbe S, Schuller HJ, (2009) Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces cerevisiae: identification of a conditional mutation in the pantothenate kinase gene CAB1. Curr Genet 55: 163-173.
    • (2009) Curr Genet , vol.55 , pp. 163-173
    • Olzhausen, J.1    Schubbe, S.2    Schuller, H.J.3
  • 6
    • 0033593330 scopus 로고    scopus 로고
    • Cloning and characterization of a eukaryotic pantothenate kinase gene (panK) from Aspergillus nidulans
    • Calder RB, Williams RSB, Ramaswamy G, Rock CO, Campbell E, et al. (1999) Cloning and characterization of a eukaryotic pantothenate kinase gene (panK) from Aspergillus nidulans. J Biol Chem 274: 2014-2020.
    • (1999) J Biol Chem , vol.274 , pp. 2014-2020
    • Calder, R.B.1    Williams, R.S.B.2    Ramaswamy, G.3    Rock, C.O.4    Campbell, E.5
  • 7
    • 0035100102 scopus 로고    scopus 로고
    • fumble encodes a pantothenate kinase homolog required for proper mitosis and meiosis in Drosophila melanogaster
    • Afshar K, Gonczy P, DiNardo S, Wasserman SA, (2001) fumble encodes a pantothenate kinase homolog required for proper mitosis and meiosis in Drosophila melanogaster. Genetics 157: 1267-1276.
    • (2001) Genetics , vol.157 , pp. 1267-1276
    • Afshar, K.1    Gonczy, P.2    DiNardo, S.3    Wasserman, S.A.4
  • 8
    • 33947241895 scopus 로고    scopus 로고
    • Chemical knockout of pantothenate kinase reveals the metabolic and genetic program responsible for hepatic coenzyme A homeostasis
    • Zhang YM, Chohnan S, Virga KG, Stevens RD, Ilkayeva OR, et al. (2007) Chemical knockout of pantothenate kinase reveals the metabolic and genetic program responsible for hepatic coenzyme A homeostasis. Chem Biol 14: 291-302.
    • (2007) Chem Biol , vol.14 , pp. 291-302
    • Zhang, Y.M.1    Chohnan, S.2    Virga, K.G.3    Stevens, R.D.4    Ilkayeva, O.R.5
  • 9
    • 77956223798 scopus 로고    scopus 로고
    • Pantothenate kinase 1 is required to support the metabolic transition from the fed to the fasted state
    • Leonardi R, Rehg JE, Rock CO, Jackowski S, (2010) Pantothenate kinase 1 is required to support the metabolic transition from the fed to the fasted state. PLoS ONE 5: e11107.
    • (2010) PLoS ONE , vol.5
    • Leonardi, R.1    Rehg, J.E.2    Rock, C.O.3    Jackowski, S.4
  • 10
    • 33846818915 scopus 로고    scopus 로고
    • Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine
    • Leonardi R, Rock CO, Jackowski S, Zhang Y-M, (2007) Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine. Proc Natl Acad Sci U S A 104: 1494-1499.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1494-1499
    • Leonardi, R.1    Rock, C.O.2    Jackowski, S.3    Zhang, Y.-M.4
  • 12
    • 12344334370 scopus 로고    scopus 로고
    • Deficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia
    • Kuo YM, Duncan JL, Westaway SK, Yang H, Nune G, et al. (2005) Deficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia. Hum Mol Genet 14: 49-57.
    • (2005) Hum Mol Genet , vol.14 , pp. 49-57
    • Kuo, Y.M.1    Duncan, J.L.2    Westaway, S.K.3    Yang, H.4    Nune, G.5
  • 13
    • 0035957936 scopus 로고    scopus 로고
    • Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria
    • Strauss E, Kinsland C, Ge Y, McLafferty FW, Begley TP, (2001) Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria. J Biol Chem 276: 13513-13516.
    • (2001) J Biol Chem , vol.276 , pp. 13513-13516
    • Strauss, E.1    Kinsland, C.2    Ge, Y.3    McLafferty, F.W.4    Begley, T.P.5
  • 14
    • 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 CO, Jackowski S, (2006) Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration. J Biol Chem 281: 107-114.
    • (2006) J Biol Chem , vol.281 , pp. 107-114
    • Zhang, Y.-M.1    Rock, C.O.2    Jackowski, S.3
  • 15
    • 34948897631 scopus 로고    scopus 로고
    • Crystal structures of human pantothenate kinases. Insights into allosteric regulation and mutations linked to a neurodegeneration disorder
    • Hong BS, Senisterra G, Rabeh WM, Vedadi M, Leonardi R, et al. (2007) Crystal structures of human pantothenate kinases. Insights into allosteric regulation and mutations linked to a neurodegeneration disorder. J Biol Chem 282: 27984-27993.
    • (2007) J Biol Chem , vol.282 , pp. 27984-27993
    • Hong, B.S.1    Senisterra, G.2    Rabeh, W.M.3    Vedadi, M.4    Leonardi, R.5
  • 16
    • 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 PT, Truax AC, Trojanowski JQ, Lee VMY, (2005) 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: 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
  • 17
    • 34249999964 scopus 로고    scopus 로고
    • Deprivation of pantothenic acid elicits a movement disorder and azoospermia in a mouse model of pantothenate kinase-associated neurodegeneration
    • Kuo YM, Hayflick SJ, Gitschier J, (2007) Deprivation of pantothenic acid elicits a movement disorder and azoospermia in a mouse model of pantothenate kinase-associated neurodegeneration. J Inherit Metab Dis 30: 310-317.
    • (2007) J Inherit Metab Dis , vol.30 , pp. 310-317
    • Kuo, Y.M.1    Hayflick, S.J.2    Gitschier, J.3
  • 18
    • 0032531101 scopus 로고    scopus 로고
    • Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation
    • Ibdah JA, Tein I, Dionisi-Vici C, Bennett MJ, Ijlst L, et al. (1998) Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation. J Clin Invest 102: 1193-1199.
    • (1998) J Clin Invest , vol.102 , pp. 1193-1199
    • Ibdah, J.A.1    Tein, I.2    Dionisi-Vici, C.3    Bennett, M.J.4    Ijlst, L.5
  • 19
    • 55349090314 scopus 로고    scopus 로고
    • The nudix hydrolase 7 is an acyl-CoA diphosphatase involved in regulating peroxisomal coenzyme A homeostasis
    • Reilly SJ, Tillander V, Ofman R, Alexson SE, Hunt MC, (2008) The nudix hydrolase 7 is an acyl-CoA diphosphatase involved in regulating peroxisomal coenzyme A homeostasis. J Biochem 144: 655-663.
    • (2008) J Biochem , vol.144 , pp. 655-663
    • Reilly, S.J.1    Tillander, V.2    Ofman, R.3    Alexson, S.E.4    Hunt, M.C.5
  • 20
    • 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, Wanders RJ, (2006) Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity. Biochem J 393: 537-543.
    • (2006) Biochem J , vol.393 , pp. 537-543
    • Ofman, R.1    Speijer, D.2    Leen, R.3    Wanders, R.J.4
  • 21
    • 0035397652 scopus 로고    scopus 로고
    • The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives
    • Gasmi L, McLennan AG, (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
  • 22
    • 34347259219 scopus 로고    scopus 로고
    • ERRgamma directs and maintains the transition to oxidative metabolism in the postnatal heart
    • Alaynick WA, Kondo RP, Xie W, He W, Dufour CR, et al. (2007) ERRgamma directs and maintains the transition to oxidative metabolism in the postnatal heart. Cell Metab 6: 13-24.
    • (2007) Cell Metab , vol.6 , pp. 13-24
    • Alaynick, W.A.1    Kondo, R.P.2    Xie, W.3    He, W.4    Dufour, C.R.5
  • 23
    • 0036364560 scopus 로고    scopus 로고
    • Energy metabolism in the brain
    • Hertz L, Dienel GA, (2002) Energy metabolism in the brain. Int Rev Neurobiol 51: 1-102.
    • (2002) Int Rev Neurobiol , vol.51 , pp. 1-102
    • Hertz, L.1    Dienel, G.A.2
  • 24
    • 0023470792 scopus 로고
    • Capacity for substrate utilization in oxidative metabolism by neurons, astrocytes, and oligodendrocytes from developing brain in primary culture
    • Edmond J, Robbins RA, Bergstrom JD, Cole RA, de VJ, (1987) Capacity for substrate utilization in oxidative metabolism by neurons, astrocytes, and oligodendrocytes from developing brain in primary culture. J Neurosci Res 18: 551-561.
    • (1987) J Neurosci Res , vol.18 , pp. 551-561
    • Edmond, J.1    Robbins, R.A.2    Bergstrom, J.D.3    Cole, R.A.4    de, V.J.5
  • 25
    • 0022528413 scopus 로고
    • Glucose carbon recycling and oxidation in human newborns
    • Denne SC, Kalhan SC, (1986) Glucose carbon recycling and oxidation in human newborns. Am J Physiol 251: E71-E77.
    • (1986) Am J Physiol , vol.251
    • Denne, S.C.1    Kalhan, S.C.2
  • 27
    • 0016797754 scopus 로고
    • Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios
    • Pettit FH, Pelley JW, Reed LJ, (1975) Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios. Biochem Biophys Res Commun 65: 575-582.
    • (1975) Biochem Biophys Res Commun , vol.65 , pp. 575-582
    • Pettit, F.H.1    Pelley, J.W.2    Reed, L.J.3
  • 28
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin SJ, Ford E, Haigis M, Liszt G, Guarente L, (2004) Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev 18: 12-16.
    • (2004) Genes Dev , vol.18 , pp. 12-16
    • Lin, S.J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 29
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows WC, Lee S, Denu JM, (2006) Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc Natl Acad Sci U S A 103: 10230-10235.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 31
    • 78649482634 scopus 로고    scopus 로고
    • SIRT1: recent lessons from mouse models
    • Herranz D, Serrano M, (2010) SIRT1: recent lessons from mouse models. Nat Rev Cancer 10: 819-823.
    • (2010) Nat Rev Cancer , vol.10 , pp. 819-823
    • Herranz, D.1    Serrano, M.2
  • 32
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao S, Xu W, Jiang W, Yu W, Lin Y, et al. (2010) Regulation of cellular metabolism by protein lysine acetylation. Science 327: 1000-1004.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3    Yu, W.4    Lin, Y.5
  • 33
    • 82955214822 scopus 로고    scopus 로고
    • Impaired Coenzyme A metabolism affects histone and tubulin acetylation in Drosophila and human cell models of pantothenate kinase associated neurodegeneration
    • Siudeja K, Srinivasan B, Xu L, Rana A, de JJ, et al. (2011) Impaired Coenzyme A metabolism affects histone and tubulin acetylation in Drosophila and human cell models of pantothenate kinase associated neurodegeneration. EMBO Mol Med 3: 1-12.
    • (2011) EMBO Mol Med , vol.3 , pp. 1-12
    • Siudeja, K.1    Srinivasan, B.2    Xu, L.3    Rana, A.4    de, J.J.5
  • 34
    • 84867420625 scopus 로고    scopus 로고
    • On Acetyl-CoA as a Gauge of Cellular Metabolic State
    • (in press)
    • Cai L, Tu BP, (2011) On Acetyl-CoA as a Gauge of Cellular Metabolic State. Cold Spring Harb Symp Quant Biol (in press).
    • (2011) Cold Spring Harb Symp Quant Biol
    • Cai, L.1    Tu, B.P.2
  • 36
    • 1842504252 scopus 로고    scopus 로고
    • Mitochondrial localization of human PANK2 and hypotheses of secondary iron accumulation in pantothenate kinase-associated neurodegeneration
    • Johnson MA, Kuo YM, Westaway SK, Parker SM, Ching KH, et al. (2004) Mitochondrial localization of human PANK2 and hypotheses of secondary iron accumulation in pantothenate kinase-associated neurodegeneration. Ann N Y Acad Sci 1012: 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
  • 37
    • 79959262895 scopus 로고    scopus 로고
    • Gene expression biomarkers in the brain of a mouse model for Alzheimer's disease: mining of microarray data by logic classification and feature selection
    • Arisi I, D'Onofrio M, Brandi R, Felsani A, Capsoni S, et al. (2011) Gene expression biomarkers in the brain of a mouse model for Alzheimer's disease: mining of microarray data by logic classification and feature selection. J Alzheimers Dis 24: 721-738.
    • (2011) J Alzheimers Dis , vol.24 , pp. 721-738
    • Arisi, I.1    D'Onofrio, M.2    Brandi, R.3    Felsani, A.4    Capsoni, S.5
  • 38
    • 0033562350 scopus 로고    scopus 로고
    • Development and validation of real-time quantitative reverse transcriptase-polymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro
    • Winer J, Jung CK, Shackel I, Williams PM, (1999) Development and validation of real-time quantitative reverse transcriptase-polymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro. Anal Biochem 270: 41-49.
    • (1999) Anal Biochem , vol.270 , pp. 41-49
    • Winer, J.1    Jung, C.K.2    Shackel, I.3    Williams, P.M.4
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (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
  • 40
    • 41249101849 scopus 로고    scopus 로고
    • Glycerophospholipid identification and quantitation by electrospray ionization mass spectrometry
    • Ivanova PT, Milne SB, Byrne MO, Xiang Y, Brown HA, (2007) Glycerophospholipid identification and quantitation by electrospray ionization mass spectrometry. Methods Enzymol 432: 21-57.
    • (2007) Methods Enzymol , vol.432 , pp. 21-57
    • Ivanova, P.T.1    Milne, S.B.2    Byrne, M.O.3    Xiang, Y.4    Brown, H.A.5
  • 41
    • 0030956407 scopus 로고    scopus 로고
    • Hepatic fatty acid metabolism in pigs and rats: major differences in endproducts, O2 uptake, and ß-oxidation
    • Adams SH, Lin X, Yu XX, Odle J, Drackley JK, (1997) Hepatic fatty acid metabolism in pigs and rats: major differences in endproducts, O2 uptake, and ß-oxidation. Am J Physiol 272: R1641-R1646.
    • (1997) Am J Physiol , vol.272
    • Adams, S.H.1    Lin, X.2    Yu, X.X.3    Odle, J.4    Drackley, J.K.5
  • 42
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ, (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37: 911-917.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2


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