메뉴 건너뛰기




Volumn 402, Issue 1, 2010, Pages 158-162

Coenzyme A and its thioester pools in fasted and fed rat tissues

Author keywords

Acetyl CoA; Brain; CoA metabolism; Coenzyme A; Malonyl CoA; Rats

Indexed keywords

ACETYL COENZYME A; COENZYME A; LONG CHAIN FATTY ACID COENZYME A LIGASE; MALONYL COENZYME A; THIOESTER;

EID: 78049312280     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.10.009     Document Type: Article
Times cited : (21)

References (35)
  • 1
    • 0002562806 scopus 로고
    • Metabolism of Coenzyme A
    • Academic Press, New York, D.S. Greenberg (Ed.)
    • Abiko Y. Metabolism of Coenzyme A. Metabolic Pathway 1975, 1-25. Academic Press, New York. D.S. Greenberg (Ed.).
    • (1975) Metabolic Pathway , pp. 1-25
    • Abiko, Y.1
  • 3
    • 0011531565 scopus 로고
    • Immobilized coenzymes and derivatives
    • Academic Press, New York, J. Everse, B. Anderson, K. You (Eds.)
    • Lee C.H., Chen A.F. Immobilized coenzymes and derivatives. The pyridine nucleotide coenzymes 1982, 189. Academic Press, New York. J. Everse, B. Anderson, K. You (Eds.).
    • (1982) The pyridine nucleotide coenzymes , pp. 189
    • Lee, C.H.1    Chen, A.F.2
  • 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., Jackowski S. Pantothenate kinase regulation of the intracellular concentration of coenzyme A. J. Biol. Chem. 2000, 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
  • 5
    • 0037193667 scopus 로고    scopus 로고
    • The murine pantothenate kinase (PanK1) gene encodes two differentially regulated pantothenate kinase isozymes
    • Rock C.O., Karim M.A., Zhang Y.-M., Jackowski S. The murine pantothenate kinase (PanK1) gene encodes two differentially regulated pantothenate kinase isozymes. Gene 2002, 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
  • 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., Jackowski S. Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters. J. Biol. Chem. 2005, 280:32594-32601.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32594-32601
    • Zhang, Y.-M.1    Rock, C.O.2    Jackowski, S.3
  • 7
    • 33644864274 scopus 로고    scopus 로고
    • Biochemical properties of human pantothenate kinase 2 isoformes and mutations linked to pantothenate kinase-associated neurodegeneration
    • Zhang Y.-M., Rock C.O., Jackowski S. Biochemical properties of human pantothenate kinase 2 isoformes and mutations linked to pantothenate kinase-associated neurodegeneration. J. Biol. Chem. 2006, 281:107-114.
    • (2006) J. Biol. Chem. , vol.281 , pp. 107-114
    • Zhang, Y.-M.1    Rock, C.O.2    Jackowski, S.3
  • 8
    • 33846818915 scopus 로고    scopus 로고
    • Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine
    • Leonardi R., Rock C.O., Jackowski S., Zhang Y.-M. Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine. Proc. Natl. Acad. Sci. USA 2007, 104:1494-1499.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1494-1499
    • Leonardi, R.1    Rock, C.O.2    Jackowski, S.3    Zhang, Y.-M.4
  • 10
    • 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 J.E., Rock C.O., Jackowski S. Pantothenate kinase 1 is required to support the metabolic transition from the fed to the fasted state. PLos One 2010, 5:e11107.
    • (2010) PLos One , vol.5
    • Leonardi, R.1    Rehg, J.E.2    Rock, C.O.3    Jackowski, S.4
  • 11
    • 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., 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. 1973, 132:373-379.
    • (1973) Biochem. J. , vol.132 , pp. 373-379
    • Kondrup, J.1    Grunnet, N.2
  • 12
    • 0017824474 scopus 로고
    • Coenzyme A and carnitine distribution in normal and ischemic hearts
    • Idell-Wenger J.A., Grotyohann L.W., Neely J.R. Coenzyme A and carnitine distribution in normal and ischemic hearts. J. Biol. Chem. 1978, 253:4310-4318.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4310-4318
    • Idell-Wenger, J.A.1    Grotyohann, L.W.2    Neely, J.R.3
  • 13
    • 0018225585 scopus 로고
    • The relationship between metabolic state and total CoA content of rat liver and heart
    • Smith C.M., Cano M.L., Potyraj J. The relationship between metabolic state and total CoA content of rat liver and heart. J. Nutr. 1978, 108:854-862.
    • (1978) J. Nutr. , vol.108 , pp. 854-862
    • Smith, C.M.1    Cano, M.L.2    Potyraj, J.3
  • 14
    • 0018290370 scopus 로고
    • Clofibrate-induced increase in coenzyme A concentration in rat tissues
    • Voltti H., Savolainen M.J., Jauhonen V.P., Hassinen I.E. Clofibrate-induced increase in coenzyme A concentration in rat tissues. Biochem. J. 1979, 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
  • 15
    • 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., Skrede S. Effects of thyroid state and fasting on the concentrations of CoA and malonyl-CoA in rat liver. Biochim. Biophys. Acta 1986, 876:685-687.
    • (1986) Biochim. Biophys. Acta , vol.876 , pp. 685-687
    • Lund, H.1    Stakkestad, J.A.2    Skrede, S.3
  • 16
    • 0242300121 scopus 로고    scopus 로고
    • Hypothalamic malonyl-CoA as a mediator of feeding behavior
    • Hu Z., Cha S.H., Chohnan S., Lane M.D. Hypothalamic malonyl-CoA as a mediator of feeding behavior. Proc. Natl. Acad. Sci. USA 2003, 100:12624-12629.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12624-12629
    • Hu, Z.1    Cha, S.H.2    Chohnan, S.3    Lane, M.D.4
  • 17
    • 26844446285 scopus 로고    scopus 로고
    • Inhibition of hypothalamic fatty acid synthase triggers rapid activation of fatty acid oxidation in skeletal muscle
    • Cha S.H., Hu Z., Chohnan S., Lane M.D. Inhibition of hypothalamic fatty acid synthase triggers rapid activation of fatty acid oxidation in skeletal muscle. Proc. Natl. Acad. Sci. USA 2005, 102:14557-14562.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14557-14562
    • Cha, S.H.1    Hu, Z.2    Chohnan, S.3    Lane, M.D.4
  • 18
    • 28844433549 scopus 로고    scopus 로고
    • A role for hypothalamic malonyl-CoA in the control of food intake
    • Hu Z., Dai Y., Prentki M., Chohnan S., Lane M.D. A role for hypothalamic malonyl-CoA in the control of food intake. J. Biol. Chem. 2005, 280:39681-39683.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39681-39683
    • Hu, Z.1    Dai, Y.2    Prentki, M.3    Chohnan, S.4    Lane, M.D.5
  • 19
    • 33750354533 scopus 로고    scopus 로고
    • Hypothalamic malonyl-CoA triggers mitochondrial biogenesis and oxidative gene expression in skeletal muscle: role of PGC-1α
    • Cha S.-H., Rodgers J.T., Puigserver P., Chohnan S., Lane M.D. Hypothalamic malonyl-CoA triggers mitochondrial biogenesis and oxidative gene expression in skeletal muscle: role of PGC-1α. Proc. Natl. Acad. Sci. USA 2006, 103:15410-15415.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15410-15415
    • Cha, S.-H.1    Rodgers, J.T.2    Puigserver, P.3    Chohnan, S.4    Lane, M.D.5
  • 20
    • 33845998567 scopus 로고    scopus 로고
    • The role of hypothalamic malonyl-CoA in energy homeostasis
    • Wolfgang M.J., Lane M.D. The role of hypothalamic malonyl-CoA in energy homeostasis. J. Biol. Chem. 2006, 281:37265-37269.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37265-37269
    • Wolfgang, M.J.1    Lane, M.D.2
  • 24
    • 55949086381 scopus 로고    scopus 로고
    • Differential effects of central fructose and glucose on hypothalamic malonyl-CoA and food intake
    • Cha S.H., Wolfgang M., Tokutake Y., Chohnan S., Lane M.D. Differential effects of central fructose and glucose on hypothalamic malonyl-CoA and food intake. Proc. Natl. Acad. Sci. USA 2008, 105:16871-16875.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16871-16875
    • Cha, S.H.1    Wolfgang, M.2    Tokutake, Y.3    Chohnan, S.4    Lane, M.D.5
  • 26
    • 77956201747 scopus 로고    scopus 로고
    • A ketone ester diet increased brain malonyl CoA and uncoupling proteion 4 and 5 while decreasing food intake in the normal Wistar rat
    • Kashiwaya Y., Pawlosky R., Markis W., King M.T., Bergman C., Srivastava S., Murray A., Clarke K., Veech R.L. A ketone ester diet increased brain malonyl CoA and uncoupling proteion 4 and 5 while decreasing food intake in the normal Wistar rat. J. Biol. Chem. 2010, 285:25950-25956.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25950-25956
    • Kashiwaya, Y.1    Pawlosky, R.2    Markis, W.3    King, M.T.4    Bergman, C.5    Srivastava, S.6    Murray, A.7    Clarke, K.8    Veech, R.L.9
  • 27
    • 0021986942 scopus 로고
    • Malonyl-CoA:acetyl-CoA cycling. A new micromethod for determination of acyl-CoAs with malonate decarboxylase
    • Takamura Y., Kitayama Y., Arakawa A., Yamanaka S., Tosaki M., Ogawa Y. Malonyl-CoA:acetyl-CoA cycling. A new micromethod for determination of acyl-CoAs with malonate decarboxylase. Biochim. Biophys. Acta 1985, 834:1-7.
    • (1985) Biochim. Biophys. Acta , vol.834 , pp. 1-7
    • Takamura, Y.1    Kitayama, Y.2    Arakawa, A.3    Yamanaka, S.4    Tosaki, M.5    Ogawa, Y.6
  • 28
    • 0039801029 scopus 로고
    • A simple micromethod for measurement of CoASH and short chain acyl-CoAs in Escherichia coli K12 cells
    • Chohnan S., Takamura Y. A simple micromethod for measurement of CoASH and short chain acyl-CoAs in Escherichia coli K12 cells. Agric. Biol. Chem. 1991, 55:87-94.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 87-94
    • Chohnan, S.1    Takamura, Y.2
  • 29
    • 0030998697 scopus 로고    scopus 로고
    • Changes in the size and composition of intracellular pools of nonesterified coenzyme A and coenzyme A thioesters in aerobic and facultatively anaerobic bacteria
    • Chohnan S., Furukawa H., Fujio T., Nishihara H., Takamura Y. Changes in the size and composition of intracellular pools of nonesterified coenzyme A and coenzyme A thioesters in aerobic and facultatively anaerobic bacteria. Appl. Environ. Microbiol. 1997, 63:553-560.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 553-560
    • Chohnan, S.1    Furukawa, H.2    Fujio, T.3    Nishihara, H.4    Takamura, Y.5
  • 30
    • 84964487952 scopus 로고    scopus 로고
    • Malonate decarboxylase in bacteria and its application for determination of intracellular acyl-CoA thioesters
    • Chohnan S., Takamura Y. Malonate decarboxylase in bacteria and its application for determination of intracellular acyl-CoA thioesters. Microbes Environ. 2004, 19:179-189.
    • (2004) Microbes Environ. , vol.19 , pp. 179-189
    • Chohnan, S.1    Takamura, Y.2
  • 31
    • 0013471331 scopus 로고
    • Purification and some properties of malonate decarboxylase from Pseudomonas ovalis, an oligomeric enzyme with bifunctional properties
    • Takamura Y., Kitayama Y. Purification and some properties of malonate decarboxylase from Pseudomonas ovalis, an oligomeric enzyme with bifunctional properties. Biochem. Int. 1981, 3:483-491.
    • (1981) Biochem. Int. , vol.3 , pp. 483-491
    • Takamura, Y.1    Kitayama, Y.2
  • 32
    • 0035397652 scopus 로고    scopus 로고
    • The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives
    • Gasmi I., McLeman A.G. The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives. Biochem. J. 2001, 357:33-38.
    • (2001) Biochem. J. , vol.357 , pp. 33-38
    • Gasmi, I.1    McLeman, A.G.2
  • 34
    • 55349090314 scopus 로고    scopus 로고
    • The nudix hydrolase 7 is an acyl-CoA diphosphatase involved in regulating peroxisomal coenzyme A homeostasis
    • Reilly S.J., Tillander V., Ofman R., Alexson S.E., Hunt M.C. The nudix hydrolase 7 is an acyl-CoA diphosphatase involved in regulating peroxisomal coenzyme A homeostasis. J. Biochem. 2008, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.