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Volumn 147, Issue 2, 2007, Pages 278-287

Chicken liver and muscle carnitine palmitoyltransferase 1: Nutritional regulation of messengers

Author keywords

Carnitine palmitoyltransferase 1; Chicken; Fasting; Metabolism; Succinyl CoA:3 ketoacid CoA transferase; Hydroxyacyl CoA dehydrogenase

Indexed keywords

3 OXOACID COENZYME A TRANSFERASE; CARNITINE PALMITOYLTRANSFERASE; COMPLEMENTARY DNA; ENOYL COENZYME A HYDRATASE; ISOENZYME; KETONE BODY; LIVER ENZYME; MESSENGER RNA; MUSCLE ENZYME;

EID: 34147168667     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2007.01.007     Document Type: Article
Times cited : (40)

References (44)
  • 1
    • 33747860023 scopus 로고    scopus 로고
    • Possible role of avian uncoupling protein in down-regulating mitochondrial superoxide production in skeletal muscle of fasted chickens
    • Abe T., Mujahid A., Sato K., Akiba Y., and Toyomizu M. Possible role of avian uncoupling protein in down-regulating mitochondrial superoxide production in skeletal muscle of fasted chickens. FEBS Lett. 580 (2006) 4815-4822
    • (2006) FEBS Lett. , vol.580 , pp. 4815-4822
    • Abe, T.1    Mujahid, A.2    Sato, K.3    Akiba, Y.4    Toyomizu, M.5
  • 3
    • 0020000232 scopus 로고
    • Fibre types in chicken skeletal muscles and their changes in muscular dystrophy
    • Barnard E.A., Lyles J.M., and Pizzey J.A. Fibre types in chicken skeletal muscles and their changes in muscular dystrophy. J. Physiol. 331 (1982) 333-354
    • (1982) J. Physiol. , vol.331 , pp. 333-354
    • Barnard, E.A.1    Lyles, J.M.2    Pizzey, J.A.3
  • 4
    • 0842287450 scopus 로고    scopus 로고
    • Mitochondrial beta-oxidation
    • Bartlett K., and Eaton S. Mitochondrial beta-oxidation. Eur. J. Biochem. 271 (2004) 462-469
    • (2004) Eur. J. Biochem. , vol.271 , pp. 462-469
    • Bartlett, K.1    Eaton, S.2
  • 5
    • 0014576426 scopus 로고
    • Metabolic differentiation of distinct muscle types at the level of enzymatic organization
    • Bass A., Brdiczka D., Eyer P., Hofer S., and Pette D. Metabolic differentiation of distinct muscle types at the level of enzymatic organization. Eur. J. Biochem. 10 (1969) 198-206
    • (1969) Eur. J. Biochem. , vol.10 , pp. 198-206
    • Bass, A.1    Brdiczka, D.2    Eyer, P.3    Hofer, S.4    Pette, D.5
  • 6
    • 0021006796 scopus 로고
    • Maximal activities of hexokinase, 6-phosphofructokinase, oxoglutarate dehydrogenase, and carnitine palmitoyltransferase in rat and avian muscles
    • Blomstrand E., Challiss R.A., Cooney G.J., and Newsholme E.A. Maximal activities of hexokinase, 6-phosphofructokinase, oxoglutarate dehydrogenase, and carnitine palmitoyltransferase in rat and avian muscles. Biosci. Rep. 3 (1983) 1149-1153
    • (1983) Biosci. Rep. , vol.3 , pp. 1149-1153
    • Blomstrand, E.1    Challiss, R.A.2    Cooney, G.J.3    Newsholme, E.A.4
  • 7
    • 0019798351 scopus 로고
    • The effect of fasting on the activity of liver carnitine palmitoyltransferase and its inhibition by malonyl-CoA
    • Bremer J. The effect of fasting on the activity of liver carnitine palmitoyltransferase and its inhibition by malonyl-CoA. Biochim. Biophys. Acta 665 (1981) 628-631
    • (1981) Biochim. Biophys. Acta , vol.665 , pp. 628-631
    • Bremer, J.1
  • 8
    • 0031568912 scopus 로고    scopus 로고
    • Fine chromosome mapping of the genes for human liver and muscle carnitine palmitoyltransferase I (CPT1A and CPT1B)
    • Britton C.H., Mackey D.W., Esser V., Foster D.W., Burns D.K., Yarnall D.P., Froguel P., and McGarry J.D. Fine chromosome mapping of the genes for human liver and muscle carnitine palmitoyltransferase I (CPT1A and CPT1B). Genomics 40 (1997) 209-211
    • (1997) Genomics , vol.40 , pp. 209-211
    • Britton, C.H.1    Mackey, D.W.2    Esser, V.3    Foster, D.W.4    Burns, D.K.5    Yarnall, D.P.6    Froguel, P.7    McGarry, J.D.8
  • 9
    • 0030663919 scopus 로고    scopus 로고
    • Mouse white adipocytes and 3T3-L1 cells display an anomalous pattern of carnitine palmitoyltransferase (CPT) I isoform expression during differentiation. Inter-tissue and inter-species expression of CPT I and CPT II enzymes
    • Brown N.F., Hill J.K., Esser V., Kirkland J.L., Corkey B.E., Foster D.W., and McGarry J.D. Mouse white adipocytes and 3T3-L1 cells display an anomalous pattern of carnitine palmitoyltransferase (CPT) I isoform expression during differentiation. Inter-tissue and inter-species expression of CPT I and CPT II enzymes. Biochem. J. 327 Pt1 (1997) 225-231
    • (1997) Biochem. J. , vol.327 , Issue.Pt1 , pp. 225-231
    • Brown, N.F.1    Hill, J.K.2    Esser, V.3    Kirkland, J.L.4    Corkey, B.E.5    Foster, D.W.6    McGarry, J.D.7
  • 10
    • 18144415504 scopus 로고    scopus 로고
    • Leptin receptor in the chicken ovary: potential involvement in ovarian dysfunction of ad libitum-fed broiler breeder hens
    • Cassy S., Metayer S., Crochet S., Rideau N., Collin A., and Tesseraud S. Leptin receptor in the chicken ovary: potential involvement in ovarian dysfunction of ad libitum-fed broiler breeder hens. Reprod. Biol. Endocrinol. 2 (2004) 72
    • (2004) Reprod. Biol. Endocrinol. , vol.2 , pp. 72
    • Cassy, S.1    Metayer, S.2    Crochet, S.3    Rideau, N.4    Collin, A.5    Tesseraud, S.6
  • 12
    • 0036154857 scopus 로고    scopus 로고
    • Control of mitochondrial beta-oxidation flux
    • Eaton S. Control of mitochondrial beta-oxidation flux. Prog. Lipid Res. 41 (2002) 197-239
    • (2002) Prog. Lipid Res. , vol.41 , pp. 197-239
    • Eaton, S.1
  • 13
    • 0029862741 scopus 로고    scopus 로고
    • Expression of a cDNA isolated from rat brown adipose tissue and heart identifies the product as the muscle isoform of carnitine palmitoyltransferase I (M-CPT I). M-CPT I is the predominant CPT I isoform expressed in both white (epididymal) and brown adipocytes
    • Esser V., Brown N.F., Cowan A.T., Foster D.W., and McGarry J.D. Expression of a cDNA isolated from rat brown adipose tissue and heart identifies the product as the muscle isoform of carnitine palmitoyltransferase I (M-CPT I). M-CPT I is the predominant CPT I isoform expressed in both white (epididymal) and brown adipocytes. J. Biol. Chem. 271 (1996) 6972-6977
    • (1996) J. Biol. Chem. , vol.271 , pp. 6972-6977
    • Esser, V.1    Brown, N.F.2    Cowan, A.T.3    Foster, D.W.4    McGarry, J.D.5
  • 14
    • 0023814844 scopus 로고
    • Energy metabolism in genetically fat and lean chickens: diet- and cold-induced thermogenesis
    • Geraert P.A., MacLeod M.G., and Leclercq B. Energy metabolism in genetically fat and lean chickens: diet- and cold-induced thermogenesis. J. Nutr. 118 (1988) 1232-1239
    • (1988) J. Nutr. , vol.118 , pp. 1232-1239
    • Geraert, P.A.1    MacLeod, M.G.2    Leclercq, B.3
  • 16
    • 0025169009 scopus 로고
    • Regulation of carnitine palmitoyltransferase I in chick liver
    • Griffin H.D., Windsor D., and Zammit V.A. Regulation of carnitine palmitoyltransferase I in chick liver. Biochem. Soc. Trans. 18 (1990) 981-982
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 981-982
    • Griffin, H.D.1    Windsor, D.2    Zammit, V.A.3
  • 18
    • 0033921984 scopus 로고    scopus 로고
    • Exercise attenuates the fasting-induced transcriptional activation of metabolic genes in skeletal muscle
    • Hildebrandt A.L., and Neufer P.D. Exercise attenuates the fasting-induced transcriptional activation of metabolic genes in skeletal muscle. Am. J. Physiol., Endocrinol. Metab. 278 (2000) E1078-E1086
    • (2000) Am. J. Physiol., Endocrinol. Metab. , vol.278
    • Hildebrandt, A.L.1    Neufer, P.D.2
  • 19
    • 0021958914 scopus 로고
    • Developmental changes in the activities of peroxisomal and mitochondrial beta-oxidation in chicken liver
    • Ishii H., Ishii S., Suga T., and Kazama M. Developmental changes in the activities of peroxisomal and mitochondrial beta-oxidation in chicken liver. Arch. Biochem. Biophys. 237 (1985) 151-159
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 151-159
    • Ishii, H.1    Ishii, S.2    Suga, T.3    Kazama, M.4
  • 20
    • 0033400310 scopus 로고    scopus 로고
    • Skeletal muscle fatty acid metabolism in association with insulin resistance, obesity, and weight loss
    • Kelley D.E., Goodpaster B., Wing R.R., and Simoneau J.-A. Skeletal muscle fatty acid metabolism in association with insulin resistance, obesity, and weight loss. Am. J. Physiol., Endocrinol. Metab. 277 (1999) E1130-E1141
    • (1999) Am. J. Physiol., Endocrinol. Metab. , vol.277
    • Kelley, D.E.1    Goodpaster, B.2    Wing, R.R.3    Simoneau, J.-A.4
  • 23
    • 0001917107 scopus 로고
    • Genetic selection of meat-type chickens for high and low abdominal fat content
    • Leclercq B., and Whitehead C.C. (Eds), INRA-Butterworths, London
    • Leclercq B. Genetic selection of meat-type chickens for high and low abdominal fat content. In: Leclercq B., and Whitehead C.C. (Eds). Leanness in Domestic Birds, vol. (1988), INRA-Butterworths, London 25-40
    • (1988) Leanness in Domestic Birds, vol. , pp. 25-40
    • Leclercq, B.1
  • 24
    • 0000188952 scopus 로고
    • Selecting broilers for low or high abdominal fat: initial observations
    • Leclercq B., Blum J.C., and Boyer J.P. Selecting broilers for low or high abdominal fat: initial observations. Br. Poult. Sci. (1980) 107-113
    • (1980) Br. Poult. Sci. , pp. 107-113
    • Leclercq, B.1    Blum, J.C.2    Boyer, J.P.3
  • 25
    • 12444334643 scopus 로고    scopus 로고
    • Lipotoxicity, an imbalance between lipogenesis de novo and fatty acid oxidation
    • Lelliott C., and Vidal-Puig A.J. Lipotoxicity, an imbalance between lipogenesis de novo and fatty acid oxidation. Int. J. Obes. Relat. Metab. Disord. 28 Suppl 4 (2004) S22-S28
    • (2004) Int. J. Obes. Relat. Metab. Disord. , vol.28 , Issue.SUPPL. 4
    • Lelliott, C.1    Vidal-Puig, A.J.2
  • 26
    • 85047684624 scopus 로고    scopus 로고
    • The effect of supplementary dietary L-carnitine on the growth performance, serum components, carcase traits and enzyme activities in relation to fatty acid beta-oxidation of broiler chickens
    • Lien T.F., and Horng Y.M. The effect of supplementary dietary L-carnitine on the growth performance, serum components, carcase traits and enzyme activities in relation to fatty acid beta-oxidation of broiler chickens. Br. Poult. Sci. 42 (2001) 92-95
    • (2001) Br. Poult. Sci. , vol.42 , pp. 92-95
    • Lien, T.F.1    Horng, Y.M.2
  • 27
    • 0035865496 scopus 로고    scopus 로고
    • Long-chain fatty acids regulate liver carnitine palmitoyltransferase I gene (L-CPT I) expression through a peroxisome-proliferator-activated receptor alpha (PPARalpha)-independent pathway
    • Louet J.F., Chatelain F., Decaux J.F., Park E.A., Kohl C., Pineau T., Girard J., and Pegorier J.P. Long-chain fatty acids regulate liver carnitine palmitoyltransferase I gene (L-CPT I) expression through a peroxisome-proliferator-activated receptor alpha (PPARalpha)-independent pathway. Biochem. J. 354 (2001) 189-197
    • (2001) Biochem. J. , vol.354 , pp. 189-197
    • Louet, J.F.1    Chatelain, F.2    Decaux, J.F.3    Park, E.A.4    Kohl, C.5    Pineau, T.6    Girard, J.7    Pegorier, J.P.8
  • 28
    • 0034957825 scopus 로고    scopus 로고
    • Regulation of liver carnitine palmitoyltransferase I gene expression by hormones and fatty acids
    • Louet J.F., Le May C., Pegorier J.P., Decaux J.F., and Girard J. Regulation of liver carnitine palmitoyltransferase I gene expression by hormones and fatty acids. Biochem. Soc. Trans. 29 (2001) 310-316
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 310-316
    • Louet, J.F.1    Le May, C.2    Pegorier, J.P.3    Decaux, J.F.4    Girard, J.5
  • 29
    • 0031043030 scopus 로고    scopus 로고
    • The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis
    • McGarry J.D., and Brown N.F. The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis. Eur. J. Biochem. 244 (1997) 1-14
    • (1997) Eur. J. Biochem. , vol.244 , pp. 1-14
    • McGarry, J.D.1    Brown, N.F.2
  • 30
    • 0024503204 scopus 로고
    • Regulation of ketogenesis and the renaissance of carnitine palmitoyltransferase
    • McGarry J.D., Woeltje K.F., Kuwajima M., and Foster D.W. Regulation of ketogenesis and the renaissance of carnitine palmitoyltransferase. Diabetes Metab. Rev. 5 (1989) 271-284
    • (1989) Diabetes Metab. Rev. , vol.5 , pp. 271-284
    • McGarry, J.D.1    Woeltje, K.F.2    Kuwajima, M.3    Foster, D.W.4
  • 32
    • 0021022320 scopus 로고
    • Determination of free fatty acids: a comparative study of the enzymatic versus the gas chromatographic and the colorimetric method
    • Mulder C., Schouten J.A., and Popp-Snijders C. Determination of free fatty acids: a comparative study of the enzymatic versus the gas chromatographic and the colorimetric method. J. Clin. Chem. Clin. Biochem. 21 (1983) 823-827
    • (1983) J. Clin. Chem. Clin. Biochem. , vol.21 , pp. 823-827
    • Mulder, C.1    Schouten, J.A.2    Popp-Snijders, C.3
  • 33
    • 0141817917 scopus 로고    scopus 로고
    • A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme
    • Napal L., Dai J., Treber M., Haro D., Marrero P.F., and Woldegiorgis G. A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme. J. Biol. Chem. 278 (2003) 34084-34089
    • (2003) J. Biol. Chem. , vol.278 , pp. 34084-34089
    • Napal, L.1    Dai, J.2    Treber, M.3    Haro, D.4    Marrero, P.F.5    Woldegiorgis, G.6
  • 34
    • 0029166078 scopus 로고
    • Insulin regulates enzyme activity, malonyl-CoA sensitivity and mRNA abundance of hepatic carnitine palmitoyltransferase-I
    • Park E.A., Mynatt R.L., Cook G.A., and Kashfi K. Insulin regulates enzyme activity, malonyl-CoA sensitivity and mRNA abundance of hepatic carnitine palmitoyltransferase-I. Biochem. J. 310 Pt3 (1995) 853-858
    • (1995) Biochem. J. , vol.310 , Issue.Pt3 , pp. 853-858
    • Park, E.A.1    Mynatt, R.L.2    Cook, G.A.3    Kashfi, K.4
  • 35
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29 (2001) E45-E45
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 36
    • 0037341240 scopus 로고    scopus 로고
    • Effect of short-term fasting and refeeding on transcriptional regulation of metabolic genes in human skeletal muscle
    • Pilegaard H., Saltin B., and Neufer P.D. Effect of short-term fasting and refeeding on transcriptional regulation of metabolic genes in human skeletal muscle. Diabetes 52 (2003) 657-662
    • (2003) Diabetes , vol.52 , pp. 657-662
    • Pilegaard, H.1    Saltin, B.2    Neufer, P.D.3
  • 37
    • 0028389519 scopus 로고
    • Effects of divergent selection for body weight on three skeletal muscles characteristics in the chicken
    • Remignon H., Lefaucheur L., Blum J.C., and Ricard F.H. Effects of divergent selection for body weight on three skeletal muscles characteristics in the chicken. Br. Poult. Sci. 35 (1994) 65-76
    • (1994) Br. Poult. Sci. , vol.35 , pp. 65-76
    • Remignon, H.1    Lefaucheur, L.2    Blum, J.C.3    Ricard, F.H.4
  • 38
    • 16244409470 scopus 로고    scopus 로고
    • Effect of starvation on hepatic acyl-CoA synthetase, carnitine palmitoyltransferase-I, and acetyl-CoA carboxylase mRNA levels in rats
    • Ryu M.H., Daily III J.W., and Cha Y.S. Effect of starvation on hepatic acyl-CoA synthetase, carnitine palmitoyltransferase-I, and acetyl-CoA carboxylase mRNA levels in rats. Nutrition 21 (2005) 537-542
    • (2005) Nutrition , vol.21 , pp. 537-542
    • Ryu, M.H.1    Daily III, J.W.2    Cha, Y.S.3
  • 39
    • 0036811465 scopus 로고    scopus 로고
    • Skeletal muscle heterogeneity in fasting-induced upregulation of genes encoding UCP2, UCP3, PPARgamma and key enzymes of lipid oxidation
    • Samec S., Seydoux J., Russell A.P., Montani J.P., and Dulloo A.G. Skeletal muscle heterogeneity in fasting-induced upregulation of genes encoding UCP2, UCP3, PPARgamma and key enzymes of lipid oxidation. Pflugers Arch. 445 (2002) 80-86
    • (2002) Pflugers Arch. , vol.445 , pp. 80-86
    • Samec, S.1    Seydoux, J.2    Russell, A.P.3    Montani, J.P.4    Dulloo, A.G.5
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 0029954776 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA and genomic clones encoding human muscle type carnitine palmitoyltransferase I
    • Yamazaki N., Shinohara Y., Shima A., Yamanaka Y., and Terada H. Isolation and characterization of cDNA and genomic clones encoding human muscle type carnitine palmitoyltransferase I. Biochim. Biophys. Acta 1307 (1996) 157-161
    • (1996) Biochim. Biophys. Acta , vol.1307 , pp. 157-161
    • Yamazaki, N.1    Shinohara, Y.2    Shima, A.3    Yamanaka, Y.4    Terada, H.5
  • 42
    • 0030798104 scopus 로고    scopus 로고
    • Structural features of the gene encoding human muscle type carnitine palmitoyltransferase I
    • Yamazaki N., Yamanaka Y., Hashimoto Y., Shinohara Y., Shima A., and Terada H. Structural features of the gene encoding human muscle type carnitine palmitoyltransferase I. FEBS Lett. 409 (1997) 401-406
    • (1997) FEBS Lett. , vol.409 , pp. 401-406
    • Yamazaki, N.1    Yamanaka, Y.2    Hashimoto, Y.3    Shinohara, Y.4    Shima, A.5    Terada, H.6
  • 44
    • 0020773785 scopus 로고
    • Regulation of hepatic fatty acid oxidation and ketogenesis
    • Zammit V.A. Regulation of hepatic fatty acid oxidation and ketogenesis. Proc. Nutr. Soc. 42 (1983) 289-302
    • (1983) Proc. Nutr. Soc. , vol.42 , pp. 289-302
    • Zammit, V.A.1


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