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Volumn 61, Issue 12, 2012, Pages 1703-1713

Shc proteins influence the activities of enzymes involved in fatty acid oxidation and ketogenesis

Author keywords

Fasting; Fatty acid oxidation; Fed to starved transition; Liver; Skeletan muscle

Indexed keywords

3 HYDROXYBUTYRATE DEHYDROGENASE; ACETYL COENZYME A ACETYLTRANSFERASE; HORMONE SENSITIVE LIPASE; PROTEIN SHC;

EID: 84869509508     PISSN: 00260495     EISSN: 15328600     Source Type: Journal    
DOI: 10.1016/j.metabol.2012.05.007     Document Type: Article
Times cited : (10)

References (44)
  • 1
  • 4
    • 0026777369 scopus 로고
    • A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
    • G. Pelicci, L. Lanfrancone, and F. Grignani A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction Cell 70 1992 93 104
    • (1992) Cell , vol.70 , pp. 93-104
    • Pelicci, G.1    Lanfrancone, L.2    Grignani, F.3
  • 5
    • 0028328533 scopus 로고
    • Involvement of Shc in insulin- and epidermal growth factor-induced activation of p21ras
    • G.J. Pronk, A.M. de Vries-Smits, and L. Buday Involvement of Shc in insulin- and epidermal growth factor-induced activation of p21ras Mol Cell Biol 14 1994 1575 1581
    • (1994) Mol Cell Biol , vol.14 , pp. 1575-1581
    • Pronk, G.J.1    De Vries-Smits, A.M.2    Buday, L.3
  • 6
    • 0028242350 scopus 로고
    • Evidence for a functional role of Shc proteins in mitogenic signaling induced by insulin, insulin-like growth factor-1, and epidermal growth factor
    • T. Sasaoka, D.W. Rose, and B.H. Jhun Evidence for a functional role of Shc proteins in mitogenic signaling induced by insulin, insulin-like growth factor-1, and epidermal growth factor J Biol Chem 269 1994 13689 13694 (Pubitemid 24206151)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.18 , pp. 13689-13694
    • Sasaoka, T.1    Rose, D.W.2    Jhun, B.H.3    Saltiel, A.R.4    Draznin, B.5    Olefsky, J.M.6
  • 7
    • 0032489518 scopus 로고    scopus 로고
    • A role for Src in signal relay by the platelet-derived growth factor α receptor
    • DOI 10.1074/jbc.273.10.5908
    • J.A. Gelderloos, S. Rosenkranz, and C. Bazenet A role for Src in signal relay by the platelet-derived growth factor alpha receptor J Biol Chem 273 1998 5908 5915 (Pubitemid 28124070)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5908-5915
    • Gelderloos, J.A.1    Rosenkranz, S.2    Bazenet, C.3    Kazlauskas, A.4
  • 8
    • 0028243655 scopus 로고
    • Direct interaction between Shc and the platelet-derived growth factor beta-receptor
    • K. Yokote, S. Mori, and K. Hansen Direct interaction between Shc and the platelet-derived growth factor beta-receptor J Biol Chem 269 1994 15337 15343
    • (1994) J Biol Chem , vol.269 , pp. 15337-15343
    • Yokote, K.1    Mori, S.2    Hansen, K.3
  • 10
    • 0035474473 scopus 로고    scopus 로고
    • Signaling via Shc family adapter proteins
    • DOI 10.1038/sj.onc.1204776
    • K.S. Ravichandran Signaling via Shc family adapter proteins Oncogene 20 2001 6322 6330 (Pubitemid 32977841)
    • (2001) Oncogene , vol.20 , Issue.44 REV. ISS. 5 , pp. 6322-6330
    • Ravichandran, K.S.1
  • 11
    • 78651344799 scopus 로고    scopus 로고
    • The Shc locus regulates insulin signaling and adiposity in mammals
    • A.A. Tomilov, J.J. Ramsey, and K. Hagopian The Shc locus regulates insulin signaling and adiposity in mammals Aging Cell 10 2011 55 65
    • (2011) Aging Cell , vol.10 , pp. 55-65
    • Tomilov, A.A.1    Ramsey, J.J.2    Hagopian, K.3
  • 12
    • 57749091893 scopus 로고    scopus 로고
    • P66Shc-generated oxidative signal promotes fat accumulation
    • I. Berniakovich, M. Trinei, and M. Stendardo p66Shc-generated oxidative signal promotes fat accumulation J Biol Chem 283 2008 34283 34293
    • (2008) J Biol Chem , vol.283 , pp. 34283-34293
    • Berniakovich, I.1    Trinei, M.2    Stendardo, M.3
  • 13
    • 77955798757 scopus 로고    scopus 로고
    • Mammalian life-span determinant p66shcA mediates obesity-induced insulin resistance
    • S.C. Ranieri, S. Fusco, and E. Panieri Mammalian life-span determinant p66shcA mediates obesity-induced insulin resistance Proc Natl Acad Sci U S A 107 2010 13420 13425
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 13420-13425
    • Ranieri, S.C.1    Fusco, S.2    Panieri, E.3
  • 14
    • 0021996088 scopus 로고
    • An essential cysteine residue located in the vicinity of the FAD-binding site in short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria
    • K. Okamura-Ikeda, Y. Ikeda, and K. Tanaka An essential cysteine residue located in the vicinity of the FAD-binding site in short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria J Biol Chem 260 1985 1338 1345 (Pubitemid 15173656)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.2 , pp. 1338-1345
    • Okamura-Ikeda, K.1    Ikeda, Y.2    Tanaka, K.3
  • 16
    • 0016412389 scopus 로고
    • 3-Ketoacyl-CoA thiolases of mammalian tissues
    • B. Middleton 3-Ketoacyl-CoA thiolases of mammalian tissues Methods Enzymol 35 1975 128 136
    • (1975) Methods Enzymol , vol.35 , pp. 128-136
    • Middleton, B.1
  • 17
    • 77957011800 scopus 로고
    • Citrate synthase from rat liver
    • D. Shephard, and P.B. Garland Citrate synthase from rat liver Methods Enzymol 13 1969 11 16
    • (1969) Methods Enzymol , vol.13 , pp. 11-16
    • Shephard, D.1    Garland, P.B.2
  • 18
    • 0000416021 scopus 로고
    • Lactate dehydrogenase
    • H.U. Bergmeyer, Academic Press New York
    • H.U. Bergmeyer, and E. Bernt Lactate dehydrogenase H.U. Bergmeyer, Methods of enzymatic analysis 1974 Academic Press New York 574 579
    • (1974) Methods of Enzymatic Analysis , pp. 574-579
    • Bergmeyer, H.U.1    Bernt, E.2
  • 19
    • 0018977041 scopus 로고
    • The presence of a new 3-oxoacyl-CoA thiolase in rat liver peroxisomes
    • S. Miyazawa, T. Osumi, and T. Hashimoto The presence of a new 3-oxoacyl-CoA thiolase in rat liver peroxisomes Eur J Biochem 103 1980 589 596
    • (1980) Eur J Biochem , vol.103 , pp. 589-596
    • Miyazawa, S.1    Osumi, T.2    Hashimoto, T.3
  • 20
    • 0000402729 scopus 로고
    • D-b-hydroxybutyrate dehydrogenase of mitochondria
    • A.L. Lehninger, H.C. Sudduth, and J.B. Wise D-b-hydroxybutyrate dehydrogenase of mitochondria J Biol Chem 235 1960 2450 2455
    • (1960) J Biol Chem , vol.235 , pp. 2450-2455
    • Lehninger, A.L.1    Sudduth, H.C.2    Wise, J.B.3
  • 21
    • 34548484350 scopus 로고    scopus 로고
    • Nitration of tryptophan 372 in succinyl-CoA:3-ketoacid CoA transferase during aging in rat heart mitochondria
    • DOI 10.1021/bi7001482
    • I. Rebrin, C. Bregere, and S. Kamzalov Nitration of tryptophan 372 in succinyl-CoA:3-ketoacid CoA transferase during aging in rat heart mitochondria Biochemistry 46 2007 10130 10144 (Pubitemid 47378605)
    • (2007) Biochemistry , vol.46 , Issue.35 , pp. 10130-10144
    • Rebrin, I.1    Bregere, C.2    Kamzalov, S.3    Gallaher, T.K.4    Sohal, R.S.5
  • 22
    • 1642522022 scopus 로고    scopus 로고
    • 2 production and susceptibility to stress conditions of rat liver mitochondria
    • DOI 10.1016/j.freeradbiomed.2003.11.012
    • P. Venditti, R. De Rosa, and S. Di Meo Effect of cold-induced hyperthyroidism on H2O2 production and susceptibility to stress conditions of rat liver mitochondria Free Radic Biol Med 36 2004 348 358 (Pubitemid 38130233)
    • (2004) Free Radical Biology and Medicine , vol.36 , Issue.3 , pp. 348-358
    • Venditti, P.1    De Rosa, R.2    Di Meo, S.3
  • 23
    • 77958586697 scopus 로고    scopus 로고
    • Complex I-associated hydrogen peroxide production is decreased and electron transport chain enzyme activities are altered in n-3 enriched fat-1 mice
    • K. Hagopian, K.L. Weber, and D.T. Hwee Complex I-associated hydrogen peroxide production is decreased and electron transport chain enzyme activities are altered in n-3 enriched fat-1 mice PLoS One 5 2010 e12696
    • (2010) PLoS One , vol.5 , pp. 12696
    • Hagopian, K.1    Weber, K.L.2    Hwee, D.T.3
  • 24
    • 79960712083 scopus 로고    scopus 로고
    • High throughput microplate respiratory measurements using minimal quantities of isolated mitochondria
    • G.W. Rogers, M.D. Brand, and S. Petrosyan High throughput microplate respiratory measurements using minimal quantities of isolated mitochondria PLoS One 6 2011 e21746
    • (2011) PLoS One , vol.6 , pp. 21746
    • Rogers, G.W.1    Brand, M.D.2    Petrosyan, S.3
  • 27
    • 77951093550 scopus 로고    scopus 로고
    • PGC-1alpha is required for training-induced prevention of age-associated decline in mitochondrial enzymes in mouse skeletal muscle
    • L. Leick, S.S. Lyngby, and J.F. Wojtaszewski PGC-1alpha is required for training-induced prevention of age-associated decline in mitochondrial enzymes in mouse skeletal muscle Exp Gerontol 45 2010 336 342
    • (2010) Exp Gerontol , vol.45 , pp. 336-342
    • Leick, L.1    Lyngby, S.S.2    Wojtaszewski, J.F.3
  • 29
    • 53049095685 scopus 로고    scopus 로고
    • Endurance capacity in maturing mdx mice is markedly enhanced by combined voluntary wheel running and green tea extract
    • J.A. Call, K.A. Voelker, and A.V. Wolff Endurance capacity in maturing mdx mice is markedly enhanced by combined voluntary wheel running and green tea extract J Appl Physiol 105 2008 923 932
    • (2008) J Appl Physiol , vol.105 , pp. 923-932
    • Call, J.A.1    Voelker, K.A.2    Wolff, A.V.3
  • 30
    • 34547588219 scopus 로고    scopus 로고
    • Excess lipid availability increases mitochondrial fatty acid oxidative capacity in muscle: Evidence against a role for reduced fatty acid oxidation in lipid-induced insulin resistance in rodents
    • DOI 10.2337/db07-0093
    • N. Turner, C.R. Bruce, and S.M. Beale Excess lipid availability increases mitochondrial fatty acid oxidative capacity in muscle: evidence against a role for reduced fatty acid oxidation in lipid-induced insulin resistance in rodents Diabetes 56 2007 2085 2092 (Pubitemid 47195821)
    • (2007) Diabetes , vol.56 , Issue.8 , pp. 2085-2092
    • Turner, N.1    Bruce, C.R.2    Beale, S.M.3    Hoehn, K.L.4    So, T.5    Rolph, M.S.6    Cooney, G.J.7
  • 31
    • 0026519290 scopus 로고
    • Metabolic response to a high-fat diet in neonatal and adult rat muscle
    • P.M. Nemeth, B.W. Rosser, and R.M. Choksi Metabolic response to a high-fat diet in neonatal and adult rat muscle Am J Physiol 262 1992 C282 C286
    • (1992) Am J Physiol , vol.262
    • Nemeth, P.M.1    Rosser, B.W.2    Choksi, R.M.3
  • 32
    • 0025764527 scopus 로고
    • Additive effects of training and high-fat diet on energy metabolism during exercise
    • B. Simi, B. Sempore, and M.H. Mayet Additive effects of training and high-fat diet on energy metabolism during exercise J Appl Physiol 71 1991 197 203
    • (1991) J Appl Physiol , vol.71 , pp. 197-203
    • Simi, B.1    Sempore, B.2    Mayet, M.H.3
  • 33
    • 0021069165 scopus 로고
    • Phosphorylation of hormone-sensitive lipase by cyclic AMP-dependent protein kinase
    • P. Stralfors, and P. Belfrage Phosphorylation of hormone-sensitive lipase by cyclic AMP-dependent protein kinase J Biol Chem 258 1983 15146 15152 (Pubitemid 14178947)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.24 , pp. 15146-15152
    • Stralfors, P.1    Belfrage, P.2
  • 35
    • 0031034366 scopus 로고    scopus 로고
    • Contribution of energy intake and tissue enzymatic profile to body weight gain in high-fat-fed rats
    • E.C. Gayles, M.J. Pagliassotti, and P.A. Prach Contribution of energy intake and tissue enzymatic profile to body weight gain in high-fat-fed rats Am J Physiol 272 1997 R188 R194
    • (1997) Am J Physiol , vol.272
    • Gayles, E.C.1    Pagliassotti, M.J.2    Prach, P.A.3
  • 36
    • 20444390600 scopus 로고    scopus 로고
    • Phenotypic profile of SWR/J and A/J mice compared to control strains: Possible mechanisms underlying resistance to obesity on a high-fat diet
    • DOI 10.1016/j.brainres.2005.03.047, PII S0006899305005093
    • S.F. Leibowitz, J. Alexander, and J.T. Dourmashkin Phenotypic profile of SWR/J and A/J mice compared to control strains: possible mechanisms underlying resistance to obesity on a high-fat diet Brain Res 1047 2005 137 147 (Pubitemid 40799309)
    • (2005) Brain Research , vol.1047 , Issue.2 , pp. 137-147
    • Leibowitz, S.F.1    Alexander, J.2    Dourmashkin, J.T.3    Hill, J.O.4    Gayles, E.C.5    Chang, G.-Q.6
  • 37
    • 63649121321 scopus 로고    scopus 로고
    • Regulation by exercise of skeletal muscle content of mitochondria and GLUT4
    • J.O. Holloszy Regulation by exercise of skeletal muscle content of mitochondria and GLUT4 J Physiol Pharmacol 59 Suppl. 7 2008 5 18
    • (2008) J Physiol Pharmacol , vol.59 , Issue.SUPPL. 7 , pp. 5-18
    • Holloszy, J.O.1
  • 38
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • S. Zhao, W. Xu, and W. Jiang Regulation of cellular metabolism by protein lysine acetylation Science 327 2010 1000 1004
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3
  • 39
    • 34247634168 scopus 로고    scopus 로고
    • Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry
    • DOI 10.1016/j.bbapap.2007.03.012, PII S1570963907000544
    • A.M. Distler, J. Kerner, and C.L. Hoppel Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry Biochim Biophys Acta 1774 2007 628 636 (Pubitemid 46670809)
    • (2007) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1774 , Issue.5 , pp. 628-636
    • Distler, A.M.1    Kerner, J.2    Hoppel, C.L.3
  • 40
    • 0016704070 scopus 로고
    • Exercise-induced increase in the capacity of rat skeletal muscle to oxidize ketones
    • W.W. Winder, K.M. Baldwin, and J.O. Holloszy Exercise-induced increase in the capacity of rat skeletal muscle to oxidize ketones Can J Physiol Pharmacol 53 1975 86 91
    • (1975) Can J Physiol Pharmacol , vol.53 , pp. 86-91
    • Winder, W.W.1    Baldwin, K.M.2    Holloszy, J.O.3
  • 41
    • 0014972144 scopus 로고
    • Activities of enzymes involved in acetoacetate utilization in adult mammalian tissues
    • D.H. Williamson, M.W. Bates, and M.A. Page Activities of enzymes involved in acetoacetate utilization in adult mammalian tissues Biochem J 121 1971 41 47
    • (1971) Biochem J , vol.121 , pp. 41-47
    • Williamson, D.H.1    Bates, M.W.2    Page, M.A.3
  • 42
    • 0033400713 scopus 로고    scopus 로고
    • Ketone bodies: A review of physiology, pathophysiology and application of monitoring to diabetes
    • L. Laffel Ketone bodies: a review of physiology, pathophysiology and application of monitoring to diabetes Diabetes Metab Res Rev 15 1999 412 426 (Pubitemid 30066228)
    • (1999) Diabetes/Metabolism Research and Reviews , vol.15 , Issue.6 , pp. 412-426
    • Laffel, L.1
  • 43
    • 1042276529 scopus 로고    scopus 로고
    • Pathways and control of ketone body metabolism: On the fringe of lipid biochemistry
    • DOI 10.1016/j.plefa.2003.11.001
    • T. Fukao, G.D. Lopaschuk, and G.A. Mitchell Pathways and control of ketone body metabolism: on the fringe of lipid biochemistry Prostaglandins Leukot Essent Fatty Acids 70 2004 243 251 (Pubitemid 38200951)
    • (2004) Prostaglandins Leukotrienes and Essential Fatty Acids , vol.70 , Issue.3 , pp. 243-251
    • Fukao, T.1    Lopaschuk, G.D.2    Mitchell, G.A.3
  • 44
    • 0014303713 scopus 로고
    • Activity and intracellular distribution of enzymes of ketone-body metabolism in rat liver
    • D.H. Williamson, M.W. Bates, and H.A. Krebs Activity and intracellular distribution of enzymes of ketone-body metabolism in rat liver Biochem J 108 1968 353 361
    • (1968) Biochem J , vol.108 , pp. 353-361
    • Williamson, D.H.1    Bates, M.W.2    Krebs, H.A.3


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