메뉴 건너뛰기




Volumn 11, Issue 5, 2010, Pages 412-426

Regulation of skeletal muscle oxidative capacity and insulin signaling by the mitochondrial rhomboid protease PARL

(18)  Civitarese, Anthony E a,b,i   MacLean, Paul S c   Carling, Stacy a   Kerr Bayles, Lyndal d   McMillan, Ryan P f   Pierce, Anson g   Becker, Thomas C h   Moro, Cedric a   Finlayson, Jean b   Lefort, Natalie b   Newgard, Christopher B h   Mandarino, Lawrence b,i   Cefalu, William a   Walder, Ken d   Collier, Greg R d,e   Hulver, Matthew W f   Smith, Steven R a   Ravussin, Eric a  


Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; MESSENGER RNA; PARL PROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PROTEINASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; GLYCOGEN; METALLOPROTEINASE; MITOCHONDRIAL PROTEIN; PARL PROTEIN, HUMAN; PARL PROTEIN, MOUSE; PPARGC1A PROTEIN, MOUSE; TRANSACTIVATOR PROTEIN;

EID: 77955284487     PISSN: 15504131     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cmet.2010.04.004     Document Type: Article
Times cited : (75)

References (88)
  • 2
    • 66749094133 scopus 로고    scopus 로고
    • Plasma acylcarnitine profiles suggest incomplete long-chain fatty acid beta-oxidation and altered tricarboxylic acid cycle activity in type 2 diabetic African-American women
    • S.H. Adams, C.L. Hoppel, K.H. Lok, L. Zhao, S.W. Wong, P.E. Minkler, D.H. Hwang, J.W. Newman, and W.T. Garvey Plasma acylcarnitine profiles suggest incomplete long-chain fatty acid beta-oxidation and altered tricarboxylic acid cycle activity in type 2 diabetic African-American women J. Nutr. 139 2009 1073 1081
    • (2009) J. Nutr. , vol.139 , pp. 1073-1081
    • Adams, S.H.1    Hoppel, C.L.2    Lok, K.H.3    Zhao, L.4    Wong, S.W.5    Minkler, P.E.6    Hwang, D.H.7    Newman, J.W.8    Garvey, W.T.9
  • 4
    • 0023718495 scopus 로고
    • Coupling membranes as energy-transmitting cables. I. Filamentous mitochondria in fibroblasts and mitochondrial clusters in cardiomyocytes
    • A.A. Amchenkova, L.E. Bakeeva, Y.S. Chentsov, V.P. Skulachev, and D.B. Zorov Coupling membranes as energy-transmitting cables. I. Filamentous mitochondria in fibroblasts and mitochondrial clusters in cardiomyocytes J. Cell. Biol. 107 1988 481 495
    • (1988) J. Cell. Biol. , vol.107 , pp. 481-495
    • Amchenkova, A.A.1    Bakeeva, L.E.2    Chentsov, Y.S.3    Skulachev, V.P.4    Zorov, D.B.5
  • 6
    • 34248141686 scopus 로고    scopus 로고
    • Impaired mitochondrial substrate oxidation in muscle of insulin-resistant offspring of type 2 diabetic patients
    • D.E. Befroy, K.F. Petersen, S. Dufour, G.F. Mason, R.A. de Graaf, D.L. Rothman, and G.I. Shulman Impaired mitochondrial substrate oxidation in muscle of insulin-resistant offspring of type 2 diabetic patients Diabetes 56 2007 1376 1381
    • (2007) Diabetes , vol.56 , pp. 1376-1381
    • Befroy, D.E.1    Petersen, K.F.2    Dufour, S.3    Mason, G.F.4    De Graaf, R.A.5    Rothman, D.L.6    Shulman, G.I.7
  • 7
    • 42949083922 scopus 로고    scopus 로고
    • Modest PGC-1alpha overexpression in muscle in vivo is sufficient to increase insulin sensitivity and palmitate oxidation in subsarcolemmal, not intermyofibrillar, mitochondria
    • C.R. Benton, J.G. Nickerson, J. Lally, X.X. Han, G.P. Holloway, J.F. Glatz, J.J. Luiken, T.E. Graham, J.J. Heikkila, and A. Bonen Modest PGC-1alpha overexpression in muscle in vivo is sufficient to increase insulin sensitivity and palmitate oxidation in subsarcolemmal, not intermyofibrillar, mitochondria J. Biol. Chem. 283 2008 4228 4240
    • (2008) J. Biol. Chem. , vol.283 , pp. 4228-4240
    • Benton, C.R.1    Nickerson, J.G.2    Lally, J.3    Han, X.X.4    Holloway, G.P.5    Glatz, J.F.6    Luiken, J.J.7    Graham, T.E.8    Heikkila, J.J.9    Bonen, A.10
  • 8
    • 33847611885 scopus 로고    scopus 로고
    • Patients with type 2 diabetes have normal mitochondrial function in skeletal muscle
    • R. Boushel, E. Gnaiger, P. Schjerling, M. Skovbro, R. Kraunsøe, and F. Dela Patients with type 2 diabetes have normal mitochondrial function in skeletal muscle Diabetologia 50 2007 790 796
    • (2007) Diabetologia , vol.50 , pp. 790-796
    • Boushel, R.1    Gnaiger, E.2    Schjerling, P.3    Skovbro, M.4    Kraunsøe, R.5    Dela, F.6
  • 9
    • 0142164965 scopus 로고    scopus 로고
    • Characterizing the effects of saturated fatty acids on insulin signaling and ceramide and diacylglycerol accumulation in 3T3-L1 adipocytes and C2C12 myotubes
    • J.A. Chavez, and S.A. Summers Characterizing the effects of saturated fatty acids on insulin signaling and ceramide and diacylglycerol accumulation in 3T3-L1 adipocytes and C2C12 myotubes Arch. Biochem. Biophys. 419 2003 101 109
    • (2003) Arch. Biochem. Biophys. , vol.419 , pp. 101-109
    • Chavez, J.A.1    Summers, S.A.2
  • 12
    • 40849092781 scopus 로고    scopus 로고
    • Mitochondrial energetics and insulin resistance
    • A.E. Civitarese, and E. Ravussin Mitochondrial energetics and insulin resistance Endocrinology 149 2008 950 954
    • (2008) Endocrinology , vol.149 , pp. 950-954
    • Civitarese, A.E.1    Ravussin, E.2
  • 15
    • 33847752716 scopus 로고    scopus 로고
    • Mitochondrial function, fibre types and ageing: New insights from human muscle in vivo
    • K.E. Conley, C.E. Amara, S.A. Jubrias, and D.J. Marcinek Mitochondrial function, fibre types and ageing: new insights from human muscle in vivo Exp. Physiol. 92 2007 333 339
    • (2007) Exp. Physiol. , vol.92 , pp. 333-339
    • Conley, K.E.1    Amara, C.E.2    Jubrias, S.A.3    Marcinek, D.J.4
  • 16
    • 0032775947 scopus 로고    scopus 로고
    • Relation of triglyceride stores in skeletal muscle cells to central obesity and insulin sensitivity in European and South Asian men
    • N.G. Forouhi, G. Jenkinson, E.L. Thomas, S. Mullick, S. Mierisova, U. Bhonsle, P.M. McKeigue, and J.D. Bell Relation of triglyceride stores in skeletal muscle cells to central obesity and insulin sensitivity in European and South Asian men Diabetologia 42 1999 932 935
    • (1999) Diabetologia , vol.42 , pp. 932-935
    • Forouhi, N.G.1    Jenkinson, G.2    Thomas, E.L.3    Mullick, S.4    Mierisova, S.5    Bhonsle, U.6    McKeigue, P.M.7    Bell, J.D.8
  • 19
    • 0037494885 scopus 로고    scopus 로고
    • The cristal membrane of mitochondria is the principal site of oxidative phosphorylation
    • R.W. Gilkerson, J.M. Selker, and R.A. Capaldi The cristal membrane of mitochondria is the principal site of oxidative phosphorylation FEBS Lett. 546 2003 355 358
    • (2003) FEBS Lett. , vol.546 , pp. 355-358
    • Gilkerson, R.W.1    Selker, J.M.2    Capaldi, R.A.3
  • 20
    • 0034107084 scopus 로고    scopus 로고
    • Thigh adipose tissue distribution is associated with insulin resistance in obesity and in type 2 diabetes mellitus
    • B.H. Goodpaster, F.L. Thaete, and D.E. Kelley Thigh adipose tissue distribution is associated with insulin resistance in obesity and in type 2 diabetes mellitus Am. J. Clin. Nutr. 71 2000 885 892
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 885-892
    • Goodpaster, B.H.1    Thaete, F.L.2    Kelley, D.E.3
  • 21
    • 0034112806 scopus 로고    scopus 로고
    • Intramuscular lipid content is increased in obesity and decreased by weight loss
    • B.H. Goodpaster, R. Theriault, S.C. Watkins, and D.E. Kelley Intramuscular lipid content is increased in obesity and decreased by weight loss Metabolism 49 2000 467 472
    • (2000) Metabolism , vol.49 , pp. 467-472
    • Goodpaster, B.H.1    Theriault, R.2    Watkins, S.C.3    Kelley, D.E.4
  • 22
    • 34548313686 scopus 로고    scopus 로고
    • Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
    • L. Griparic, T. Kanazawa, and A.M. van der Bliek Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage J. Cell Biol. 178 2007 757 764
    • (2007) J. Cell Biol. , vol.178 , pp. 757-764
    • Griparic, L.1    Kanazawa, T.2    Van Der Bliek, A.M.3
  • 24
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • M. Herlan, F. Vogel, C. Bornhovd, W. Neupert, and A.S. Reichert Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA J. Biol. Chem. 278 2003 27781 27788
    • (2003) J. Biol. Chem. , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhovd, C.3    Neupert, W.4    Reichert, A.S.5
  • 25
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • P.J. Hollenbeck, and W.M. Saxton The axonal transport of mitochondria J. Cell Sci. 118 2005 5411 5419
    • (2005) J. Cell Sci. , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 26
    • 0021343295 scopus 로고
    • Adaptations of skeletal muscle to endurance exercise and their metabolic consequences
    • J.O. Holloszy, and E.F. Coyle Adaptations of skeletal muscle to endurance exercise and their metabolic consequences J. Appl. Physiol. 56 1984 831 838
    • (1984) J. Appl. Physiol. , vol.56 , pp. 831-838
    • Holloszy, J.O.1    Coyle, E.F.2
  • 29
    • 0033834262 scopus 로고    scopus 로고
    • A metabolic control analysis of kinetic controls in ATP free energy metabolism in contracting skeletal muscle
    • J.A. Jeneson, H.V. Westerhoff, and M.J. Kushmerick A metabolic control analysis of kinetic controls in ATP free energy metabolism in contracting skeletal muscle Am. J. Physiol. Cell Physiol. 279 2000 C813 C832
    • (2000) Am. J. Physiol. Cell Physiol. , vol.279
    • Jeneson, J.A.1    Westerhoff, H.V.2    Kushmerick, M.J.3
  • 30
    • 0036788293 scopus 로고    scopus 로고
    • Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes
    • D.E. Kelley, J. He, E.V. Menshikova, and V.B. Ritov Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes Diabetes 51 2002 2944 2950
    • (2002) Diabetes , vol.51 , pp. 2944-2950
    • Kelley, D.E.1    He, J.2    Menshikova, E.V.3    Ritov, V.B.4
  • 31
    • 0034076660 scopus 로고    scopus 로고
    • Fuel selection in human skeletal muscle in insulin resistance: A reexamination
    • D.E. Kelley, and L.J. Mandarino Fuel selection in human skeletal muscle in insulin resistance: a reexamination Diabetes 49 2000 677 683
    • (2000) Diabetes , vol.49 , pp. 677-683
    • Kelley, D.E.1    Mandarino, L.J.2
  • 32
    • 0031752685 scopus 로고    scopus 로고
    • Global burden of diabetes, 1995-2025: Prevalence, numerical estimates, and projections
    • H. King, R.E. Aubert, and W.H. Herman Global burden of diabetes, 1995-2025: prevalence, numerical estimates, and projections Diabetes Care 21 1998 1414 1431
    • (1998) Diabetes Care , vol.21 , pp. 1414-1431
    • King, H.1    Aubert, R.E.2    Herman, W.H.3
  • 39
    • 0027762766 scopus 로고
    • Insulin resistance and insulin secretory dysfunction as precursors of non-insulin-dependent diabetes mellitus. Prospective studies of Pima Indians
    • S. Lillioja, D.M. Mott, M. Spraul, R. Ferraro, J.E. Foley, E. Ravussin, W.C. Knowler, P.H. Bennett, and C. Bogardus Insulin resistance and insulin secretory dysfunction as precursors of non-insulin-dependent diabetes mellitus. Prospective studies of Pima Indians N. Engl. J. Med. 329 1993 1988 1992
    • (1993) N. Engl. J. Med. , vol.329 , pp. 1988-1992
    • Lillioja, S.1    Mott, D.M.2    Spraul, M.3    Ferraro, R.4    Foley, J.E.5    Ravussin, E.6    Knowler, W.C.7    Bennett, P.H.8    Bogardus, C.9
  • 41
    • 33644534186 scopus 로고    scopus 로고
    • Aging and the brown Norway rat leydig cell antioxidant defense system
    • L. Luo, H. Chen, M.A. Trush, M.D. Show, M.D. Anway, and B.R. Zirkin Aging and the brown Norway rat leydig cell antioxidant defense system J. Androl. 27 2006 240 247
    • (2006) J. Androl. , vol.27 , pp. 240-247
    • Luo, L.1    Chen, H.2    Trush, M.A.3    Show, M.D.4    Anway, M.D.5    Zirkin, B.R.6
  • 43
    • 23644434842 scopus 로고    scopus 로고
    • Physiological increases in uncoupling protein 3 augment fatty acid oxidation and decrease reactive oxygen species production without uncoupling respiration in muscle cells
    • J.D. MacLellan, M.F. Gerrits, A. Gowing, P.J. Smith, M.B. Wheeler, and M.E. Harper Physiological increases in uncoupling protein 3 augment fatty acid oxidation and decrease reactive oxygen species production without uncoupling respiration in muscle cells Diabetes 54 2005 2343 2350
    • (2005) Diabetes , vol.54 , pp. 2343-2350
    • MacLellan, J.D.1    Gerrits, M.F.2    Gowing, A.3    Smith, P.J.4    Wheeler, M.B.5    Harper, M.E.6
  • 44
    • 0037177592 scopus 로고    scopus 로고
    • Unraveling the causes of diabetes
    • J. Marx Unraveling the causes of diabetes Science 296 2002 686 689
    • (2002) Science , vol.296 , pp. 686-689
    • Marx, J.1
  • 45
    • 0026468362 scopus 로고
    • What if Minkowski had been ageusic? An alternative angle on diabetes
    • J.D. McGarry What if Minkowski had been ageusic? An alternative angle on diabetes Science 258 1992 766 770
    • (1992) Science , vol.258 , pp. 766-770
    • McGarry, J.D.1
  • 46
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • G.A. McQuibban, S. Saurya, and M. Freeman Mitochondrial membrane remodelling regulated by a conserved rhomboid protease Nature 423 2003 537 541
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 47
    • 34548084014 scopus 로고    scopus 로고
    • Macroautophagy: Protector in the diabetes drama?
    • A.J. Meijer, and P. Codogno Macroautophagy: protector in the diabetes drama? Autophagy 3 2007 523 526
    • (2007) Autophagy , vol.3 , pp. 523-526
    • Meijer, A.J.1    Codogno, P.2
  • 50
    • 67349125152 scopus 로고    scopus 로고
    • Loss of Drp1 function alters OPA1 processing and changes mitochondrial membrane organization
    • K. Mopert, P. Hajek, S. Frank, C. Chen, J. Kaufmann, and A. Santel Loss of Drp1 function alters OPA1 processing and changes mitochondrial membrane organization Exp. Cell Res. 315 2009 2165 2180
    • (2009) Exp. Cell Res. , vol.315 , pp. 2165-2180
    • Mopert, K.1    Hajek, P.2    Frank, S.3    Chen, C.4    Kaufmann, J.5    Santel, A.6
  • 51
    • 31044433308 scopus 로고    scopus 로고
    • Reduced mitochondrial density and increased IRS-1 serine phosphorylation in muscle of insulin-resistant offspring of type 2 diabetic parents
    • K. Morino, K.F. Petersen, S. Dufour, D. Befroy, J. Frattini, N. Shatzkes, S. Neschen, M.F. White, S. Bilz, and S. Sono Reduced mitochondrial density and increased IRS-1 serine phosphorylation in muscle of insulin-resistant offspring of type 2 diabetic parents J. Clin. Invest. 115 2005 3587 3593
    • (2005) J. Clin. Invest. , vol.115 , pp. 3587-3593
    • Morino, K.1    Petersen, K.F.2    Dufour, S.3    Befroy, D.4    Frattini, J.5    Shatzkes, N.6    Neschen, S.7    White, M.F.8    Bilz, S.9    Sono, S.10
  • 52
    • 0035050152 scopus 로고    scopus 로고
    • Muscle-specific overexpression of the adenovirus primary receptor CAR overcomes low efficiency of gene transfer to mature skeletal muscle
    • J. Nalbantoglu, N. Larochelle, E. Wolf, G. Karpati, H. Lochmuller, and P.C. Holland Muscle-specific overexpression of the adenovirus primary receptor CAR overcomes low efficiency of gene transfer to mature skeletal muscle J. Virol. 75 2001 4276 4282
    • (2001) J. Virol. , vol.75 , pp. 4276-4282
    • Nalbantoglu, J.1    Larochelle, N.2    Wolf, E.3    Karpati, G.4    Lochmuller, H.5    Holland, P.C.6
  • 53
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1alpha
    • S. Nemoto, M.M. Fergusson, and T. Finkel SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1alpha J. Biol. Chem. 280 2005 16456 16460
    • (2005) J. Biol. Chem. , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 56
    • 34250768073 scopus 로고    scopus 로고
    • A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis
    • L. Pellegrini, and L. Scorrano A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis Cell Death Differ. 14 2007 1275 1284
    • (2007) Cell Death Differ. , vol.14 , pp. 1275-1284
    • Pellegrini, L.1    Scorrano, L.2
  • 57
    • 0032764784 scopus 로고    scopus 로고
    • Intramyocellular triglyceride content is a determinant of in vivo insulin resistance in humans: A 1H-13C nuclear magnetic resonance spectroscopy assessment in offspring of type 2 diabetic parents
    • G. Perseghin, P. Scifo, F. De Cobelli, E. Pagliato, A. Battezzati, C. Arcelloni, A. Vanzulli, G. Testolin, G. Pozza, A. Del Maschio, and L. Luzi Intramyocellular triglyceride content is a determinant of in vivo insulin resistance in humans: a 1H-13C nuclear magnetic resonance spectroscopy assessment in offspring of type 2 diabetic parents Diabetes 48 1999 1600 1606
    • (1999) Diabetes , vol.48 , pp. 1600-1606
    • Perseghin, G.1    Scifo, P.2    De Cobelli, F.3    Pagliato, E.4    Battezzati, A.5    Arcelloni, C.6    Vanzulli, A.7    Testolin, G.8    Pozza, G.9    Del Maschio, A.10    Luzi, L.11
  • 59
    • 1642377274 scopus 로고    scopus 로고
    • Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes
    • K.F. Petersen, S. Dufour, D. Befroy, R. Garcia, and G.I. Shulman Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes N. Engl. J. Med. 350 2004 664 671
    • (2004) N. Engl. J. Med. , vol.350 , pp. 664-671
    • Petersen, K.F.1    Dufour, S.2    Befroy, D.3    Garcia, R.4    Shulman, G.I.5
  • 60
    • 25644448096 scopus 로고    scopus 로고
    • Decreased insulin-stimulated ATP synthesis and phosphate transport in muscle of insulin-resistant offspring of type 2 diabetic parents
    • K.F. Petersen, S. Dufour, and G.I. Shulman Decreased insulin-stimulated ATP synthesis and phosphate transport in muscle of insulin-resistant offspring of type 2 diabetic parents PLoS Med. 2 2005 e233
    • (2005) PLoS Med. , vol.2 , pp. 233
    • Petersen, K.F.1    Dufour, S.2    Shulman, G.I.3
  • 64
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • J.T. Rodgers, C. Lerin, W. Haas, S.P. Gygi, B.M. Spiegelman, and P. Puigserver Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1 Nature 434 2005 113 118
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 65
    • 42049114034 scopus 로고    scopus 로고
    • Transcriptional paradigms in mammalian mitochondrial biogenesis and function
    • R.C. Scarpulla Transcriptional paradigms in mammalian mitochondrial biogenesis and function Physiol. Rev. 88 2008 611 638
    • (2008) Physiol. Rev. , vol.88 , pp. 611-638
    • Scarpulla, R.C.1
  • 66
    • 33750427891 scopus 로고    scopus 로고
    • PGC1alpha expression is controlled in skeletal muscles by PPARbeta, whose ablation results in fiber-type switching, obesity, and type 2 diabetes
    • M. Schuler, F. Ali, C. Chambon, D. Duteil, J.M. Bornert, A. Tardivel, B. Desvergne, W. Wahli, P. Chambon, and D. Metzger PGC1alpha expression is controlled in skeletal muscles by PPARbeta, whose ablation results in fiber-type switching, obesity, and type 2 diabetes Cell Metab. 4 2006 407 414
    • (2006) Cell Metab. , vol.4 , pp. 407-414
    • Schuler, M.1    Ali, F.2    Chambon, C.3    Duteil, D.4    Bornert, J.M.5    Tardivel, A.6    Desvergne, B.7    Wahli, W.8    Chambon, P.9    Metzger, D.10
  • 67
    • 0043095416 scopus 로고    scopus 로고
    • Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion
    • H. Sesaki, S.M. Southard, A.E. Hobbs, and R.E. Jensen Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion Biochem. Biophys. Res. Commun. 308 2003 276 283
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 276-283
    • Sesaki, H.1    Southard, S.M.2    Hobbs, A.E.3    Jensen, R.E.4
  • 68
    • 2442490089 scopus 로고    scopus 로고
    • Self-regulated cleavage of the mitochondrial intramembrane-cleaving protease PARL yields Pbeta, a nuclear-targeted peptide
    • A. Sík, B.J. Passer, E.V. Koonin, and L. Pellegrini Self-regulated cleavage of the mitochondrial intramembrane-cleaving protease PARL yields Pbeta, a nuclear-targeted peptide J. Biol. Chem. 279 2004 15323 15329
    • (2004) J. Biol. Chem. , vol.279 , pp. 15323-15329
    • Sík, A.1    Passer, B.J.2    Koonin, E.V.3    Pellegrini, L.4
  • 69
    • 0035146891 scopus 로고    scopus 로고
    • Mitochondrial filaments and clusters as intracellular power-transmitting cables
    • V.P. Skulachev Mitochondrial filaments and clusters as intracellular power-transmitting cables Trends Biochem. Sci. 26 2001 23 29
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 23-29
    • Skulachev, V.P.1
  • 71
    • 34247590356 scopus 로고    scopus 로고
    • PGC-1beta controls mitochondrial metabolism to modulate circadian activity, adaptive thermogenesis, and hepatic steatosis
    • J. Sonoda, I.R. Mehl, L.W. Chong, R.R. Nofsinger, and R.M. Evans PGC-1beta controls mitochondrial metabolism to modulate circadian activity, adaptive thermogenesis, and hepatic steatosis Proc. Natl. Acad. Sci. USA 104 2007 5223 5228
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5223-5228
    • Sonoda, J.1    Mehl, I.R.2    Chong, L.W.3    Nofsinger, R.R.4    Evans, R.M.5
  • 72
    • 21344444333 scopus 로고    scopus 로고
    • A high-fat diet coordinately downregulates genes required for mitochondrial oxidative phosphorylation in skeletal muscle
    • L.M. Sparks, H. Xie, R.A. Koza, R. Mynatt, M.W. Hulver, G.A. Bray, and S.R. Smith A high-fat diet coordinately downregulates genes required for mitochondrial oxidative phosphorylation in skeletal muscle Diabetes 54 2005 1926 1933
    • (2005) Diabetes , vol.54 , pp. 1926-1933
    • Sparks, L.M.1    Xie, H.2    Koza, R.A.3    Mynatt, R.4    Hulver, M.W.5    Bray, G.A.6    Smith, S.R.7
  • 73
    • 33749579213 scopus 로고    scopus 로고
    • High-fat/low-carbohydrate diets regulate glucose metabolism via a long-term transcriptional loop
    • L.M. Sparks, H. Xie, R.A. Koza, R. Mynatt, G.A. Bray, and S.R. Smith High-fat/low-carbohydrate diets regulate glucose metabolism via a long-term transcriptional loop Metabolism 55 2006 1457 1463
    • (2006) Metabolism , vol.55 , pp. 1457-1463
    • Sparks, L.M.1    Xie, H.2    Koza, R.A.3    Mynatt, R.4    Bray, G.A.5    Smith, S.R.6
  • 74
    • 1842479419 scopus 로고    scopus 로고
    • Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology
    • D. Stojanovski, O.S. Koutsopoulos, K. Okamoto, and M.T. Ryan Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology J. Cell Sci. 117 2004 1201 1210
    • (2004) J. Cell Sci. , vol.117 , pp. 1201-1210
    • Stojanovski, D.1    Koutsopoulos, O.S.2    Okamoto, K.3    Ryan, M.T.4
  • 77
    • 20444452139 scopus 로고    scopus 로고
    • Effect of elevated lipid concentrations on human skeletal muscle gene expression
    • R.J. Tunstall, and D. Cameron-Smith Effect of elevated lipid concentrations on human skeletal muscle gene expression Metabolism 54 2005 952 959
    • (2005) Metabolism , vol.54 , pp. 952-959
    • Tunstall, R.J.1    Cameron-Smith, D.2
  • 79
    • 22144472218 scopus 로고    scopus 로고
    • Dynamic changes in fat oxidation in human primary myocytes mirror metabolic characteristics of the donor
    • B. Ukropcova, M. McNeil, O. Sereda, L. de Jonge, H. Xie, G.A. Bray, and S.R. Smith Dynamic changes in fat oxidation in human primary myocytes mirror metabolic characteristics of the donor J. Clin. Invest. 115 2005 1934 1941
    • (2005) J. Clin. Invest. , vol.115 , pp. 1934-1941
    • Ukropcova, B.1    McNeil, M.2    Sereda, O.3    De Jonge, L.4    Xie, H.5    Bray, G.A.6    Smith, S.R.7
  • 80
    • 33847344733 scopus 로고    scopus 로고
    • Family history of diabetes links impaired substrate switching and reduced mitochondrial content in skeletal muscle
    • B. Ukropcova, O. Sereda, L. de Jonge, I. Bogacka, T. Nguyen, H. Xie, G.A. Bray, and S.R. Smith Family history of diabetes links impaired substrate switching and reduced mitochondrial content in skeletal muscle Diabetes 56 2007 720 727
    • (2007) Diabetes , vol.56 , pp. 720-727
    • Ukropcova, B.1    Sereda, O.2    De Jonge, L.3    Bogacka, I.4    Nguyen, T.5    Xie, H.6    Bray, G.A.7    Smith, S.R.8
  • 82
    • 0032898197 scopus 로고    scopus 로고
    • Relationships between muscle mitochondrial DNA content, mitochondrial enzyme activity and oxidative capacity in man: Alterations with disease
    • H. Wang, W.R. Hiatt, T.J. Barstow, and E.P. Brass Relationships between muscle mitochondrial DNA content, mitochondrial enzyme activity and oxidative capacity in man: alterations with disease Eur. J. Appl. Physiol. Occup. Physiol. 80 1999 22 27
    • (1999) Eur. J. Appl. Physiol. Occup. Physiol. , vol.80 , pp. 22-27
    • Wang, H.1    Hiatt, W.R.2    Barstow, T.J.3    Brass, E.P.4
  • 83
    • 25644432770 scopus 로고    scopus 로고
    • Contributions of the ubiquitin-proteasome pathway and apoptosis to human skeletal muscle wasting with age
    • S.A. Whitman, M.J. Wacker, S.R. Richmond, and M.P. Godard Contributions of the ubiquitin-proteasome pathway and apoptosis to human skeletal muscle wasting with age Pflugers Arch. 450 2005 437 446
    • (2005) Pflugers Arch. , vol.450 , pp. 437-446
    • Whitman, S.A.1    Wacker, M.J.2    Richmond, S.R.3    Godard, M.P.4
  • 85
    • 0037184925 scopus 로고    scopus 로고
    • Mechanism by which fatty acids inhibit insulin activation of insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol 3-kinase activity in muscle
    • C. Yu, Y. Chen, G.W. Cline, D. Zhang, H. Zong, Y. Wang, R. Bergeron, J.K. Kim, S.W. Cushman, and G.J. Cooney Mechanism by which fatty acids inhibit insulin activation of insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol 3-kinase activity in muscle J. Biol. Chem. 277 2002 50230 50236
    • (2002) J. Biol. Chem. , vol.277 , pp. 50230-50236
    • Yu, C.1    Chen, Y.2    Cline, G.W.3    Zhang, D.4    Zong, H.5    Wang, Y.6    Bergeron, R.7    Kim, J.K.8    Cushman, S.W.9    Cooney, G.J.10
  • 86
    • 33644552417 scopus 로고    scopus 로고
    • Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology
    • T. Yu, J.L. Robotham, and Y. Yoon Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology Proc. Natl. Acad. Sci. USA 103 2006 2653 2658
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2653-2658
    • Yu, T.1    Robotham, J.L.2    Yoon, Y.3
  • 87
    • 36749082168 scopus 로고    scopus 로고
    • Mitochondrial dysfunction due to long-chain Acyl-CoA dehydrogenase deficiency causes hepatic steatosis and hepatic insulin resistance
    • D. Zhang, Z.X. Liu, C.S. Choi, L. Tian, R. Kibbey, J. Dong, G.W. Cline, P.A. Wood, and G.I. Shulman Mitochondrial dysfunction due to long-chain Acyl-CoA dehydrogenase deficiency causes hepatic steatosis and hepatic insulin resistance Proc. Natl. Acad. Sci. USA 104 2007 17075 17080
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17075-17080
    • Zhang, D.1    Liu, Z.X.2    Choi, C.S.3    Tian, L.4    Kibbey, R.5    Dong, J.6    Cline, G.W.7    Wood, P.A.8    Shulman, G.I.9
  • 88
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • P. Zimmet, K.G. Alberti, and J. Shaw Global and societal implications of the diabetes epidemic Nature 414 2001 782 787
    • (2001) Nature , vol.414 , pp. 782-787
    • Zimmet, P.1    Alberti, K.G.2    Shaw, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.