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Volumn 181, Issue 2, 2012, Pages 583-592

AMPK activation stimulates autophagy and ameliorates muscular dystrophy in the mdx mouse diaphragm

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINO 4 IMIDAZOLECARBOXAMIDE RIBOSIDE; ACETYL COENZYME A CARBOXYLASE; CALCIUM; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE ALPHA; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1BETA; PROTEIN BNIP3; UNCLASSIFIED DRUG; UTROPHIN;

EID: 84864124772     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2012.04.004     Document Type: Article
Times cited : (182)

References (50)
  • 1
    • 0023614271 scopus 로고
    • Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals
    • M. Koenig, E.P. Hoffman, C.J. Bertelson, A.P. Monaco, C. Feener, L.M. Kunkel Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals Cell 50 1987 509 517
    • (1987) Cell , vol.50 , pp. 509-517
    • Koenig, M.1    Hoffman, E.P.2    Bertelson, C.J.3    Monaco, A.P.4    Feener, C.5    Kunkel, L.M.6
  • 4
    • 0036839039 scopus 로고    scopus 로고
    • Molecular pathophysiology of myofiber injury in deficiencies of the dystrophin-glycoprotein complex
    • B.J. Petrof Molecular pathophysiology of myofiber injury in deficiencies of the dystrophin-glycoprotein complex Am J Phys Med Rehabil 81 11 Suppl 2002 S162 S174
    • (2002) Am J Phys Med Rehabil , vol.81 , Issue.11 SUPPL.
    • Petrof, B.J.1
  • 5
    • 0031800369 scopus 로고    scopus 로고
    • Impaired mitochondrial oxidative phosphorylation in skeletal muscle of the dystrophin-deficient mdx mouse
    • A.V. Kuznetsov, K. Winkler, F.R. Wiedemann, B.P. von, K. Dietzmann, W.S. Kunz Impaired mitochondrial oxidative phosphorylation in skeletal muscle of the dystrophin-deficient mdx mouse Mol Cell Biochem 183 1998 87 96
    • (1998) Mol Cell Biochem , vol.183 , pp. 87-96
    • Kuznetsov, A.V.1    Winkler, K.2    Wiedemann, F.R.3    Von, B.P.4    Dietzmann, K.5    Kunz, W.S.6
  • 6
    • 0034638834 scopus 로고    scopus 로고
    • Expression profiling in the muscular dystrophies: Identification of novel aspects of molecular pathophysiology
    • Y.W. Chen, P. Zhao, R. Borup, E.P. Hoffman Expression profiling in the muscular dystrophies: identification of novel aspects of molecular pathophysiology J Cell Biol 151 2000 1321 1336
    • (2000) J Cell Biol , vol.151 , pp. 1321-1336
    • Chen, Y.W.1    Zhao, P.2    Borup, R.3    Hoffman, E.P.4
  • 7
    • 34147109662 scopus 로고    scopus 로고
    • PGC-1alpha regulates the neuromuscular junction program and ameliorates Duchenne muscular dystrophy
    • C. Handschin, Y.M. Kobayashi, S. Chin, P. Seale, K.P. Campbell, B.M. Spiegelman PGC-1alpha regulates the neuromuscular junction program and ameliorates Duchenne muscular dystrophy Genes Dev 21 2007 770 783
    • (2007) Genes Dev , vol.21 , pp. 770-783
    • Handschin, C.1    Kobayashi, Y.M.2    Chin, S.3    Seale, P.4    Campbell, K.P.5    Spiegelman, B.M.6
  • 8
    • 34648828532 scopus 로고    scopus 로고
    • AMP-activated/SNF1 protein kinases: Conserved guardians of cellular energy
    • D.G. Hardie AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy Nat Rev Mol Cell Biol 8 2007 774 785
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 774-785
    • Hardie, D.G.1
  • 9
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • B. Levine, G. Kroemer Autophagy in the pathogenesis of disease Cell 132 2008 27 42
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 10
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • N. Mizushima, B. Levine, A.M. Cuervo, D.J. Klionsky Autophagy fights disease through cellular self-digestion Nature 451 2008 1069 1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 19
    • 13844303635 scopus 로고    scopus 로고
    • Alpha7B integrin changes in mdx mouse muscles after L-arginine administration
    • D. Chazalette, K. Hnia, F. Rivier, G. Hugon, D. Mornet alpha7B integrin changes in mdx mouse muscles after L-arginine administration FEBS Lett 579 2005 1079 1084
    • (2005) FEBS Lett , vol.579 , pp. 1079-1084
    • Chazalette, D.1    Hnia, K.2    Rivier, F.3    Hugon, G.4    Mornet, D.5
  • 21
    • 79951703669 scopus 로고    scopus 로고
    • Cyclophilin-D is dispensable for atrophy and mitochondrial apoptotic signalling in denervated muscle
    • F.N. Daussin, R. Godin, A. Ascah, S. Deschênes, Y. Burelle Cyclophilin-D is dispensable for atrophy and mitochondrial apoptotic signalling in denervated muscle J Physiol 589 2011 855 861
    • (2011) J Physiol , vol.589 , pp. 855-861
    • Daussin, F.N.1    Godin, R.2    Ascah, A.3    Deschênes, S.4    Burelle, Y.5
  • 24
    • 84862908818 scopus 로고    scopus 로고
    • AMPK and mTOR in cellular energy homeostasis and drug targets
    • K. Inoki, J. Kim, K.L. Guan AMPK and mTOR in cellular energy homeostasis and drug targets Annu Rev Pharmacol Toxicol 52 2012 381 400
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 381-400
    • Inoki, K.1    Kim, J.2    Guan, K.L.3
  • 25
    • 80051692198 scopus 로고    scopus 로고
    • Chronic AMPK activation evokes the slow, oxidative myogenic program and triggers beneficial adaptations in mdx mouse skeletal muscle
    • V. Ljubicic, P. Miura, M. Burt, L. Boudreault, S. Khogali, J.A. Lunde, J.M. Renaud, B.J. Jasmin Chronic AMPK activation evokes the slow, oxidative myogenic program and triggers beneficial adaptations in mdx mouse skeletal muscle Hum Mol Genet 20 2011 3478 3493
    • (2011) Hum Mol Genet , vol.20 , pp. 3478-3493
    • Ljubicic, V.1    Miura, P.2    Burt, M.3    Boudreault, L.4    Khogali, S.5    Lunde, J.A.6    Renaud, J.M.7    Jasmin, B.J.8
  • 26
    • 0023697916 scopus 로고
    • Small-caliber skeletal muscle fibers do not suffer necrosis in mdx mouse dystrophy
    • G. Karpati, S. Carpenter, S. Prescott Small-caliber skeletal muscle fibers do not suffer necrosis in mdx mouse dystrophy Muscle Nerve 11 1988 795 803
    • (1988) Muscle Nerve , vol.11 , pp. 795-803
    • Karpati, G.1    Carpenter, S.2    Prescott, S.3
  • 27
    • 0031907287 scopus 로고    scopus 로고
    • Adenovirus-mediated dystrophin minigene transfer improves muscle strength in adult dystrophic (mdx) mice
    • L. Yang, H. Lochmüller, J. Luo, B. Massie, J. Nalbantoglu, G. Karpati, B.J. Petrof Adenovirus-mediated dystrophin minigene transfer improves muscle strength in adult dystrophic (mdx) mice Gene Ther 5 1998 369 379
    • (1998) Gene Ther , vol.5 , pp. 369-379
    • Yang, L.1    Lochmüller, H.2    Luo, J.3    Massie, B.4    Nalbantoglu, J.5    Karpati, G.6    Petrof, B.J.7
  • 28
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • J. Du, X. Wang, C. Miereles, J.L. Bailey, R. Debigare, B. Zheng, S.R. Price, W.E. Mitch Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions J Clin Invest 113 2004 115 123
    • (2004) J Clin Invest , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6    Price, S.R.7    Mitch, W.E.8
  • 30
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • Y. Wei, S. Pattingre, S. Sinha, M. Bassik, B. Levine JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy Mol Cell 30 2008 678 688
    • (2008) Mol Cell , vol.30 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3    Bassik, M.4    Levine, B.5
  • 31
  • 32
    • 78149476877 scopus 로고    scopus 로고
    • The association of AMPK with ULK1 regulates autophagy
    • J.W. Lee, S. Park, Y. Takahashi, H.G. Wang The association of AMPK with ULK1 regulates autophagy PLoS One 5 2010 e15394
    • (2010) PLoS One , vol.5 , pp. 15394
    • Lee, J.W.1    Park, S.2    Takahashi, Y.3    Wang, H.G.4
  • 33
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • J. Kim, M. Kundu, B. Viollet, K.L. Guan AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1 Nat Cell Biol 13 2011 132 141
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 34
    • 84858780524 scopus 로고    scopus 로고
    • Rapamycin ameliorates dystrophic phenotype in mdx mouse skeletal muscle
    • S. Eghtesad, S. Jhunjhunwala, S.R. Little, P.R. Clemens Rapamycin ameliorates dystrophic phenotype in mdx mouse skeletal muscle Mol Med 17 2011 917 924
    • (2011) Mol Med , vol.17 , pp. 917-924
    • Eghtesad, S.1    Jhunjhunwala, S.2    Little, S.R.3    Clemens, P.R.4
  • 35
    • 77950479450 scopus 로고    scopus 로고
    • Autophagy in skeletal muscle
    • M. Sandri Autophagy in skeletal muscle FEBS Lett 584 2010 1411 1416
    • (2010) FEBS Lett , vol.584 , pp. 1411-1416
    • Sandri, M.1
  • 37
    • 57049094929 scopus 로고    scopus 로고
    • Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease
    • N. Raben, V. Hill, L. Shea, S. Takikita, R. Baum, N. Mizushima, E. Ralston, P. Plotz Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease Hum Mol Genet 17 2008 3897 3908
    • (2008) Hum Mol Genet , vol.17 , pp. 3897-3908
    • Raben, N.1    Hill, V.2    Shea, L.3    Takikita, S.4    Baum, R.5    Mizushima, N.6    Ralston, E.7    Plotz, P.8
  • 38
    • 68649108571 scopus 로고    scopus 로고
    • Characteristics and possible functions of mitochondrial Ca(2+) transport mechanisms
    • T.E. Gunter, S.S. Sheu Characteristics and possible functions of mitochondrial Ca(2+) transport mechanisms Biochim Biophys Acta 1787 2009 1291 1308
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1291-1308
    • Gunter, T.E.1    Sheu, S.S.2
  • 39
    • 80052627393 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in Ca(2+)-dependent apoptosis and necrosis
    • A. Rasola, P. Bernardi Mitochondrial permeability transition in Ca(2+)-dependent apoptosis and necrosis Cell Calcium 50 2011 222 233
    • (2011) Cell Calcium , vol.50 , pp. 222-233
    • Rasola, A.1    Bernardi, P.2
  • 40
    • 78249257768 scopus 로고    scopus 로고
    • Mitochondrial functional impairment with aging is exaggerated in isolated mitochondria compared to permeabilized myofibers
    • M. Picard, D. Ritchie, K.J. Wright, C. Romestaing, M.M. Thomas, S.L. Rowan, T. Taivassalo, R.T. Hepple Mitochondrial functional impairment with aging is exaggerated in isolated mitochondria compared to permeabilized myofibers Aging Cell 9 2010 1032 1046
    • (2010) Aging Cell , vol.9 , pp. 1032-1046
    • Picard, M.1    Ritchie, D.2    Wright, K.J.3    Romestaing, C.4    Thomas, M.M.5    Rowan, S.L.6    Taivassalo, T.7    Hepple, R.T.8
  • 44
    • 77957683915 scopus 로고    scopus 로고
    • Bnip3-mediated mitochondrial autophagy is independent of the mitochondrial permeability transition pore
    • M.N. Quinsay, R.L. Thomas, Y. Lee, A.B. Gustafsson Bnip3-mediated mitochondrial autophagy is independent of the mitochondrial permeability transition pore Autophagy 6 2010 855 862
    • (2010) Autophagy , vol.6 , pp. 855-862
    • Quinsay, M.N.1    Thomas, R.L.2    Lee, Y.3    Gustafsson, A.B.4
  • 45
    • 73949099327 scopus 로고    scopus 로고
    • Increased muscle PGC-1alpha expression protects from sarcopenia and metabolic disease during aging
    • T. Wenz, S.G. Rossi, R.L. Rotundo, B.M. Spiegelman, C.T. Moraes Increased muscle PGC-1alpha expression protects from sarcopenia and metabolic disease during aging Proc Natl Acad Sci USA 106 2009 20405 20410
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20405-20410
    • Wenz, T.1    Rossi, S.G.2    Rotundo, R.L.3    Spiegelman, B.M.4    Moraes, C.T.5
  • 48
    • 33744926902 scopus 로고    scopus 로고
    • Caspase activation contributes to endotoxin-induced diaphragm weakness
    • G.S. Supinski, L.A. Callahan Caspase activation contributes to endotoxin-induced diaphragm weakness J Appl Physiol 100 2006 1770 1777
    • (2006) J Appl Physiol , vol.100 , pp. 1770-1777
    • Supinski, G.S.1    Callahan, L.A.2
  • 49
    • 53849097675 scopus 로고    scopus 로고
    • Investigation of Debio 025, a cyclophilin inhibitor, in the dystrophic mdx mouse, a model for Duchenne muscular dystrophy
    • J. Reutenauer, O.M. Dorchies, O. Patthey-Vuadens, G. Vuagniaux, U.T. Ruegg Investigation of Debio 025, a cyclophilin inhibitor, in the dystrophic mdx mouse, a model for Duchenne muscular dystrophy Br J Pharmacol 155 2008 574 584
    • (2008) Br J Pharmacol , vol.155 , pp. 574-584
    • Reutenauer, J.1    Dorchies, O.M.2    Patthey-Vuadens, O.3    Vuagniaux, G.4    Ruegg, U.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.