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Volumn 93, Issue , 2016, Pages 32-40

PGC-1α overexpression via local transfection attenuates mitophagy pathway in muscle disuse atrophy

Author keywords

Apoptosis; Immobilization; Mitochondria; Mitophagy; Muscle; Muscle disuse a trophy; Oxidative stress; PGC 1 overexpression

Indexed keywords

ANTIOXIDANT; BECLIN 1; CASPASE 3; MICROTUBULE ASSOCIATED PROTEIN 1A; MICROTUBULE ASSOCIATED PROTEIN 5; MITOCHONDRIAL DNA; MITOCHONDRIAL E3 UBIQUITIN PROTEIN LIGASE 1; OXIDOREDUCTASE; PARKIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BNIP3; PTEN INDUCED PUTATIVE KINASE 1; TRANSCRIPTION FACTOR FOXO; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; PPARGC1A PROTEIN, MOUSE; REACTIVE OXYGEN METABOLITE;

EID: 84957871047     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2015.12.032     Document Type: Article
Times cited : (71)

References (37)
  • 2
    • 84890379609 scopus 로고    scopus 로고
    • Muscle immobilization and remobilization downregulates PGC-1α signaling and the mitochondrial biogenesis pathway
    • C. Kang, and L.L. Ji Muscle immobilization and remobilization downregulates PGC-1α signaling and the mitochondrial biogenesis pathway J. Appl. Physiol. 115 2013 1618 1625
    • (2013) J. Appl. Physiol. , vol.115 , pp. 1618-1625
    • Kang, C.1    Ji, L.L.2
  • 3
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of muscle wasting - the role of the ubiquitin-proteasome pathway
    • F.H. Epstein, W.E. Mitch, and A.L. Goldberg Mechanisms of muscle wasting - the role of the ubiquitin-proteasome pathway N. Engl. J. Med. 335 1996 1897 1905
    • (1996) N. Engl. J. Med. , vol.335 , pp. 1897-1905
    • Epstein, F.H.1    Mitch, W.E.2    Goldberg, A.L.3
  • 9
    • 84872094183 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of muscle atrophy
    • P. Bonaldo, and M. Sandri Cellular and molecular mechanisms of muscle atrophy Dis. Model Mech. 6 2013 25 39
    • (2013) Dis. Model Mech. , vol.6 , pp. 25-39
    • Bonaldo, P.1    Sandri, M.2
  • 10
    • 84899450195 scopus 로고    scopus 로고
    • FoxO transcription factors: their roles in the maintenance of skeletal muscle homeostasis
    • A.M. Sanchez, R.B. Candau, and H. Bernardi FoxO transcription factors: their roles in the maintenance of skeletal muscle homeostasis Cell. Mol. Life Sci. 71 2014 1657 1671
    • (2014) Cell. Mol. Life Sci. , vol.71 , pp. 1657-1671
    • Sanchez, A.M.1    Candau, R.B.2    Bernardi, H.3
  • 11
    • 73949088946 scopus 로고    scopus 로고
    • Ros-mediated activation of NF-κB and foxo during muscle disuse
    • S.L. Dodd, B.J. Gagnon, S.M. Senf, B.A. Hain, and A.R. Judge Ros-mediated activation of NF-κB and foxo during muscle disuse Muscle Nerve 41 2010 110 113
    • (2010) Muscle Nerve , vol.41 , pp. 110-113
    • Dodd, S.L.1    Gagnon, B.J.2    Senf, S.M.3    Hain, B.A.4    Judge, A.R.5
  • 12
    • 84927127813 scopus 로고    scopus 로고
    • 2 production in mouse skeletal muscle: association with p 66Shc and FOXO3a signaling and antioxidant enzymes
    • 2 production in mouse skeletal muscle: association with p 66Shc and FOXO3a signaling and antioxidant enzymes Oxid. Med. Cell. Longev. 2015 2015 Article ID 536456 10 pp.
    • (2015) Oxid. Med. Cell. Longev. , vol.2015
    • Wang, P.1    Li, C.G.2    Qi, Z.3    Cui, D.4    Ding, S.5
  • 15
    • 47949104798 scopus 로고    scopus 로고
    • The role of exercise and PGC1α in inflammation and chronic disease
    • C. Handschin, and B.M. Spiegelman The role of exercise and PGC1α in inflammation and chronic disease Nature 454 2008 463 469
    • (2008) Nature , vol.454 , pp. 463-469
    • Handschin, C.1    Spiegelman, B.M.2
  • 16
    • 84893567123 scopus 로고    scopus 로고
    • Reloading functionally ameliorates disuse-induced muscle atrophy by reversing mitochondrial dysfunction, and similar benefits are gained by administering a combination of mitochondrial nutrients
    • J. Liu, Y. Peng, Z. Feng, W. Shi, L. Qu, Y. Li, J. Liu, and J. Long Reloading functionally ameliorates disuse-induced muscle atrophy by reversing mitochondrial dysfunction, and similar benefits are gained by administering a combination of mitochondrial nutrients Free Radic. Biol. Med. 69 2014 116 128
    • (2014) Free Radic. Biol. Med. , vol.69 , pp. 116-128
    • Liu, J.1    Peng, Y.2    Feng, Z.3    Shi, W.4    Qu, L.5    Li, Y.6    Liu, J.7    Long, J.8
  • 17
    • 84946945269 scopus 로고    scopus 로고
    • PGC-1alpha overexpression by in vivo transfection attenuates mitochondrial deterioration of skeletal muscle caused by immobilization
    • C. Kang, C.A. Goodman, T.A. Hornberger, and L.L. Ji PGC-1alpha overexpression by in vivo transfection attenuates mitochondrial deterioration of skeletal muscle caused by immobilization FASEB J. 29 2015 4092 4106
    • (2015) FASEB J. , vol.29 , pp. 4092-4106
    • Kang, C.1    Goodman, C.A.2    Hornberger, T.A.3    Ji, L.L.4
  • 18
    • 84911906873 scopus 로고    scopus 로고
    • PGC1-alpha over-expression prevents metabolic alterations and soleus muscle atrophy in hindlimb unloaded mice
    • J. Cannavino, L. Brocca, M. Sandri, R. Bottinelli, and M.A. Pellegrino PGC1-alpha over-expression prevents metabolic alterations and soleus muscle atrophy in hindlimb unloaded mice J. Physiol. 592 2014 4575 4589
    • (2014) J. Physiol. , vol.592 , pp. 4575-4589
    • Cannavino, J.1    Brocca, L.2    Sandri, M.3    Bottinelli, R.4    Pellegrino, M.A.5
  • 19
    • 73949099327 scopus 로고    scopus 로고
    • Increased muscle PGC-1α expression protects from sarcopenia and metabolic disease during aging
    • T. Wenz, S.G. Rossi, R.L. Rotundo, B.M. Spiegelman, and C.T. Moraes Increased muscle PGC-1α expression protects from sarcopenia and metabolic disease during aging Proc. Natl. Acad. Sci. 106 2009 20405 20410
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 20405-20410
    • Wenz, T.1    Rossi, S.G.2    Rotundo, R.L.3    Spiegelman, B.M.4    Moraes, C.T.5
  • 20
    • 84555195856 scopus 로고    scopus 로고
    • Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling
    • J. Lee, G. Samantha, and Z. Jianhua Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling Biochem. J. 441 2012 523 540
    • (2012) Biochem. J. , vol.441 , pp. 523-540
    • Lee, J.1    Samantha, G.2    Jianhua, Z.3
  • 21
    • 84927946082 scopus 로고    scopus 로고
    • PGC-1α buffers ROS-mediated removal of mitochondria during myogenesis
    • S. Baldelli, K. Aquilano, and M. Ciriolo PGC-1α buffers ROS-mediated removal of mitochondria during myogenesis Cell Death Dis. 5 2014 e1515
    • (2014) Cell Death Dis. , vol.5
    • Baldelli, S.1    Aquilano, K.2    Ciriolo, M.3
  • 22
    • 84902682891 scopus 로고    scopus 로고
    • MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin
    • J. Yun, R. Puri, H. Yang, M.A. Lizzio, C. Wu, Z. Sheng, and M. Guo MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin Elife 3 2014 e01958
    • (2014) Elife , vol.3
    • Yun, J.1    Puri, R.2    Yang, H.3    Lizzio, M.A.4    Wu, C.5    Sheng, Z.6    Guo, M.7
  • 23
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
    • H. Chen, M. Vermulst, Y.E. Wang, A. Chomyn, T.A. Prolla, J.M. McCaffery, and D.C. Chan Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations Cell 141 2010 280 289
    • (2010) Cell , vol.141 , pp. 280-289
    • Chen, H.1    Vermulst, M.2    Wang, Y.E.3    Chomyn, A.4    Prolla, T.A.5    McCaffery, J.M.6    Chan, D.C.7
  • 24
    • 84855532023 scopus 로고    scopus 로고
    • AMPK promotes skeletal muscle autophagy through activation of forkhead FoxO3a and interaction with Ulk1
    • A.M. Sanchez, A. Csibi, A. Raibon, K. Cornille, S. Gay, H. Bernardi, and R. Candau AMPK promotes skeletal muscle autophagy through activation of forkhead FoxO3a and interaction with Ulk1 J. Cell. Biochem. 113 2012 695 710
    • (2012) J. Cell. Biochem. , vol.113 , pp. 695-710
    • Sanchez, A.M.1    Csibi, A.2    Raibon, A.3    Cornille, K.4    Gay, S.5    Bernardi, H.6    Candau, R.7
  • 26
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • J. Zhao, J.J. Brault, A. Schild, P. Cao, M. Sandri, S. Schiaffino, S.H. Lecker, and A.L. Goldberg FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells Cell Metab. 6 2007 472 483
    • (2007) Cell Metab. , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6    Lecker, S.H.7    Goldberg, A.L.8
  • 27
    • 33750445482 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in mammals
    • D.C. Chan Mitochondrial fusion and fission in mammals Annu. Rev. Cell Dev. Biol. 22 2006 79 99
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 79-99
    • Chan, D.C.1
  • 29
    • 39149102870 scopus 로고    scopus 로고
    • Stimulation of mitochondrial biogenesis and autophagy by lipopolysaccharide in the neonatal rat cardiomyocyte protects against programmed cell death
    • D.L. Hickson-Bick, C. Jones, and L.M. Buja Stimulation of mitochondrial biogenesis and autophagy by lipopolysaccharide in the neonatal rat cardiomyocyte protects against programmed cell death J. Mol. Cell. Cardiol. 44 2008 411 418
    • (2008) J. Mol. Cell. Cardiol. , vol.44 , pp. 411-418
    • Hickson-Bick, D.L.1    Jones, C.2    Buja, L.M.3
  • 31
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • M.L. Circu, and T.Y. Aw Reactive oxygen species, cellular redox systems, and apoptosis Free Radic. Biol. Med. 48 2010 749 762
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 32
    • 0037879052 scopus 로고    scopus 로고
    • The mitochondrial membrane potential (δψm) in apoptosis; an update
    • J.D. Ly, D. Grubb, and A. Lawen The mitochondrial membrane potential (δψm) in apoptosis; an update Apoptosis 8 2003 115 128
    • (2003) Apoptosis , vol.8 , pp. 115-128
    • Ly, J.D.1    Grubb, D.2    Lawen, A.3
  • 33
    • 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, and W.E. Mitch Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions J. Clin. Investig. 113 2004 115 123
    • (2004) J. Clin. Investig. , 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
  • 34
    • 0034161884 scopus 로고    scopus 로고
    • Cell death in denervated skeletal muscle is distinct from classical apoptosis
    • A.B. Borisov, and B.M. Carlson Cell death in denervated skeletal muscle is distinct from classical apoptosis Anat. Rec. 258 2000 305 318
    • (2000) Anat. Rec. , vol.258 , pp. 305-318
    • Borisov, A.B.1    Carlson, B.M.2
  • 35
    • 25844516560 scopus 로고    scopus 로고
    • Apoptotic responses to hindlimb suspension in gastrocnemius muscles from young adult and aged rats
    • P.M. Siu, E.E. Pistilli, and S.E. Alway Apoptotic responses to hindlimb suspension in gastrocnemius muscles from young adult and aged rats Am. J. Physiol. Regul. Integr. Comp. Physiol. 289 2005 R1015 R1026
    • (2005) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.289 , pp. R1015-R1026
    • Siu, P.M.1    Pistilli, E.E.2    Alway, S.E.3


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