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Volumn 4, Issue 3, 2011, Pages 269-278

Cellular and molecular mechanisms of apoptosis in age-related muscle atrophy

Author keywords

Aging; Mitochondria; p53; Sarcopenia; Skeletal muscle; Tumor necrosis factor alpha

Indexed keywords

APOPTOSOME; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE; CASPASE 10; CASPASE 12; CASPASE 8; CASPASE 9; CELL RECEPTOR; CYSTEINE PROTEINASE; CYTOCHROME C; ENDONUCLEASE G; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN P53; PROTEIN PRECURSOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 82955246250     PISSN: 18746098     EISSN: 18746128     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (22)

References (92)
  • 1
    • 0028863055 scopus 로고
    • Human aging, muscle mass, and fiber type composition
    • Lexell J. Human aging, muscle mass, and fiber type composition. J Gerontol A Biol Sci Med Sci 1995; 50 (Spec No): 11-6.
    • (1995) J Gerontol A Biol Sci Med Sci , vol.50 , Issue.SPEC. NO , pp. 11-16
    • Lexell, J.1
  • 2
    • 0142062997 scopus 로고    scopus 로고
    • Sarcopenia: Causes, consequences, and preventions
    • Marcell TJ. Sarcopenia: causes, consequences, and preventions. J Gerontol A Biol Sci Med Sci 2003; 58 (10): M911-6.
    • (2003) J Gerontol A Biol Sci Med Sci , vol.58 , Issue.10
    • Marcell, T.J.1
  • 3
    • 0031260095 scopus 로고    scopus 로고
    • Caloric restriction attenuates dityrosine cross-linking of cardiac and skeletal muscle proteins in aging mice
    • Leeuwenburgh C, Wagner P, Holloszy JO, Sohal RS, Heinecke JW. Caloric restriction attenuates dityrosine cross-linking of cardiac and skeletal muscle proteins in aging mice. Arch Biochem Biophys 1997; 346 (1): 74-80.
    • (1997) Arch Biochem Biophys , vol.346 , Issue.1 , pp. 74-80
    • Leeuwenburgh, C.1    Wagner, P.2    Holloszy, J.O.3    Sohal, R.S.4    Heinecke, J.W.5
  • 4
    • 0028849894 scopus 로고
    • Muscle atrophy and weakness with aging: Contraction-induced injury as an underlying mechanism
    • Faulkner JA, Brooks SV, Zerba E. Muscle atrophy and weakness with aging: contraction-induced injury as an underlying mechanism. J Gerontol A Biol Sci Med Sci 1995; 50 (Spec No): 124-9.
    • (1995) J Gerontol A Biol Sci Med Sci , vol.50 , Issue.SPEC. NO , pp. 124-129
    • Faulkner, J.A.1    Brooks, S.V.2    Zerba, E.3
  • 5
    • 0036089622 scopus 로고    scopus 로고
    • Mitochondrial abnormalities are more frequent in muscles undergoing sarcopenia
    • Bua EA, McKiernan SH, Wanagat J, McKenzie D, Aiken JM. Mitochondrial abnormalities are more frequent in muscles undergoing sarcopenia. J Appl Physiol 2002; 92 (6): 2617-24.
    • (2002) J Appl Physiol , vol.92 , Issue.6 , pp. 2617-2624
    • Bua, E.A.1    McKiernan, S.H.2    Wanagat, J.3    McKenzie, D.4    Aiken, J.M.5
  • 6
    • 33751432392 scopus 로고    scopus 로고
    • Elevated caspase and AIF gene expression correlate with progression of sarcopenia during aging in male F344BN rats
    • Baker DJ, Hepple RT. Elevated caspase and AIF gene expression correlate with progression of sarcopenia during aging in male F344BN rats. Exp Gerontol 2006; 41 (11): 1149-56.
    • (2006) Exp Gerontol , vol.41 , Issue.11 , pp. 1149-1156
    • Baker, D.J.1    Hepple, R.T.2
  • 7
    • 29644437922 scopus 로고    scopus 로고
    • Age-related alterations in expression of apoptosis regulatory proteins and heat shock proteins in rat skeletal muscle
    • Chung L, Ng YC. Age-related alterations in expression of apoptosis regulatory proteins and heat shock proteins in rat skeletal muscle. Biochim Biophys Acta 2006; 1762: 103-9.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 103-109
    • Chung, L.1    Ng, Y.C.2
  • 9
    • 0347318125 scopus 로고    scopus 로고
    • Aging and lifelong calorie restriction result in adaptations of skeletal muscle apoptosis repressor, apoptosis-inducing factor, X-linked inhibitor of apoptosis, caspase-3, and caspase-12
    • Dirks AJ, Leeuwenburgh C. Aging and lifelong calorie restriction result in adaptations of skeletal muscle apoptosis repressor, apoptosis-inducing factor, X-linked inhibitor of apoptosis, caspase-3, and caspase-12. Free Radic Biol Med 2004; 36 (1): 27-39.
    • (2004) Free Radic Biol Med , vol.36 , Issue.1 , pp. 27-39
    • Dirks, A.J.1    Leeuwenburgh, C.2
  • 10
    • 33745208498 scopus 로고    scopus 로고
    • Sarcopenia-related apoptosis is regulated differently in fast-and slow-twitch muscles of the aging F344/N x BN rat model
    • Rice KM, Blough ER. Sarcopenia-related apoptosis is regulated differently in fast-and slow-twitch muscles of the aging F344/N x BN rat model. Mech Ageing Dev 2006; 127 (8): 670-9.
    • (2006) Mech Ageing Dev , vol.127 , Issue.8 , pp. 670-679
    • Rice, K.M.1    Blough, E.R.2
  • 11
    • 33845373054 scopus 로고    scopus 로고
    • Death receptor-associated proapoptotic signaling in aged skeletal muscle
    • Pistilli EE, Jackson JR, Alway SE. Death receptor-associated proapoptotic signaling in aged skeletal muscle. Apoptosis 2006; 11 (12): 2115-26.
    • (2006) Apoptosis , vol.11 , Issue.12 , pp. 2115-2126
    • Pistilli, E.E.1    Jackson, J.R.2    Alway, S.E.3
  • 12
    • 33645972267 scopus 로고    scopus 로고
    • Molecular regulation of apoptosis in fast plantaris muscles of aged rats
    • Pistilli EE, Siu PM, Alway SE. Molecular regulation of apoptosis in fast plantaris muscles of aged rats. J Gerontol A Biol Sci Med Sci 2006; 61 (3): 245-55.
    • (2006) J Gerontol A Biol Sci Med Sci , vol.61 , Issue.3 , pp. 245-255
    • Pistilli, E.E.1    Siu, P.M.2    Alway, S.E.3
  • 13
    • 16344385647 scopus 로고    scopus 로고
    • Muscle fiber specific apoptosis and TNF-{alpha} signaling in sarcopenia are attenuated by life-long calorie restriction
    • Phillips T, Leeuwenburgh C. Muscle fiber specific apoptosis and TNF-{alpha} signaling in sarcopenia are attenuated by life-long calorie restriction. FASEB J 2005; 19 (6): 668-70.
    • (2005) FASEB J , vol.19 , Issue.6 , pp. 668-670
    • Phillips, T.1    Leeuwenburgh, C.2
  • 14
    • 33646697753 scopus 로고    scopus 로고
    • Exercise training attenuates ageinduced changes in apoptotic signaling in rat skeletal muscle
    • Song W, Kwak HB, Lawler JM. Exercise training attenuates ageinduced changes in apoptotic signaling in rat skeletal muscle. Antioxid Redox Signal 2006; 8 (3-4): 517-28.
    • (2006) Antioxid Redox Signal , vol.8 , Issue.3-4 , pp. 517-528
    • Song, W.1    Kwak, H.B.2    Lawler, J.M.3
  • 16
    • 25844516560 scopus 로고    scopus 로고
    • Apoptotic responses to hindlimb suspension in gastrocnemius muscles from young adult and aged rats
    • Siu PM, Pistilli EE, Alway SE. Apoptotic responses to hindlimb suspension in gastrocnemius muscles from young adult and aged rats. Am J Physiol Regul Integr Comp Physiol 2005; 289 (4): R1015-26.
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.289 , Issue.4
    • Siu, P.M.1    Pistilli, E.E.2    Alway, S.E.3
  • 17
    • 36249011363 scopus 로고    scopus 로고
    • Agedependent upregulation of p53 and cytochrome c release and susceptibility to apoptosis in skeletal muscle fiber of aged rats: Role of carnitine and lipoic acid
    • Tamilselvan J, Jayaraman G, Sivarajan K, Panneerselvam C. Agedependent upregulation of p53 and cytochrome c release and susceptibility to apoptosis in skeletal muscle fiber of aged rats: Role of carnitine and lipoic acid. Free Radic Biol Med 2007; 43 (12): 1656-69.
    • (2007) Free Radic Biol Med , vol.43 , Issue.12 , pp. 1656-1669
    • Tamilselvan, J.1    Jayaraman, G.2    Sivarajan, K.3    Panneerselvam, C.4
  • 18
    • 63149106832 scopus 로고    scopus 로고
    • Differential cell death regulation between adult-unloaded and aged rat soleus muscle
    • Ogata T, Machida S, Oishi Y, Higuchi M, Muraoka I. Differential cell death regulation between adult-unloaded and aged rat soleus muscle. Mech Ageing Dev 2009; 130 (5): 328-36.
    • (2009) Mech Ageing Dev , vol.130 , Issue.5 , pp. 328-336
    • Ogata, T.1    Machida, S.2    Oishi, Y.3    Higuchi, M.4    Muraoka, I.5
  • 19
    • 60549115947 scopus 로고    scopus 로고
    • Changes in IL-15 expression and death-receptor apoptotic signaling in rat gastrocnemius muscle with aging and life-long calorie restriction
    • Marzetti E, Carter CS, Wohlgemuth SE, Lees HA, Giovannini S, Anderson B, Quinn LS, Leeuwenburgh C. Changes in IL-15 expression and death-receptor apoptotic signaling in rat gastrocnemius muscle with aging and life-long calorie restriction. Mech Ageing Dev 2009; 130 (4): 272-80.
    • (2009) Mech Ageing Dev , vol.130 , Issue.4 , pp. 272-280
    • Marzetti, E.1    Carter, C.S.2    Wohlgemuth, S.E.3    Lees, H.A.4    Giovannini, S.5    Anderson, B.6    Quinn, L.S.7    Leeuwenburgh, C.8
  • 20
    • 0032997908 scopus 로고    scopus 로고
    • Estrogen modulates neuronal Bcl-xL expression and betaamyloid-induced apoptosis: Relevance to Alzheimer's disease
    • Pike CJ. Estrogen modulates neuronal Bcl-xL expression and betaamyloid-induced apoptosis: relevance to Alzheimer's disease. J Neurochem 1999; 72 (4): 1552-63.
    • (1999) J Neurochem , vol.72 , Issue.4 , pp. 1552-1563
    • Pike, C.J.1
  • 21
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson MP. Apoptosis in neurodegenerative disorders. Nat Rev Mol Cell Biol 2000; 1 (2): 120-9.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , Issue.2 , pp. 120-129
    • Mattson, M.P.1
  • 22
    • 0032526374 scopus 로고    scopus 로고
    • Apoptosis: Basic mechanisms and implications for cardiovascular disease
    • Haunstetter A, Izumo S. Apoptosis: basic mechanisms and implications for cardiovascular disease. Circ Res 1998; 82 (11): 1111-29.
    • (1998) Circ Res , vol.82 , Issue.11 , pp. 1111-1129
    • Haunstetter, A.1    Izumo, S.2
  • 23
    • 0032489850 scopus 로고    scopus 로고
    • Cooperative interactions between RB and p53 regulate cell proliferation, cell senescence, and apoptosis in human vascular smooth muscle cells from atherosclerotic plaques
    • Bennett MR, Macdonald K, Chan SW, Boyle JJ, Weissberg PL. Cooperative interactions between RB and p53 regulate cell proliferation, cell senescence, and apoptosis in human vascular smooth muscle cells from atherosclerotic plaques. Circ Res 1998; 82 (6): 704-12.
    • (1998) Circ Res , vol.82 , Issue.6 , pp. 704-712
    • Bennett, M.R.1    Macdonald, K.2    Chan, S.W.3    Boyle, J.J.4    Weissberg, P.L.5
  • 24
    • 0037203345 scopus 로고    scopus 로고
    • Lipoapoptosis: Its mechanism and its diseases
    • Unger RH, Orci L. Lipoapoptosis: its mechanism and its diseases. Biochim Biophys Acta 2002; 1585 (2-3): 202-12.
    • (2002) Biochim Biophys Acta , vol.1585 , Issue.2-3 , pp. 202-212
    • Unger, R.H.1    Orci, L.2
  • 25
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: Activation, specificity, and regulation
    • Pop C, Salvesen GS. Human caspases: activation, specificity, and regulation. J Biol Chem 2009; 284 (33): 21777-81.
    • (2009) J Biol Chem , vol.284 , Issue.33 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 26
    • 0347601880 scopus 로고    scopus 로고
    • A decade of caspases
    • Degterev A, Boyce M, Yuan J. A decade of caspases. Oncogene 2003; 22 (53): 8543-67.
    • (2003) Oncogene , vol.22 , Issue.53 , pp. 8543-8567
    • Degterev, A.1    Boyce, M.2    Yuan, J.3
  • 27
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk JE, Green DR. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol 2008; 18 (4): 157-64.
    • (2008) Trends Cell Biol , vol.18 , Issue.4 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 28
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91 (4): 479-89.
    • (1997) Cell , vol.91 , Issue.4 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6
  • 30
    • 0036544535 scopus 로고    scopus 로고
    • The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3-and caspase 9-interacting sites
    • Silke J, Hawkins CJ, Ekert PG, Chew J, Day CL, Pakusch M, et al. The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3-and caspase 9-interacting sites. J Cell Biol 2002; 157 (1): 115-24.
    • (2002) J Cell Biol , vol.157 , Issue.1 , pp. 115-124
    • Silke, J.1    Hawkins, C.J.2    Ekert, P.G.3    Chew, J.4    Day, C.L.5    Pakusch, M.6
  • 31
    • 0037427441 scopus 로고    scopus 로고
    • Mammalian mitochondrial IAP binding proteins
    • Vaux DL, Silke J. Mammalian mitochondrial IAP binding proteins. Biochem Biophys Res Commun 2003; 304 (3): 499-504.
    • (2003) Biochem Biophys Res Commun , vol.304 , Issue.3 , pp. 499-504
    • Vaux, D.L.1    Silke, J.2
  • 32
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y, Imai Y, Nakayama H, Takahashi K, Takio K, Takahashi R. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol Cell 2001; 8 (3): 613-21.
    • (2001) Mol Cell , vol.8 , Issue.3 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 33
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosisinducing factor
    • Susin SA, Lorenzo HK, Zamzami N, Marzo I, Snow BE, Brothers GM, et al. Molecular characterization of mitochondrial apoptosisinducing factor. Nature 1999; 397 (6718): 441-6.
    • (1999) Nature , vol.397 , Issue.6718 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3    Marzo, I.4    Snow, B.E.5    Brothers, G.M.6
  • 34
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li LY, Luo X, Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 2001; 412 (6842): 95-9.
    • (2001) Nature , vol.412 , Issue.6842 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 36
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • Baud V, Karin M. Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol 2001; 11 (9): 372-7.
    • (2001) Trends Cell Biol , vol.11 , Issue.9 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 37
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003; 114 (2): 181-90.
    • (2003) Cell , vol.114 , Issue.2 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 38
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the Light: The Growing Complexity of p53
    • Vousden KH, Prives C. Blinded by the Light: The Growing Complexity of p53. Cell 2009; 137 (3): 413-31.
    • (2009) Cell , vol.137 , Issue.3 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 39
    • 0034735904 scopus 로고    scopus 로고
    • MDM2-dependent ubiquitination of nuclear and cytoplasmic P53
    • Yu ZK, Geyer RK, Maki CG. MDM2-dependent ubiquitination of nuclear and cytoplasmic P53. Oncogene 2000; 19 (51): 5892-7.
    • (2000) Oncogene , vol.19 , Issue.51 , pp. 5892-5897
    • Yu, Z.K.1    Geyer, R.K.2    Maki, C.G.3
  • 40
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth J, Dobbelstein M, Freedman DA, Shenk T, Levine AJ. Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J 1998; 17 (2): 554-64.
    • (1998) EMBO J , vol.17 , Issue.2 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 41
    • 0028952841 scopus 로고
    • Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms
    • Jeffrey PD, Gorina S, Pavletich NP. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science 1995; 267 (5203): 1498-502.
    • (1995) Science , vol.267 , Issue.5203 , pp. 1498-1502
    • Jeffrey, P.D.1    Gorina, S.2    Pavletich, N.P.3
  • 42
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks CL, Gu W. Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr Opin Cell Biol 2003; 15 (2): 164-71.
    • (2003) Curr Opin Cell Biol , vol.15 , Issue.2 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 43
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives C, Hall PA. The p53 pathway. J Pathol 1999; 187 (1): 112-26.
    • (1999) J Pathol , vol.187 , Issue.1 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 44
    • 1542353401 scopus 로고    scopus 로고
    • Control of apoptosis by p53
    • Fridman JS, Lowe SW. Control of apoptosis by p53. Oncogene 2003; 22 (56): 9030-40.
    • (2003) Oncogene , vol.22 , Issue.56 , pp. 9030-9040
    • Fridman, J.S.1    Lowe, S.W.2
  • 45
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • Vogelstein B, Lane D, Levine AJ. Surfing the p53 network. Nature 2000; 408 (6810): 307-10.
    • (2000) Nature , vol.408 , Issue.6810 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.J.3
  • 46
    • 67349086630 scopus 로고    scopus 로고
    • The mitochondrial p53 pathway
    • Vaseva AV, Moll UM. The mitochondrial p53 pathway. Biochim Biophys Acta 2009; 1787 (5): 414-20.
    • (2009) Biochim Biophys Acta , vol.1787 , Issue.5 , pp. 414-420
    • Vaseva, A.V.1    Moll, U.M.2
  • 48
    • 0035884191 scopus 로고    scopus 로고
    • APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis
    • Robles AI, Bemmels NA, Foraker AB, Harris CC. APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis. Cancer Res 2001; 61 (18): 6660-4.
    • (2001) Cancer Res , vol.61 , Issue.18 , pp. 6660-6664
    • Robles, A.I.1    Bemmels, N.A.2    Foraker, A.B.3    Harris, C.C.4
  • 50
    • 33646807491 scopus 로고    scopus 로고
    • Transcriptional regulation by p53: One protein, many possibilities
    • Laptenko O, Prives C. Transcriptional regulation by p53: one protein, many possibilities. Cell Death Differ 2006; 13 (6): 951-61.
    • (2006) Cell Death Differ , vol.13 , Issue.6 , pp. 951-961
    • Laptenko, O.1    Prives, C.2
  • 51
    • 27544486327 scopus 로고    scopus 로고
    • Transcriptionindependent pro-apoptotic functions of p53
    • Moll UM, Wolff S, Speidel D, Deppert W. Transcriptionindependent pro-apoptotic functions of p53. Curr Opin Cell Biol 2005; 17 (6): 631-6.
    • (2005) Curr Opin Cell Biol , vol.17 , Issue.6 , pp. 631-636
    • Moll, U.M.1    Wolff, S.2    Speidel, D.3    Deppert, W.4
  • 52
    • 65949083750 scopus 로고    scopus 로고
    • Cytoplasmic functions of the tumour suppressor p53
    • Green DR, Kroemer G. Cytoplasmic functions of the tumour suppressor p53. Nature 2009; 458 (7242): 1127-30.
    • (2009) Nature , vol.458 , Issue.7242 , pp. 1127-1130
    • Green, D.R.1    Kroemer, G.2
  • 53
    • 68849093989 scopus 로고    scopus 로고
    • Tumour suppression by p53: The importance of apoptosis and cellular senescence
    • Zuckerman V, Wolyniec K, Sionov RV, Haupt S, Haupt Y. Tumour suppression by p53: the importance of apoptosis and cellular senescence. J Pathol 2009; 219 (1): 3-15.
    • (2009) J Pathol , vol.219 , Issue.1 , pp. 3-15
    • Zuckerman, V.1    Wolyniec, K.2    Sionov, R.V.3    Haupt, S.4    Haupt, Y.5
  • 54
    • 72549085096 scopus 로고    scopus 로고
    • Transcription-independent p53 apoptosis: An alternative route to death
    • Speidel D. Transcription-independent p53 apoptosis: an alternative route to death. Trends Cell Biol 2010; 20 (1): 14-24.
    • (2010) Trends Cell Biol , vol.20 , Issue.1 , pp. 14-24
    • Speidel, D.1
  • 55
    • 0842278331 scopus 로고    scopus 로고
    • Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis
    • Chipuk JE, Kuwana T, Bouchier-Hayes L, Droin NM, Newmeyer DD, Schuler M, et al. Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 2004; 303 (5660): 1010-4.
    • (2004) Science , vol.303 , Issue.5660 , pp. 1010-1014
    • Chipuk, J.E.1    Kuwana, T.2    Bouchier-Hayes, L.3    Droin, N.M.4    Newmeyer, D.D.5    Schuler, M.6
  • 56
    • 33845193134 scopus 로고    scopus 로고
    • The Bad guy cooperates with good cop p53: Bad is transcriptionally up-regulated by p53 and forms a Bad/p53 complex at the mitochondria to induce apoptosis
    • Jiang P, Du W, Heese K, Wu M. The Bad guy cooperates with good cop p53: Bad is transcriptionally up-regulated by p53 and forms a Bad/p53 complex at the mitochondria to induce apoptosis. Mol Cell Biol 2006; 26 (23): 9071-82.
    • (2006) Mol Cell Biol , vol.26 , Issue.23 , pp. 9071-9082
    • Jiang, P.1    Du, W.2    Heese, K.3    Wu, M.4
  • 57
    • 24644436766 scopus 로고    scopus 로고
    • PUMA couples the nuclear and cytoplasmic proapoptotic function of p53
    • Chipuk JE, Bouchier-Hayes L, Kuwana T, Newmeyer DD, Green DR. PUMA couples the nuclear and cytoplasmic proapoptotic function of p53. Science 2005; 309 (5741): 1732-5.
    • (2005) Science , vol.309 , Issue.5741 , pp. 1732-1735
    • Chipuk, J.E.1    Bouchier-Hayes, L.2    Kuwana, T.3    Newmeyer, D.D.4    Green, D.R.5
  • 58
    • 36849074245 scopus 로고    scopus 로고
    • Hepatic IGFBP1 is a prosurvival factor that binds to BAK, protects the liver from apoptosis, and antagonizes the proapoptotic actions of p53 at mitochondria
    • Leu JI, George DL. Hepatic IGFBP1 is a prosurvival factor that binds to BAK, protects the liver from apoptosis, and antagonizes the proapoptotic actions of p53 at mitochondria. Genes Dev 2007; 21 (23): 3095-109.
    • (2007) Genes Dev , vol.21 , Issue.23 , pp. 3095-3109
    • Leu, J.I.1    George, D.L.2
  • 59
    • 33847276654 scopus 로고    scopus 로고
    • Monoubiquitylation promotes mitochondrial p53 translocation
    • Marchenko ND, Wolff S, Erster S, Becker K, Moll UM. Monoubiquitylation promotes mitochondrial p53 translocation. EMBO J 2007; 26 (4): 923-34.
    • (2007) EMBO J , vol.26 , Issue.4 , pp. 923-934
    • Marchenko, N.D.1    Wolff, S.2    Erster, S.3    Becker, K.4    Moll, U.M.5
  • 60
    • 66249089036 scopus 로고    scopus 로고
    • Role of p53 in mitochondrial biogenesis and apoptosis in skeletal muscle
    • Saleem A, Adhihetty PJ, Hood DA. Role of p53 in mitochondrial biogenesis and apoptosis in skeletal muscle. Physiol Genomics 2009; 37 (1): 58-66.
    • (2009) Physiol Genomics , vol.37 , Issue.1 , pp. 58-66
    • Saleem, A.1    Adhihetty, P.J.2    Hood, D.A.3
  • 61
    • 70349655709 scopus 로고    scopus 로고
    • p53 improves aerobic exercise capacity and augments skeletal muscle mitochondrial DNA content
    • Park JY, Wang PY, Matsumoto T, Sung HJ, Ma W, Choi JW, et al. p53 improves aerobic exercise capacity and augments skeletal muscle mitochondrial DNA content. Circ Res 2009; 105 (7): 705-12.
    • (2009) Circ Res , vol.105 , Issue.7 , pp. 705-712
    • Park, J.Y.1    Wang, P.Y.2    Matsumoto, T.3    Sung, H.J.4    Ma, W.5    Choi, J.W.6
  • 62
    • 25644432770 scopus 로고    scopus 로고
    • Contributions of the ubiquitin-proteasome pathway and apoptosis to human skeletal muscle wasting with age
    • Whitman SA, Wacker MJ, Richmond SR, Godard MP. Contributions of the ubiquitin-proteasome pathway and apoptosis to human skeletal muscle wasting with age. Pflugers Arch 2005; 450 (6): 437-46.
    • (2005) Pflugers Arch , vol.450 , Issue.6 , pp. 437-446
    • Whitman, S.A.1    Wacker, M.J.2    Richmond, S.R.3    Godard, M.P.4
  • 63
    • 46649114727 scopus 로고    scopus 로고
    • Age-related activation of mitochondrial caspaseindependent apoptotic signaling in rat gastrocnemius muscle
    • Marzetti E, Wohlgemuth SE, Lees HA, Chung HY, Giovannini S, Leeuwenburgh C. Age-related activation of mitochondrial caspaseindependent apoptotic signaling in rat gastrocnemius muscle. Mech Ageing Dev 2008; 129 (9): 542-9.
    • (2008) Mech Ageing Dev , vol.129 , Issue.9 , pp. 542-549
    • Marzetti, E.1    Wohlgemuth, S.E.2    Lees, H.A.3    Chung, H.Y.4    Giovannini, S.5    Leeuwenburgh, C.6
  • 64
    • 0036088709 scopus 로고    scopus 로고
    • Potential role for Id myogenic repressors in apoptosis and attenuation of hypertrophy in muscles of aged rats
    • Alway SE, Degens H, Krishnamurthy G, Smith CA. Potential role for Id myogenic repressors in apoptosis and attenuation of hypertrophy in muscles of aged rats. Am J Physiol Cell Physiol 2002; 283 (1): C66-76.
    • (2002) Am J Physiol Cell Physiol , vol.283 , Issue.1
    • Alway, S.E.1    Degens, H.2    Krishnamurthy, G.3    Smith, C.A.4
  • 65
    • 73949099327 scopus 로고    scopus 로고
    • Increased muscle PGC-1alpha expression protects from sarcopenia and metabolic disease during aging
    • Wenz T, Rossi SG, Rotundo RL, Spiegelman BM, Moraes CT. Increased muscle PGC-1alpha expression protects from sarcopenia and metabolic disease during aging. Proc Natl Acad Sci USA 2009; 106 (48): 20405-10.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.48 , pp. 20405-20410
    • Wenz, T.1    Rossi, S.G.2    Rotundo, R.L.3    Spiegelman, B.M.4    Moraes, C.T.5
  • 66
    • 27944475065 scopus 로고    scopus 로고
    • Muscle-specific loss of apoptosis-inducing factor leads to mitochondrial dysfunction, skeletal muscle atrophy, and dilated cardiomyopathy
    • Joza N, Oudit GY, Brown D, Benit P, Kassiri Z, Vahsen N, et al. Muscle-specific loss of apoptosis-inducing factor leads to mitochondrial dysfunction, skeletal muscle atrophy, and dilated cardiomyopathy. Mol Cell Biol 2005; 25 (23): 10261-72.
    • (2005) Mol Cell Biol , vol.25 , Issue.23 , pp. 10261-10272
    • Joza, N.1    Oudit, G.Y.2    Brown, D.3    Benit, P.4    Kassiri, Z.5    Vahsen, N.6
  • 70
    • 0033696398 scopus 로고    scopus 로고
    • NF-kappaB mediates the protein loss induced by TNF-alpha in differentiated skeletal muscle myotubes
    • Li YP, Reid MB. NF-kappaB mediates the protein loss induced by TNF-alpha in differentiated skeletal muscle myotubes. Am J Physiol Regul Integr Comp Physiol 2000; 279 (4): R1165-70.
    • (2000) Am J Physiol Regul Integr Comp Physiol , vol.279 , Issue.4
    • Li, Y.P.1    Reid, M.B.2
  • 71
    • 1642580487 scopus 로고    scopus 로고
    • Multifaceted roles of TNFalpha in myoblast destruction: A multitude of signal transduction pathways
    • Stewart CE, Newcomb PV, Holly JM. Multifaceted roles of TNFalpha in myoblast destruction: a multitude of signal transduction pathways. J Cell Physiol 2004; 198 (2): 237-47.
    • (2004) J Cell Physiol , vol.198 , Issue.2 , pp. 237-247
    • Stewart, C.E.1    Newcomb, P.V.2    Holly, J.M.3
  • 72
    • 0032534588 scopus 로고    scopus 로고
    • TRAF2 expression in differentiated muscle
    • MacLachlan TK, Giordano A. TRAF2 expression in differentiated muscle. J Cell Biochem 1998; 71 (4): 461-6.
    • (1998) J Cell Biochem , vol.71 , Issue.4 , pp. 461-466
    • MacLachlan, T.K.1    Giordano, A.2
  • 73
    • 0024547167 scopus 로고
    • Infusion of tumor necrosis factor/cachectin promotes muscle catabolism in the rat. A synergistic effect with interleukin 1
    • Flores EA, Bistrian BR, Pomposelli JJ, Dinarello CA, Blackburn GL, Istfan NW. Infusion of tumor necrosis factor/cachectin promotes muscle catabolism in the rat. A synergistic effect with interleukin 1. J Clin Invest 1989; 83 (5): 1614-22.
    • (1989) J Clin Invest , vol.83 , Issue.5 , pp. 1614-1622
    • Flores, E.A.1    Bistrian, B.R.2    Pomposelli, J.J.3    Dinarello, C.A.4    Blackburn, G.L.5    Istfan, N.W.6
  • 74
    • 0026085487 scopus 로고
    • Body composition and metabolic rate in rat during a continuous infusion of cachectin
    • Hoshino E, Pichard C, Greenwood CE, Kuo GC, Cameron RG, Kurian R, et al. Body composition and metabolic rate in rat during a continuous infusion of cachectin. Am J Physiol 1991; 260 (1 Pt 1): E27-36.
    • (1991) Am J Physiol , vol.260 , Issue.1 PART 1
    • Hoshino, E.1    Pichard, C.2    Greenwood, C.E.3    Kuo, G.C.4    Cameron, R.G.5    Kurian, R.6
  • 75
    • 0031771539 scopus 로고    scopus 로고
    • Changes in body composition and dietary intake induced by tumor necrosis factor alpha and corticosterone--individually and in combination
    • Raina N, Jeejeebhoy KN. Changes in body composition and dietary intake induced by tumor necrosis factor alpha and corticosterone--individually and in combination. Am J Clin Nutr 1998; 68 (6): 1284-90.
    • (1998) Am J Clin Nutr , vol.68 , Issue.6 , pp. 1284-1290
    • Raina, N.1    Jeejeebhoy, K.N.2
  • 77
    • 0031802331 scopus 로고    scopus 로고
    • Skeletal muscle myocytes undergo protein loss and reactive oxygenmediated NF-kappaB activation in response to tumor necrosis factor alpha
    • Li YP, Schwartz RJ, Waddell ID, Holloway BR, Reid MB. Skeletal muscle myocytes undergo protein loss and reactive oxygenmediated NF-kappaB activation in response to tumor necrosis factor alpha. FASEB J 1998; 12 (10): 871-80.
    • (1998) FASEB J , vol.12 , Issue.10 , pp. 871-880
    • Li, Y.P.1    Schwartz, R.J.2    Waddell, I.D.3    Holloway, B.R.4    Reid, M.B.5
  • 78
    • 2942662046 scopus 로고    scopus 로고
    • NF-kappaB activation and iNOS upregulation in skeletal muscle of patients with COPD and low body weight
    • Agusti A, Morla M, Sauleda J, Saus C, Busquets X. NF-kappaB activation and iNOS upregulation in skeletal muscle of patients with COPD and low body weight. Thorax 2004; 59 (6): 483-7.
    • (2004) Thorax , vol.59 , Issue.6 , pp. 483-487
    • Agusti, A.1    Morla, M.2    Sauleda, J.3    Saus, C.4    Busquets, X.5
  • 79
    • 0037854031 scopus 로고    scopus 로고
    • Nitric oxide and its role in apoptosis
    • Brune B, von Knethen A, Sandau KB. Nitric oxide and its role in apoptosis. Eur J Pharmacol 1998; 351 (3): 261-72.
    • (1998) Eur J Pharmacol , vol.351 , Issue.3 , pp. 261-272
    • Brune, B.1    von Knethen, A.2    Sandau, K.B.3
  • 80
    • 0034693038 scopus 로고    scopus 로고
    • Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite
    • Reiter CD, Teng RJ, Beckman JS. Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite. J Biol Chem 2000; 275 (42): 32460-6.
    • (2000) J Biol Chem , vol.275 , Issue.42 , pp. 32460-32466
    • Reiter, C.D.1    Teng, R.J.2    Beckman, J.S.3
  • 81
    • 0036236271 scopus 로고    scopus 로고
    • Aging and the role of reactive nitrogen species
    • Drew B, Leeuwenburgh C. Aging and the role of reactive nitrogen species. Ann N Y Acad Sci 2002; 959: 66-81.
    • (2002) Ann N Y Acad Sci , vol.959 , pp. 66-81
    • Drew, B.1    Leeuwenburgh, C.2
  • 82
    • 0031035583 scopus 로고    scopus 로고
    • Reactive nitrogen intermediates promote low density lipoprotein oxidation in human atherosclerotic intima
    • Leeuwenburgh C, Hardy MM, Hazen SL, Wagner P, Oh-ishi S, Steinbrecher UP, et al. Reactive nitrogen intermediates promote low density lipoprotein oxidation in human atherosclerotic intima. J Biol Chem 1997; 272 (3): 1433-6.
    • (1997) J Biol Chem , vol.272 , Issue.3 , pp. 1433-1436
    • Leeuwenburgh, C.1    Hardy, M.M.2    Hazen, S.L.3    Wagner, P.4    Oh-ishi, S.5    Steinbrecher, U.P.6
  • 83
    • 14644400387 scopus 로고    scopus 로고
    • TNFalpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle
    • Li YP, Chen Y, John J, Moylan J, Jin B, Mann DL, et al. TNFalpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J 2005; 19 (3): 362-70.
    • (2005) FASEB J , vol.19 , Issue.3 , pp. 362-370
    • Li, Y.P.1    Chen, Y.2    John, J.3    Moylan, J.4    Jin, B.5    Mann, D.L.6
  • 85
    • 33645831979 scopus 로고    scopus 로고
    • Hindlimb unloading increases muscle content of cytosolic but not nuclear Id2 and p53 proteins in young adult and aged rats
    • Siu PM, Pistilli EE, Murlasits Z, Alway SE. Hindlimb unloading increases muscle content of cytosolic but not nuclear Id2 and p53 proteins in young adult and aged rats. J Appl Physiol 2006; 100 (3): 907-16.
    • (2006) J Appl Physiol , vol.100 , Issue.3 , pp. 907-916
    • Siu, P.M.1    Pistilli, E.E.2    Murlasits, Z.3    Alway, S.E.4
  • 86
    • 17644417848 scopus 로고    scopus 로고
    • Id2 and p53 participate in apoptosis during unloading-induced muscle atrophy
    • Siu PM, Alway SE. Id2 and p53 participate in apoptosis during unloading-induced muscle atrophy. Am J Physiol Cell Physiol 2005; 288 (5): C1058-73.
    • (2005) Am J Physiol Cell Physiol , vol.288 , Issue.5
    • Siu, P.M.1    Alway, S.E.2
  • 87
    • 29644437922 scopus 로고    scopus 로고
    • Age-related alterations in expression of apoptosis regulatory proteins and heat shock proteins in rat skeletal muscle
    • Chung L, Ng YC. Age-related alterations in expression of apoptosis regulatory proteins and heat shock proteins in rat skeletal muscle. Biochim Biophys Acta 2006; 1762 (1): 103-9.
    • (2006) Biochim Biophys Acta , vol.1762 , Issue.1 , pp. 103-109
    • Chung, L.1    Ng, Y.C.2
  • 89
    • 41149139501 scopus 로고    scopus 로고
    • Nuclear apoptosis contributes to sarcopenia
    • Alway SE, Siu PM. Nuclear apoptosis contributes to sarcopenia. Exerc Sport Sci Rev 2008; 36 (2): 51-7.
    • (2008) Exerc Sport Sci Rev , vol.36 , Issue.2 , pp. 51-57
    • Alway, S.E.1    Siu, P.M.2
  • 90
    • 0036788751 scopus 로고    scopus 로고
    • Apoptosis and muscle fibre loss in neuromuscular disorders
    • Tews DS. Apoptosis and muscle fibre loss in neuromuscular disorders. Neuromuscul Disord 2002; 12 (7-8): 613-22.
    • (2002) Neuromuscul Disord , vol.12 , Issue.7-8 , pp. 613-622
    • Tews, D.S.1
  • 92
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • Du J, Wang X, Miereles C, Bailey JL, Debigare R, Zheng B, et al. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 2004; 113 (1): 115-23.
    • (2004) J Clin Invest , vol.113 , Issue.1 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6


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