메뉴 건너뛰기




Volumn 9, Issue 4, 2006, Pages 395-402

Insights into muscle atrophy and recovery pathway based on genetic models

Author keywords

Expression analysis; Muscle atrophy; Recovery pathways; Reductive remodeling pathways

Indexed keywords

AMINO ACID; ANABOLIC AGENT; BOWMAN BIRK INHIBITOR; CLENBUTEROL; CREATINE; ICOSAPENTAENOIC ACID; MESSENGER RNA; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY MYO 029; MUSCLE PROTEIN; TESTOSTERONE; UNCLASSIFIED DRUG;

EID: 33746209093     PISSN: 13631950     EISSN: 15353885     Source Type: Journal    
DOI: 10.1097/01.mco.0000232899.51544.69     Document Type: Review
Times cited : (9)

References (44)
  • 1
    • 0035745756 scopus 로고    scopus 로고
    • Functional and structural adaptations of skeletal muscle to microgravity
    • Fitts RH, Riley DR, Widrick JJ. Functional and structural adaptations of skeletal muscle to microgravity. J Exp Biol 2001; 204:3201-3208.
    • (2001) J Exp Biol , vol.204 , pp. 3201-3208
    • Fitts, R.H.1    Riley, D.R.2    Widrick, J.J.3
  • 2
    • 21044434210 scopus 로고    scopus 로고
    • Transcriptional reprogramming during reloading of atrophied rat soleus muscle
    • Fluck M, Schmutz S, Wittwer M, et al. Transcriptional reprogramming during reloading of atrophied rat soleus muscle. Am J Physiol Regul lntegr Comp Physiol 2005; 289:R4-R14. Begins to identify the sequence of steps in the remodeling process.
    • (2005) Am J Physiol Regul Lntegr Comp Physiol , vol.289
    • Fluck, M.1    Schmutz, S.2    Wittwer, M.3
  • 3
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • Sandri M, Sandri C, Gilbert A, et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 2004; 117:399-412.
    • (2004) Cell , vol.117 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3
  • 4
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • Stitt TN, Drujan D, Clarke BA, et al. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell 2004; 14:395-403.
    • (2004) Mol Cell , vol.14 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3
  • 5
    • 11144237310 scopus 로고    scopus 로고
    • Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
    • U S A
    • Kedar V, McDonough H, Arya R, et al. Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc Natl Acad Sci U S A 2004; 101:18135-18140.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 18135-18140
    • Kedar, V.1    McDonough, H.2    Arya, R.3
  • 6
    • 12244291970 scopus 로고    scopus 로고
    • Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein
    • Pizon V, Iakovenko A, van der Ven PFM, et al. Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein. J Cell Sci 2002; 115:4469-4482.
    • (2002) J Cell Sci , vol.115 , pp. 4469-4482
    • Pizon, V.1    Iakovenko, A.2    Van Der Ven, P.F.M.3
  • 7
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S, Xiang F, Yakovenko A, et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 2005; 308:1599-1603. A truly elegant and comprehensive study. Describes the steps between muscle tension and protein turnover and how they relate to a human myopathy.
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3
  • 8
    • 27644471080 scopus 로고    scopus 로고
    • Dystrophin glycoprotein complex dysfunction: A regulatory link between muscular dystrophy and cancer cachexia
    • Acharyya S, Butchbach MER, Sahenk Z, et al. Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell 2005; 8:421-432.
    • (2005) Cancer Cell , vol.8 , pp. 421-432
    • Acharyya, S.1    Butchbach, M.E.R.2    Sahenk, Z.3
  • 9
    • 0034095499 scopus 로고    scopus 로고
    • Effects of oral creatine supplementation on muscular strength and body composition
    • Becque MD, Lochmann JD, Melrose DR. Effects of oral creatine supplementation on muscular strength and body composition. Med Sci Sports Exerc 2000; 32:654-658.
    • (2000) Med Sci Sports Exerc , vol.32 , pp. 654-658
    • Becque, M.D.1    Lochmann, J.D.2    Melrose, D.R.3
  • 10
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase: Fuel gauge of the mammalian cell?
    • Hardie DG, Carling D. The AMP-activated protein kinase: fuel gauge of the mammalian cell? Eur J Biochem 1997; 246:259-273.
    • (1997) Eur J Biochem , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 11
    • 28044451289 scopus 로고    scopus 로고
    • Insulin-independent pathways mediating glucose uptake in hindlimb-suspended skeletal muscle
    • Hilder TL, Baer LA, Fuller PM, et al. Insulin-independent pathways mediating glucose uptake in hindlimb-suspended skeletal muscle. J Appl Physiol 2005; 99:2181-2188.
    • (2005) J Appl Physiol , vol.99 , pp. 2181-2188
    • Hilder, T.L.1    Baer, L.A.2    Fuller, P.M.3
  • 12
    • 0037143449 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis
    • Horman S, Browne GJ, Krause U, et al. Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis. Curr Biol 2002; 12:1419-1423.
    • (2002) Curr Biol , vol.12 , pp. 1419-1423
    • Horman, S.1    Browne, G.J.2    Krause, U.3
  • 13
    • 0015381181 scopus 로고
    • Creatine and the control of myosin synthesis in differentiating skeletal muscle
    • U S A
    • Ingwall JS, Morales MF, Stockdale FE. Creatine and the control of myosin synthesis in differentiating skeletal muscle. Proc Natl Acad Sci U S A 1972; 69:2250-2253.
    • (1972) Proc Natl Acad Sci , vol.69 , pp. 2250-2253
    • Ingwall, J.S.1    Morales, M.F.2    Stockdale, F.E.3
  • 14
    • 0347285363 scopus 로고    scopus 로고
    • Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
    • Lecker SH, Jagoe RT, Gilbert A, et al. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J 2004; 18:39-51.
    • (2004) FASEB J , vol.18 , pp. 39-51
    • Lecker, S.H.1    Jagoe, R.T.2    Gilbert, A.3
  • 15
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine SC, Latres E, Baumhueter S, et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 2001; 294:1704-1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3
  • 16
    • 0033060435 scopus 로고    scopus 로고
    • Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting
    • Mitch WE, Bailey JL, Wang X, et al. Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting. Am J Physiol Cell Physiol 1999; 276:C1132-C1138.
    • (1999) Am J Physiol Cell Physiol , vol.276
    • Mitch, W.E.1    Bailey, J.L.2    Wang, X.3
  • 17
    • 0033883216 scopus 로고    scopus 로고
    • Physiology of a microgravity environment invited review: Microgravity and skeletal muscle
    • Fitts RH, Riley DR, Widrick JJ. Physiology of a microgravity environment invited review: microgravity and skeletal muscle. J Appl Physiol 2000; 89:823-839.
    • (2000) J Appl Physiol , vol.89 , pp. 823-839
    • Fitts, R.H.1    Riley, D.R.2    Widrick, J.J.3
  • 18
    • 22144476546 scopus 로고    scopus 로고
    • Metabolic consequences of disuse atrophy
    • Stein TP, Wade CE. Metabolic consequences of disuse atrophy. J Nutr 2005; 135:1824-1830.
    • (2005) J Nutr , vol.135 , pp. 1824-1830
    • Stein, T.P.1    Wade, C.E.2
  • 19
    • 11144220520 scopus 로고    scopus 로고
    • Effect of hind limb muscle unloading on liver metabolism of rats
    • Stein TP, Schluter MD, Galante AT, et al. Effect of hind limb muscle unloading on liver metabolism of rats. J Nutr Biochem 2005; 16:9-16.
    • (2005) J Nutr Biochem , vol.16 , pp. 9-16
    • Stein, T.P.1    Schluter, M.D.2    Galante, A.T.3
  • 20
    • 0036342781 scopus 로고    scopus 로고
    • Energy metabolism pathways in rat muscle under conditions of simulated microgravity
    • Stein TP, Schluter MD, Galante AT, et al. Energy metabolism pathways in rat muscle under conditions of simulated microgravity. Nutr Biochem 2002; 13:471-478.
    • (2002) Nutr Biochem , vol.13 , pp. 471-478
    • Stein, T.P.1    Schluter, M.D.2    Galante, A.T.3
  • 21
    • 0041353459 scopus 로고    scopus 로고
    • Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle
    • Stevenson EJ, Giresi PG, Koncarevic A, et al. Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle. J Physiol 2003; 551:33-48.
    • (2003) J Physiol , vol.551 , pp. 33-48
    • Stevenson, E.J.1    Giresi, P.G.2    Koncarevic, A.3
  • 22
    • 33644943620 scopus 로고    scopus 로고
    • AMPK: A key sensor of fuel and energy status in skeletal muscle
    • Hardie DG, Sakamoto K. AMPK: a key sensor of fuel and energy status in skeletal muscle. Physiology 2006; 21:48-60. An excellent review of the role and importance of AMPK in regulating muscle energy metabolism and how it may relate to muscle work capacity.
    • (2006) Physiology , vol.21 , pp. 48-60
    • Hardie, D.G.1    Sakamoto, K.2
  • 23
    • 0032536774 scopus 로고    scopus 로고
    • Dual regulation of the AMP-activated protein kinase provides a novel mechanism for the control of creatine kinase in skeletal muscle
    • Ponticos M, Lu QL, Morgan JE, et al. Dual regulation of the AMP-activated protein kinase provides a novel mechanism for the control of creatine kinase in skeletal muscle. EMBO J 1998; 17:1688-1699.
    • (1998) EMBO J , vol.17 , pp. 1688-1699
    • Ponticos, M.1    Lu, Q.L.2    Morgan, J.E.3
  • 24
    • 0023193594 scopus 로고
    • Physiologic and biochemical effects of immobilization on muscle
    • Booth FW. Physiologic and biochemical effects of immobilization on muscle. Clin Orthop 1987; 219:15-20.
    • (1987) Clin Orthop , vol.219 , pp. 15-20
    • Booth, F.W.1
  • 25
    • 0035757520 scopus 로고    scopus 로고
    • Creatine supplementation: Exploring the role of the creatine kinase/phosphocreatine system in human muscle
    • Hespel P, Eijnde BO, Derave W, et al. Creatine supplementation: exploring the role of the creatine kinase/phosphocreatine system in human muscle. Can J Appl Physiol 2001; 26:S79-S102.
    • (2001) Can J Appl Physiol , vol.26
    • Hespel, P.1    Eijnde, B.O.2    Derave, W.3
  • 26
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • Bolster DR, Crozier SJ, Kimball SR, Jefferson LS. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J Biol Chem 2002; 277:23977-23980.
    • (2002) J Biol Chem , vol.277 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 27
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki K, Zhu T, Guan K-L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 2003; 115:577-590.
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.-L.3
  • 28
    • 1942469564 scopus 로고    scopus 로고
    • Thr2446 is a novel mammalian target of rapamycin (mTOR) phosphorylation site regulated by nutrient status
    • Cheng SWY, Fryer LGD, Carling D, Shepherd PR. Thr2446 is a novel mammalian target of rapamycin (mTOR) phosphorylation site regulated by nutrient status. J Biol Chem 2004; 279:15719-15722.
    • (2004) J Biol Chem , vol.279 , pp. 15719-15722
    • Cheng, S.W.Y.1    Fryer, L.G.D.2    Carling, D.3    Shepherd, P.R.4
  • 29
    • 21344434137 scopus 로고    scopus 로고
    • Impaired voluntary running capacity of creatine kinase-deficient mice
    • Lond
    • Momken I, Lechene P, Koulmann N, et al. Impaired voluntary running capacity of creatine kinase-deficient mice. J Physiol (Lond) 2005; 565:951-964.
    • (2005) J Physiol , vol.565 , pp. 951-964
    • Momken, I.1    Lechene, P.2    Koulmann, N.3
  • 30
    • 23244443606 scopus 로고    scopus 로고
    • A single session of resistance exercise enhances insulin sensitivity for at least 24 h in healthy men
    • Koopman R, Manders RJF, Zorenc AHG, et al. A single session of resistance exercise enhances insulin sensitivity for at least 24 h in healthy men. Eur J Appl Physiol 2005; 94:180-187. An attempt to address the question of how much and for how the benefits of exercise last.
    • (2005) Eur J Appl Physiol , vol.94 , pp. 180-187
    • Koopman, R.1    Manders, R.J.F.2    Zorenc, A.H.G.3
  • 31
    • 0035059633 scopus 로고    scopus 로고
    • Large energetic adaptations of elderly muscle to resistance and endurance training
    • Jubrias SA, Esselman PC, Price LB, et al. Large energetic adaptations of elderly muscle to resistance and endurance training. J Appl Physiol 2001; 90:1663-1670.
    • (2001) J Appl Physiol , vol.90 , pp. 1663-1670
    • Jubrias, S.A.1    Esselman, P.C.2    Price, L.B.3
  • 32
    • 24044552980 scopus 로고    scopus 로고
    • Sex-based differences in skeletal muscle function and morphology with short-term limb immobilization
    • Yasuda N, Glover EI, Phillips SM, et al. Sex-based differences in skeletal muscle function and morphology with short-term limb immobilization. J Appl Physiol 2005; 99:1085-1092. Despite similar relative changes in lean body mass and muscle cross-sectional area during limb immobilization, females experienced greater reductions in distinct indices of strength. These results suggest a possible intrinsic neuromuscular alteration in females with muscle atrophy. More information on gender differences is required as this is a major unresolved problem.
    • (2005) J Appl Physiol , vol.99 , pp. 1085-1092
    • Yasuda, N.1    Glover, E.I.2    Phillips, S.M.3
  • 33
    • 0038298438 scopus 로고    scopus 로고
    • Factors influencing creatine loading into human skeletal muscle
    • Snow RJ, Murphy RM. Factors influencing creatine loading into human skeletal muscle. Exerc Sport Sci Rev 2003; 31:154-158.
    • (2003) Exerc Sport Sci Rev , vol.31 , pp. 154-158
    • Snow, R.J.1    Murphy, R.M.2
  • 34
    • 0036142663 scopus 로고    scopus 로고
    • Oral creatine supplementation enhances upper extremity work capacity in persons with cervical-level spinal cord injury
    • Jacobs PL, Mahoney ET, Cohn KA, et al. Oral creatine supplementation enhances upper extremity work capacity in persons with cervical-level spinal cord injury. Arch Phys Med Rehabil 2002; 83:19-23.
    • (2002) Arch Phys Med Rehabil , vol.83 , pp. 19-23
    • Jacobs, P.L.1    Mahoney, E.T.2    Cohn, K.A.3
  • 35
    • 2442539403 scopus 로고    scopus 로고
    • Effect of creatine supplementation on skeletal muscle of mdx mice
    • Louis M, Raymackers JM, Debaix H, et al. Effect of creatine supplementation on skeletal muscle of mdx mice. Muscle Nerve 2004; 29:687-692.
    • (2004) Muscle Nerve , vol.29 , pp. 687-692
    • Louis, M.1    Raymackers, J.M.2    Debaix, H.3
  • 36
    • 2442697688 scopus 로고    scopus 로고
    • Creatine monohydrate enhances strength and body composition in Duchenne muscular dystrophy
    • Tarnopolsky MA, Mahoney DJ, Vajsar J, et al. Creatine monohydrate enhances strength and body composition in Duchenne muscular dystrophy. Neurology 2004; 62:1771-1777.
    • (2004) Neurology , vol.62 , pp. 1771-1777
    • Tarnopolsky, M.A.1    Mahoney, D.J.2    Vajsar, J.3
  • 37
    • 0032817798 scopus 로고    scopus 로고
    • Performance and muscle fiber adaptations to creatine supplementation and heavy resistance training
    • Volek JS, Duncan ND, Mazzettis SA, et al. Performance and muscle fiber adaptations to creatine supplementation and heavy resistance training. Med Sci Sports Exerc 1999; 31:1147-1156.
    • (1999) Med Sci Sports Exerc , vol.31 , pp. 1147-1156
    • Volek, J.S.1    Duncan, N.D.2    Mazzettis, S.A.3
  • 38
    • 10744224478 scopus 로고    scopus 로고
    • Effects of creatine supplementation and exercise training on fitness in men 55-75 yr old
    • Eijnde BO, Van Leemputte M, Goris M, et al. Effects of creatine supplementation and exercise training on fitness in men 55-75 yr old. J Appl Physiol 2003; 95:818-828.
    • (2003) J Appl Physiol , vol.95 , pp. 818-828
    • Eijnde, B.O.1    Van Leemputte, M.2    Goris, M.3
  • 39
    • 0142116163 scopus 로고    scopus 로고
    • No effect of creatine supplementation on human myofibrillar and sarcoplasmic protein synthesis after resistance exercise
    • Louis M, Poortmans JR, Francaux M, et al. No effect of creatine supplementation on human myofibrillar and sarcoplasmic protein synthesis after resistance exercise. Am J Physiol Endocrinol Metab 2003; 285:E1089-E1094.
    • (2003) Am J Physiol Endocrinol Metab , vol.285
    • Louis, M.1    Poortmans, J.R.2    Francaux, M.3
  • 40
    • 0034875340 scopus 로고    scopus 로고
    • Effects of acute creatine monohydrate supplementation on leucine kinetics and mixed-muscle protein synthesis
    • Parise G, Mihic S, MacLennan D, et al. Effects of acute creatine monohydrate supplementation on leucine kinetics and mixed-muscle protein synthesis. J Appl Physiol 2001; 91:1041-1047.
    • (2001) J Appl Physiol , vol.91 , pp. 1041-1047
    • Parise, G.1    Mihic, S.2    MacLennan, D.3
  • 41
    • 0034798465 scopus 로고    scopus 로고
    • Effects of oral creatine and resistance training on myosin heavy chain expression
    • Willoughby DS, Rosene J. Effects of oral creatine and resistance training on myosin heavy chain expression. Med Sci Sports Exerc 2001; 33:1674-1681.
    • (2001) Med Sci Sports Exerc , vol.33 , pp. 1674-1681
    • Willoughby, D.S.1    Rosene, J.2
  • 42
    • 27244446077 scopus 로고    scopus 로고
    • Lower serum albumin concentration and change in muscle mass: The Health, Aging and Body Composition Study
    • Visser M, Kritchevsky SB, Newman AB, et al. Lower serum albumin concentration and change in muscle mass: the Health, Aging and Body Composition Study. Am J Clin Nutr 2005; 82:531-537. Serum albumin levels are related to both nutritional status and skeletal muscle mass. An intriguing observation.
    • (2005) Am J Clin Nutr , vol.82 , pp. 531-537
    • Visser, M.1    Kritchevsky, S.B.2    Newman, A.B.3
  • 43
    • 27544510642 scopus 로고    scopus 로고
    • Attenuation of skeletal muscle atrophy via protease inhibition
    • Morris CA, Morris LD, Kennedy AR, Sweeney HL. Attenuation of skeletal muscle atrophy via protease inhibition. J Appl Physiol 2005; 99:1719-1727. This study shows the potential for a targeted biochemical intervention. Muscle atrophy induced with hindlimb unloading was significantly reduced in animals fed a soybean-derived protease inhibitor that is nontoxic and orally bioavailable.
    • (2005) J Appl Physiol , vol.99 , pp. 1719-1727
    • Morris, C.A.1    Morris, L.D.2    Kennedy, A.R.3    Sweeney, H.L.4
  • 44
    • 3843054746 scopus 로고    scopus 로고
    • Effect of eicosapentaenoic acid, protein and amino acids on protein synthesis and degradation in skeletal muscle of cachectic mice
    • Smith HJ, Greenberg NA, Tisdale MJ. Effect of eicosapentaenoic acid, protein and amino acids on protein synthesis and degradation in skeletal muscle of cachectic mice. Br J Cancer 2004; 91:408-412.
    • (2004) Br J Cancer , vol.91 , pp. 408-412
    • Smith, H.J.1    Greenberg, N.A.2    Tisdale, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.