Various Jobs of Proteolytic Enzymes in Skeletal Muscle during Unloading: Facts and Speculations

被引:34
作者
Kachaeva, E. V. [1 ]
Shenkman, B. S. [1 ]
机构
[1] RAS, SSC RF Inst Biomed Problems, Moscow 117901, Russia
来源
JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY | 2012年
关键词
RAT SOLEUS MUSCLE; RING FINGER PROTEINS; MYOSIN HEAVY-CHAIN; KAPPA-B PATHWAY; GROWTH-FACTOR; UBIQUITIN-PROTEASOME; GENE-EXPRESSION; DISUSE ATROPHY; SARCOPLASMIC-RETICULUM; CONTRACTILE PROPERTIES;
D O I
10.1155/2012/493618
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Skeletal muscles, namely, postural muscles, as soleus, suffer from atrophy under disuse. Muscle atrophy development caused by unloading differs from that induced by denervation or other stimuli. Disuse atrophy is supposed to be the result of shift of protein synthesis/proteolysis balance towards protein degradation increase. Maintaining of the balance involves many systems of synthesis and proteolysis, whose activation leads to muscle adaptation to disuse rather than muscle degeneration. Here, we review recent data on activity of signaling systems involved in muscle atrophy development under unloading and muscle adaptation to the lack of support.
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页数:15
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共 134 条
[1]   Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors [J].
Allen, David L. ;
Unterman, Terry G. .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2007, 292 (01) :C188-C199
[2]   Effects of spaceflight on murine skeletal muscle gene expression [J].
Allen, David L. ;
Bandstra, Eric R. ;
Harrison, Brooke C. ;
Thorng, Seiha ;
Stodieck, Louis S. ;
Kostenuik, Paul J. ;
Morony, Sean ;
Lacey, David L. ;
Hammond, Timothy G. ;
Leinwand, Leslie L. ;
Argraves, W. Scott ;
Bateman, Ted A. ;
Barth, Jeremy L. .
JOURNAL OF APPLIED PHYSIOLOGY, 2009, 106 (02) :582-595
[3]   LEUCINE ATTENUATES SKELETAL MUSCLE WASTING VIA INHIBITION OF UBIQUITIN LIGASES [J].
Baptista, Igor L. ;
Leal, Marcelo L. ;
Artioli, Guilherme G. ;
Aoki, Marcelo S. ;
Fiamoncini, Jarlei ;
Turri, Antonio O. ;
Curi, Rui ;
Miyabara, Elen H. ;
Moriscot, Anselmo S. .
MUSCLE & NERVE, 2010, 41 (06) :800-808
[4]   Regulation of ubiquitin-proteasome system, caspase enzyme activities, and extracellular proteinases in rat soleus muscle in response to unloading [J].
Berthon, P. ;
Duguez, S. ;
Favier, F. B. ;
Amirouche, A. ;
Feasson, L. ;
Vico, L. ;
Denis, C. ;
Freyssenet, D. .
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 2007, 454 (04) :625-633
[5]   Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo [J].
Bodine, SC ;
Stitt, TN ;
Gonzalez, M ;
Kline, WO ;
Stover, GL ;
Bauerlein, R ;
Zlotchenko, E ;
Scrimgeour, A ;
Lawrence, JC ;
Glass, DJ ;
Yancopoulos, GD .
NATURE CELL BIOLOGY, 2001, 3 (11) :1014-1019
[6]   Identification of ubiquitin ligases required for skeletal muscle atrophy [J].
Bodine, SC ;
Latres, E ;
Baumhueter, S ;
Lai, VKM ;
Nunez, L ;
Clarke, BA ;
Poueymirou, WT ;
Panaro, FJ ;
Na, EQ ;
Dharmarajan, K ;
Pan, ZQ ;
Valenzuela, DM ;
DeChiara, TM ;
Stitt, TN ;
Yancopoulos, GD ;
Glass, DJ .
SCIENCE, 2001, 294 (5547) :1704-1708
[7]   Increased phosphorylation of myosin light chain associated with slow-to-fast transition in rat soleus [J].
Bozzo, C ;
Stevens, L ;
Toniolo, L ;
Mounier, Y ;
Reggiani, C .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2003, 285 (03) :C575-C583
[8]   IKKβ/NF-κB activation causes severe muscle wasting in mice [J].
Cai, DS ;
Frantz, JD ;
Tawa, NE ;
Melendez, PA ;
Oh, BC ;
Lidov, HGW ;
Hasselgren, PO ;
Frontera, WR ;
Lee, J ;
Glass, DJ ;
Shoelson, SE .
CELL, 2004, 119 (02) :285-298
[9]   Plasticity of skeletal muscle phenotype: Mechanical consequences [J].
Caiozzo, VJ .
MUSCLE & NERVE, 2002, 26 (06) :740-768
[10]   Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain [J].
Centner, T ;
Yano, J ;
Kimura, E ;
McElhinny, AS ;
Pelin, K ;
Witt, CC ;
Bang, ML ;
Trombitas, K ;
Granzier, H ;
Gregorio, CC ;
Sorimachi, H ;
Labeit, S .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 306 (04) :717-726