Muscle wasting and changes in muscle protein metabolism in chronic obstructive pulmonary disease

被引:76
作者
Jagoe, RT [1 ]
Engelen, MPKJ
机构
[1] Univ Liverpool, Hosp Aintree, Ctr Clin Sci, Dept Med,Pulm & Rehabil Res Grp, Liverpool L9 7AL, Merseyside, England
[2] State Univ Limburg Hosp, Dept Resp Med, NL-6201 BX Maastricht, Netherlands
关键词
amino acids; chronic obstructive pulmonary disease; muscle wasting; protein degradation; protein synthesis;
D O I
10.1183/09031936.03.00004608
中图分类号
R56 [呼吸系及胸部疾病];
学科分类号
摘要
Loss of skeletal muscle mass is now recognised as an important feature of chronic obstructive pulmonary disease (COPD) which contributes to symptoms and influences prognosis. The changes in skeletal muscle remain poorly understood, largely because only a few studies have been performed to define the adaptations in whole body and muscle protein metabolism in COPD. The first sections of this review summarise background information about skeletal muscle wasting in COPD, and focuses on the studies concerned with amino acid profiles and protein synthesis and degradation rates. To aid interpretation some discussion of the techniques commonly used is included. A variety of different catabolic factors may determine whether chronic obstructive pulmonary disease patients become cachectic, The precise role for each one of these factors as well as the intracellular pathways activated in muscle as a result of chronic obstructive pulmonary disease are unknown and remain to be defined. Details of the actions of a range of different catabolic factors and potential mechanisms will be discussed.
引用
收藏
页码:52S / 63S
页数:12
相关论文
共 134 条
[81]   Oxidative enzyme activities of the vastus lateralis muscle and the functional status in patients with COPD [J].
Maltais, F ;
LeBlanc, P ;
Whittom, F ;
Simard, C ;
Marquis, K ;
Bélanger, M ;
Breton, MJ ;
Jobin, J .
THORAX, 2000, 55 (10) :848-853
[82]   Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients [J].
Mansoor, O ;
Beaufrere, B ;
Boirie, Y ;
Ralliere, C ;
Taillandier, D ;
Aurousseau, E ;
Schoeffler, P ;
Arnal, M ;
Attaix, D .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (07) :2714-2718
[83]   Midthigh muscle cross-sectional area is a better predictor of mortality than body mass index in patients with chronic obstructive pulmonary disease [J].
Marquis, K ;
Debigaré, R ;
Lacasse, Y ;
LeBlanc, P ;
Jobin, J ;
Carrier, G ;
Maltais, F .
AMERICAN JOURNAL OF RESPIRATORY AND CRITICAL CARE MEDICINE, 2002, 166 (06) :809-813
[84]   Expression of insulin growth factor-1 splice variants and structural genes in rabbit skeletal muscle induced by stretch and stimulation [J].
McKoy, G ;
Ashley, W ;
Mander, J ;
Yang, SY ;
Williams, N ;
Russell, B ;
Goldspink, G .
JOURNAL OF PHYSIOLOGY-LONDON, 1999, 516 (02) :583-592
[85]  
MEDINA R, 1991, BIOMED BIOCHIM ACTA, V50, P347
[86]   TNF-alpha-induced insulin resistance in vivo and its prevention by troglitazone [J].
Miles, PDG ;
Romeo, OM ;
Higo, K ;
Cohen, A ;
Rafaat, K ;
Olefsky, JM .
DIABETES, 1997, 46 (11) :1678-1683
[87]   Mechanisms causing loss of lean body mass in kidney disease [J].
Mitch, WE .
AMERICAN JOURNAL OF CLINICAL NUTRITION, 1998, 67 (03) :359-366
[88]   Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting [J].
Mitch, WE ;
Bailey, JL ;
Wang, X ;
Jurkovitz, C ;
Newby, D ;
Price, SR .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 1999, 276 (05) :C1132-C1138
[89]   Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway [J].
Mordier, S ;
Deval, C ;
Béchet, D ;
Tassa, A ;
Ferrara, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (38) :29900-29906
[90]   MUSCLE WASTING IN EMPHYSEMA [J].
MORRISON, WL ;
GIBSON, JNA ;
SCRIMGEOUR, C ;
RENNIE, MJ .
CLINICAL SCIENCE, 1988, 75 (04) :415-420