浪费的
骨骼肌
蛋白酶体
泛素
细胞生物学
内科学
生物
解剖
医学
生物化学
基因
作者
Didier Attaix,Sophie Ventadour,Audrey Codran,Daniel Béchet,Daniel Taillandier,Lydie Combaret
出处
期刊:Essays in Biochemistry
[Portland Press]
日期:2005-12-01
卷期号:41 (1): 173-173
被引量:226
摘要
The ubiquitin–proteasome system (UPS) is believed to degrade the major contractile skeletal muscle proteins and plays a major role in muscle wasting. Different and multiple events in the ubiquitination, deubiquitination and proteolytic machineries are responsible for the activation of the system and subsequent muscle wasting. However, other proteolytic enzymes act upstream (possibly m-calpain, cathepsin L, and/or caspase 3) and downstream (tripeptidyl-peptidase II and aminopeptidases) of the UPS, for the complete breakdown of the myofibrillar proteins into free amino acids. Recent studies have identified a few critical proteins that seem necessary for muscle wasting {i.e. the MAFbx (muscle atrophy F-box protein, also called atrogin-1) and MuRF-1 [muscle-specific RING (really interesting new gene) finger 1] ubiquitin–protein ligases}. The characterization of their signalling pathways is leading to new pharmacological approaches that can be useful to block or partially prevent muscle wasting in human patients.
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