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• W2034308377 abstract "Muscle cachexia induced by sepsis, severe injury, cancer, and a number of other catabolic conditions is mainly caused by increased protein degradation, in particular breakdown of myofibrillar proteins. Ubiquitin-proteasome-dependent proteolysis is the predominant mechanism of muscle protein loss in these conditions, but there is evidence that several other regulatory mechanisms may be important as well. Some of those mechanisms are reviewed in this article and they include pre-, para-, and postproteasomal mechanisms. Among preproteasomal mechanisms, mediators, receptor binding, signaling pathways, activation of transcription factors, and modification of proteins are important. Several paraproteasomal mechanisms may influence the trafficking of ubiquitinated proteins and their interaction with the proteasome, including the expression and activity of the COP9 signalosome, the carboxy terminus of heat shock protein 70-interacting protein (CHIP) and valosin-containing protein (VCP). Finally, because the proteasome does not degrade proteins completely into free amino acids but into peptides, postproteasomal degradation of peptides by the giant protease tripeptidyl peptidase II (TPP II) and various aminopeptidases is important in muscle catabolism. Thus, multiple mechanisms and regulatory steps may influence the breakdown of ubiquitinated muscle proteins by the 26S proteasome." @default.
• W2034308377 created "2016-06-24" @default.
• W2034308377 creator A5001846674 @default.
• W2034308377 creator A5012684884 @default.
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• W2034308377 date "2002-01-01" @default.
• W2034308377 modified "2023-09-24" @default.
• W2034308377 title "Molecular Regulation of Muscle Cachexia: It May Be More Than the Proteasome" @default.
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• W2034308377 doi "https://doi.org/10.1006/bbrc.2001.5849" @default.
• W2034308377 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11779124" @default.
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