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When size really does matter
Author(s) -
Deschenes Michael R.
Publication year - 2007
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2007.128546
Subject(s) - muscle atrophy , atrophy , proteasome , sarcopenia , ubiquitin , protein degradation , denervation , skeletal muscle , ubiquitin ligase , biology , endocrinology , medicine , microbiology and biotechnology , gene , genetics
The loss of skeletal muscle mass has been shown to have serious health implications. For example, decreased muscle size – atrophy – has been linked with osteoporosis, type II diabetes, cachexia, and among the aged a greater incidence of falls (see Janssen & Ross, 2005). As a result, gaining a clear understanding of the molecular and cellular mechanisms that trigger muscle atrophy has become a vital health initiative. Although a recent report (Edstrom et al. 2006) suggests that a different mechanism is responsible for sarcopaenia, or age-related loss of muscle size, a convincing body of evidence has identified the ubiquitin proteosome pathway as a major regulator of the sequence of events leading to the degradation of contractile proteins in adult muscle. Crucial constituents of this pathway are ligases that tag specific proteins for degradation and insert those tagged proteins into the proteosome complex, as well as peptides that comprise the body of the proteosome, where the actual degradation occurs.