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No alteration in gene expression of components of the ubiquitin proteasome proteolytic pathway in dystrophin‐deficient muscles
Author(s) -
Combaret Lydie,
Taillandier Daniel,
Voisin Laure,
Samuels Susan E.,
Boespflug-Tanguy Odile,
Attaix Didier
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00910-6
Subject(s) - proteolysis , calpain , wasting , muscular dystrophy , proteasome , ubiquitin , duchenne muscular dystrophy , gene expression , gene , biology , microbiology and biotechnology , dystrophin , proteolytic enzymes , chemistry , endocrinology , biochemistry , genetics , enzyme
Increased expression of critical components of the ubiquitin‐dependent proteolytic pathway occurs in any muscle wasting condition so far studied in rodents where proteolysis rises. We have recently reported similar adaptations in head trauma patients [Mansoor et al. (1996) Proc. Natl. Acad. Sci. USA 93, 2714–2718]. We demonstrate here that the increased muscle protein breakdown seen in mdx mice only correlated with enhanced expression of m ‐calpain, a Ca 2+ ‐activated proteinase. By contrast, no change in mRNA levels for components of the ubiquitin‐proteasome proteolytic process was seen in muscles from both mdx mice and Duchenne muscular dystrophy patients. Thus, gene expression of components of this pathway is not regulated in the chronic wasting that characterizes muscular dystrophy.