No alteration in gene expression of components of the ubiquitin proteasome proteolytic pathway in dystrophin-deficient muscles
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...
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| Published in | FEBS letters Vol. 393; no. 2; pp. 292 - 296 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier B.V
16.09.1996
Wiley |
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| Online Access | Get full text |
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| Abstract | 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. |
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| AbstractList | 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. 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. 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 Ca2+‐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. 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. |
| Author | Taillandier, Daniel Boespflug-Tanguy, Odile Samuels, Susan E. Combaret, Lydie Voisin, Laure Attaix, Didier |
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| Copyright | 1996 FEBS Letters 393 (1996) 1873-3468 © 2015 Federation of European Biochemical Societies Distributed under a Creative Commons Attribution 4.0 International License |
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| Keywords | Ubiquitin Calpain DMD Skeletal muscle Protein turnover Muscular dystrophy Proteasome 14-kDa E2 |
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| Snippet | Increased expression of critical components of the ubiquitin-dependent proteolytic pathway occurs in any muscle wasting condition so far studied in rodents... Increased expression of critical components of the ubiquitin‐dependent proteolytic pathway occurs in any muscle wasting condition so far studied in rodents... |
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| SubjectTerms | 14-kDa E2 14-kDa ubiquitin conjugating enzyme E2 Adolescent Animals Calpain Calpain - biosynthesis Cathepsin D - biosynthesis Cathepsin L Cathepsins - biosynthesis Cellular Biology Child Cysteine Endopeptidases - biosynthesis Cysteine Endopeptidases - genetics DMD Duchonne muscular dystrophy Dystrophin - deficiency Endopeptidases Female Fibrosis Gene Expression Humans Life Sciences Male Mice Mice, Inbred mdx Multienzyme Complexes - biosynthesis Multienzyme Complexes - genetics Muscle, Skeletal - metabolism Muscle, Skeletal - pathology Muscular Dystrophies - metabolism Muscular Dystrophies - pathology Muscular Dystrophies - physiopathology Muscular dystrophy Necrosis Proteasome Proteasome Endopeptidase Complex Protein turnover Reference Values RNA, Messenger - analysis Skeletal muscle Transcription, Genetic Ubiquitin Ubiquitins - biosynthesis Ubiquitins - genetics |
| Title | No alteration in gene expression of components of the ubiquitin proteasome proteolytic pathway in dystrophin-deficient muscles |
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