No alteration in gene expression of components of the ubiquitin proteasome proteolytic pathway in dystrophin‐deficient muscles

FEBS Letters

Boespflug-Tanguy, Odile¹  Taillandier, Daniel²  Combaret, Lydie²  Voisin, Laure²  Samuels, Susan E.²  Attaix, Didier² 

[1] INSERM U 384, and Chirurgie Pédiatrique, C.H.U., 63003 Clermont-Ferrand Cedex, France;Centre de Recherche en Nutrition Humaine de Clermont-Ferrand, Unité d'Etude de Métabolisme Azoté, 63122 Ceyrat, France

关键词: Skeletal muscle;    Protein turnover;    Ubiquitin;    Proteasome;    Calpain;    Muscular dystrophy;    14-kDa E2;    14-kDa ubiquitin conjugating enzyme E2;    DMD;    Duchonne muscular dystrophy;   

DOI  :  10.1016/0014-5793(96)00910-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown