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    Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP


    Doran, Philip and Martin, Geraldine and Dowling, Paul and Jockusch, Harald and Ohlendieck, Kay (2006) Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. Proteomics, 6 (16). pp. 4610-4621. ISSN 1615-9853

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    Abstract

    Duchenne muscular dystrophy is the most commonly inherited neuromuscular disorder in humans. Although the primary genetic deficiency of dystrophin in X-linkedmuscular dystrophy is established, it isnotwell-known howpathophysiological events trigger the actual fibre degeneration. We have therefore performed a DIGE analysis of normal diaphragm muscle versus the severely affected x-linked muscular dystrophy (MDX) diaphragm, which represents an established animal model of dystrophinopathy. Out of 2398 detectable 2-D protein spots, 35 proteins showed a drastic differential expression pattern, with 21 proteins being decreased, including Fbxo11-protein, adenylate kinase, b-haemoglobin and dihydrolipoamide dehydrogenase, and 14 proteins being increased, including cvHSP, aldehyde reductase, desmin, vimentin, chaperonin, cardiac and muscle myosin heavy chain. This suggests that lack of sarcolemmal integrity triggers a generally perturbed protein expression pattern in dystrophin-deficient fibres. However, the most significant finding was the dramatic increase in the small heat shock protein cvHSP, which was confirmed by 2-D immunoblotting. Confocal fluorescence microscopy revealed elevated levels of cvHSP in MDX fibres. An immunoblotting survey of other key heat shock proteins showed a differential expression pattern in MDX diaphragm. Stress response appears to be an important cellular mechanism in dystrophic muscle andmay be exploitable as a new approach to counteractmuscle degeneration.

    Item Type: Article
    Keywords: Cardiovascular heat shock protein; DIGE; MDX diaphragm; Muscular dystrophy; Skeletal muscle proteomics;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 7349
    Identification Number: https://doi.org/10.1002/pmic.200600082
    Depositing User: Paul Dowling
    Date Deposited: 16 Aug 2016 15:45
    Journal or Publication Title: Proteomics
    Publisher: Wiley
    Refereed: Yes
    Funders: Science Foundation Ireland (SFI), Muscular Dystrophy Ireland, European Commission, Health Research Board (HRB)
    URI:

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