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

Doran P, Martin G, Dowling P, Jockusch H, Ohlendieck K (2006)
PROTEOMICS 6(16): 4610-4621.

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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-linked muscular dystrophy is established, it is not well-known how pathophysiological 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 Fbxol 1-protein, adenylate kinase, beta-haemoglobin and dihydrolipoarnide 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 and may be exploitable as a new approach to counteract muscle degeneration.
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Doran P, Martin G, Dowling P, Jockusch H, Ohlendieck K. Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. PROTEOMICS. 2006;6(16):4610-4621.
Doran, P., Martin, G., Dowling, P., Jockusch, H., & Ohlendieck, K. (2006). Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. PROTEOMICS, 6(16), 4610-4621.
Doran, P., Martin, G., Dowling, P., Jockusch, H., and Ohlendieck, K. (2006). Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. PROTEOMICS 6, 4610-4621.
Doran, P., et al., 2006. Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. PROTEOMICS, 6(16), p 4610-4621.
P. Doran, et al., “Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP”, PROTEOMICS, vol. 6, 2006, pp. 4610-4621.
Doran, P., Martin, G., Dowling, P., Jockusch, H., Ohlendieck, K.: Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. PROTEOMICS. 6, 4610-4621 (2006).
Doran, Philip, Martin, Geraldine, Dowling, Paul, Jockusch, Harald, and Ohlendieck, Kay. “Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP”. PROTEOMICS 6.16 (2006): 4610-4621.
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