Are cysteine-rich and COOH-terminal domains of dystrophin critical for sarcolemmal localization?

D Récan; P Chafey; F Leturcq; J P Hugnot; N Vincent; F Tomé; H Collin; D Simon; P Czernichow; L V Nicholson

doi:10.1172/JCI115640

Published February 1, 1992 - More info

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Abstract

It has been hypothesized that the tight localization of dystrophin at the muscle membrane is carried out by its cysteine-rich and/or carboxyl domains. We report the results of biochemical and immunocytochemical investigations of dystrophin in muscle from a 1-yr-old patient with a large deletion that removes the distal part of the dystrophin gene, thus spanning the exons coding for the cysteine-rich and the carboxy-terminal domains, and extends beyond the glycerol kinase and congenital adrenal hypoplasia genes. Immunological analysis of muscle dystrophin shows that the deletion results in the production of a truncated, but stable, polypeptide correctly localized at the sarcolemma. These data indicate that neither the cysteine-rich domain, nor the carboxyl domain, are necessary for the appearance of normal dystrophin sarcolemmal localization.

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Are cysteine-rich and COOH-terminal domains of dystrophin critical for sarcolemmal localization?

D Récan, P Chafey, F Leturcq, J P Hugnot, N Vincent, F Tomé, H Collin, D Simon, P Czernichow, and L V Nicholson

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Are cysteine-rich and COOH-terminal domains of dystrophin critical for sarcolemmal localization?

D Récan, P Chafey, F Leturcq, J P Hugnot, N Vincent, F Tomé, H Collin, D Simon, P Czernichow, and L V Nicholson

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