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The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1992 Feb;89(2):712–716. doi: 10.1172/JCI115640

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

D Récan 1, P Chafey 1, F Leturcq 1, J P Hugnot 1, N Vincent 1, F Tomé 1, H Collin 1, D Simon 1, P Czernichow 1, L V Nicholson 1, et al.
PMCID: PMC442907  PMID: 1737859

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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Selected References

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