Estimate of the proportion of Duchenne muscular dystrophy with autosomal recessive inheritance

Zatz, Mayana; Passos‐Bueno, Maria Rita; Rapaport, David

doi:10.1002/ajmg.1320320328

Cited by 39 publications

(10 citation statements)

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“…Indeed, adding the 18 Duchenne patients and the 32 patients with unrelated disorders reported in this paper to the previously reported patient studies brings the total number of patients studied to 160 patients with unrelated neuromuscular diseases (normal dystrophin) and 98 Duchenne dystrophy patients (dystrophin deficiency). Of all the patients studied, only a single diagnosed Duchenne patient has been found to have normal dystrophin (10), and this patient possibly has an autosomal recessive disorder (16). However, immunoblot and immunofluorescent data have not been reported together for any single patient.…”

mentioning

confidence: 94%

Dystrophin diagnosis: comparison of dystrophin abnormalities by immunofluorescence and immunoblot analyses.

Arahata

Hoffman

Kunkel

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

116

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Immunoblot characterization and immunofluorescence localization of dystrophin are presented for 76 human patients with various neuromuscular diseases. Normal dystrophin (shown by immunoblotting) was invariably visualized as a continuous, peripheral membrane immunostaining of myofibers. Biochemical abnormalities of dystrophin (either lower or higher molecular weight dystrophin) resulted in patchy, discontinuous immunostaining, suggesting that the abnormal dystrophin proteins are not capable of creating a complete membrane cytoskeleton network. There was a very strong correlation of clinical diagnoses with the type of dystrophin abnormality; all Duchenne muscular dystrophy patient muscle contained no detectable dystrophin, Becker muscular dystrophy patient muscle had clearly abnormal dystrophin, and unrelated diseases showed normal dystrophin. However, a single patient of five carrying the diagnosis of Fukuyama dystrophy showed no detectable dystrophin and thus appeared to be a Duchenne dystrophy patient by the biochemical assays. We know of no other case of a patient with a disease thought to be unrelated to Duchenne/Becker dystrophy yet demonstrating dystrophin deficiency. Based on the data presented, we conclude that immunofluorescence is the best technique for the detection of female carriers of Duchenne dystrophy, whereas immunoblotting appears superior for the prognostic diagnosis of Becker muscular dystrophy.

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mentioning

confidence: 94%

Dystrophin diagnosis: comparison of dystrophin abnormalities by immunofluorescence and immunoblot analyses.

Arahata

Hoffman

Kunkel

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

116

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“…Perhaps a deficiency in a dystrophin-associated glycoprotein could explain the DMD-like symptoms observed in suspected autosomal recessive patients [39,40] that express apparently normal dystrophin.…”

Section: Discussionmentioning

confidence: 99%

Dystrophin-glycoprotein complex

Sunada

Campbell

1995

Current Opinion in Neurology

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SummaryDystrophin, the high molecular weight protein product of the Duchenne muscular dystrophy (DMD) gene, is localized to the sarcolemma of normal skeletal muscle but is absent from the skeletal muscle of patients with DMD and mdx mice. The predicted amino acid sequence of dystrophin suggests that dystrophin is involved in the anchoring of sarcolemmal proteins to the underlying cytoskeleton. However, the sarcolemmal proteins which are associated with or bound to dystrophin are not known and the status of these proteins in muscle where dystrophin is absent is also unknown.Here, we review the purification of a dystrophin-glycoprotein complex and the identification of five dystrophin-associated proteins, including four dystrophin-associated glycoproteins. The dystrophin-glycoprotein complex was isolated following digitonin-solubilization of rabbit skeletal muscle membranes using WGA-Sepharose and DEAE-cellulose and further purified by sucrose density gradient centrifugation. In addition to dystrophin, the complex contains a 59 kDa protein triplet and four glycoproteins of 156 kDa, 50 kDa, 43 kDa and 35 kDa. Indirect immunofluorescence with monoclonal antibodies specific for dystrophin, the 156 kDa glycoprotein or the 50 kDa glycoprotein demonstrated a restricted localization of the dystrophin-glycoprotein complex to the sarcolemma of skeletal muscle. Immunoaffinity beads specific for dystrophin or the 50 kDa glycoprotein selectively absorb the dystrophin-322 glycoprotein complex, indicating that the components of the complex are tightly associated.A dramatic (~90%) deficiency of the 156 kDa dystrophin-associated glycoprotein was also observed in muscle from mdx mice and DMD patients. Thus, the marked reduction of the 156 kDa glycoprotein in dystrophic muscle, and possibly other dystrophin-associated proteins, may be the initial step(s) involved in the molecular pathogenesis of muscular dystrophy. The elucidation of the function of dystrophin-associated glycoproteins should help to define the function of dystrophin and explain how its absence results in DMD.

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“…In Arab countries, autosomal recessive MD has been reported mainly from Kuwait, Libya, Saudi Arabia, Sudan, Tunisia, and Qatar [Hamida et al, 1983;Salih, 1985;Farag et al, 19891 with presumptive evidence that this form of MD is more common in these communities than in other parts of the world. We think that the estimate from North America and Britain that 5% of the cases are AR [Emery, 19871 and the 6.8% figure of Zatz et al [1989] from Brazil does not apply in Arab communities because the AR gene is highly prevalent with a high rate of consanguinity and the frequency of X-linked MD is correspondingly less than that in other communities.…”

Section: Duchenne-like Muscular Dystrophy In the Arabsmentioning

confidence: 94%