Spheroid body myopathy revisited

Goebel, Hans H.; D'Agostino, A; Wilson, Jacob M.; Cole, George W.; Foroud, Tatiana; Koller, Daniel L.; Farlow, Martin R.; Azzarelli, Biagio; Muller, Jans

doi:10.1002/(sici)1097-4598(199709)20:9<1127::aid-mus6>3.0.co;2-a

Cited by 29 publications

(12 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similar disruptions of myofibrils and aggregations of desmin filaments were seen in the myocardium and intestinal smooth muscle (18). These are the classical features of desminopathies (16,26,27), and similar abnormalities have been observed in desmin null mutant mice (12)(13)(14)(15). In the mice, myofibrils are fragile upon mechanical stress, and muscle weakness develops with age.…”

Section: Muscle and Z-band Abnormalities Of A Patient With A Severesupporting

confidence: 58%

“…However, this exclusion does not necessarily rule out the possibility that certain types of desminopathies may harbor desmin gene defects, because myopathies associated with desmin abnormalities are highly heterogeneous. They include cardiomyopathies, congenital myopathies with either childhood or adult onset of disease, cardiomyopathy associated with myopathy, and a multisystemic disorder involving skeletal muscle, heart, peripheral nerves, and intestinal muscularis propria (16,(35)(36)(37)(38). In addition, morphological abnormalities in desmin-related myopathies are diverse, as is their mode of inheritance.…”

Section: Discussionmentioning

confidence: 99%

“…16). The clumping of desmin in muscle cells of these patients bears a striking resemblance to the keratin aggregates that accumulate in degenerating epithelial cells of various human keratin disorders (for review, see ref.…”

mentioning

confidence: 99%

See 2 more Smart Citations

A dysfunctional desmin mutation in a patient with severe generalized myopathy

Muñoz-Mármol

Strasser

Isamat

et al. 1998

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

242

172

View full text Add to dashboard Cite

Mice lacking desmin produce muscle fibers with Z disks and normal sarcomeric organization. However, the muscles are mechanically fragile and degenerate upon repeated contractions. We report here a human patient with severe generalized myopathy and aberrant intrasarcoplasmic accumulation of desmin intermediate filaments. Muscle tissue from this patient lacks the wild-type desmin allele and has a desmin gene mutation encoding a 7-aa deletion within the coiled-coil segment of the protein. We show that recombinant desmin harboring this deletion cannot form proper desmin intermediate filament networks in cultured cells, nor is it able to assemble into 10-nm filaments in vitro. These findings provide direct evidence that a mutation in desmin can cause human myopathies.

show abstract

Section: Muscle and Z-band Abnormalities Of A Patient With A Severesupporting

confidence: 58%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

A dysfunctional desmin mutation in a patient with severe generalized myopathy

Muñoz-Mármol

Strasser

Isamat

et al. 1998

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

242

172

View full text Add to dashboard Cite

show abstract

“…DRM constitute a newly designated group of myopathies marked by intracellular accumulation of desmin, the intermediate filament specific to muscle fibres that in some pathologic conditions may accumulate in cytoplasmic bodies [3], sarcoplasmic bodies [4], spheroid bodies [5] and granulofilamentous material [6].…”

Section: Introductionmentioning

confidence: 99%

Desmin-related myopathy: clinical, electrophysiological, radiological, neuropathological and genetic studies

Olivé

Goldfarb

Moreno

et al. 2004

Journal of the Neurological Sciences

View full text Add to dashboard Cite

“…Subsequent studies found extensive variation in symptom onset as well as disease progression and severity. 2 No other families with SBM have been reported.…”

mentioning

confidence: 99%