Literature DB >> 7565929

Desmin-related neuromuscular disorders.

H H Goebel1.   

Abstract

Desmin, the intermediate filament protein of skeletal muscle fibers, cardiac myocytes, and certain smooth muscle cells, is a member of the cytoskeleton linking Z-bands with the plasmalemma and the nucleus. The pathology of desmin in human neuromuscular disorders is always marked by increased amounts, diffusely or focally. Desmin is highly expressed in immature muscle fibers, both during fetal life and regeneration as well as in certain congenital myopathies, together with vimentin. Desmin is also enriched in neonatal myotonic dystrophy and small fibers in infantile spinal muscular atrophy. Focal accretion of desmin may be twofold, in conjunction with certain inclusion bodies, cytoplasmic and spheroid bodies, and in a more patchy fashion, granulofilamentous material. Both lesions have been found in certain families, affected by a myopathy and/or cardiomyopathy. Other proteins, e.g., dystrophin, vimentin, actin, ubiquitin, and alpha-B crystallin, may also be overexpressed. Desmin pathology may be genetically regulated or may merely reflect profoundly impaired metabolism of several proteins within myofibers.

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Year:  1995        PMID: 7565929     DOI: 10.1002/mus.880181114

Source DB:  PubMed          Journal:  Muscle Nerve        ISSN: 0148-639X            Impact factor:   3.217


  17 in total

1.  Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function.

Authors:  M P Bova; O Yaron; Q Huang; L Ding; D A Haley; P L Stewart; J Horwitz
Journal:  Proc Natl Acad Sci U S A       Date:  1999-05-25       Impact factor: 11.205

Review 2.  Desmin cytoskeleton in healthy and failing heart.

Authors:  Y Capetanaki
Journal:  Heart Fail Rev       Date:  2000-10       Impact factor: 4.214

Review 3.  Intermediate filaments as dynamic structures.

Authors:  M W Klymkowsky
Journal:  Cancer Metastasis Rev       Date:  1996-12       Impact factor: 9.264

4.  The RNA-binding protein Rbfox1 regulates splicing required for skeletal muscle structure and function.

Authors:  Simona Pedrotti; Jimena Giudice; Adan Dagnino-Acosta; Mark Knoblauch; Ravi K Singh; Amy Hanna; Qianxing Mo; John Hicks; Susan Hamilton; Thomas A Cooper
Journal:  Hum Mol Genet       Date:  2015-01-09       Impact factor: 6.150

5.  Myofibril breakdown during atrophy is a delayed response requiring the transcription factor PAX4 and desmin depolymerization.

Authors:  Alexandra Volodin; Idit Kosti; Alfred Lewis Goldberg; Shenhav Cohen
Journal:  Proc Natl Acad Sci U S A       Date:  2017-01-17       Impact factor: 11.205

6.  Clinical and myopathological characteristics of desminopathy caused by a mutation in desmin tail domain.

Authors:  Paul Maddison; Maxwell S Damian; Caroline Sewry; Catherine McGorrian; John B Winer; Zagaa Odgerel; Alexey Shatunov; Hee Suk Lee; Lev G Goldfarb
Journal:  Eur Neurol       Date:  2012-10-05       Impact factor: 1.710

7.  microRNA-206 promotes skeletal muscle regeneration and delays progression of Duchenne muscular dystrophy in mice.

Authors:  Ning Liu; Andrew H Williams; Johanna M Maxeiner; Svetlana Bezprozvannaya; John M Shelton; James A Richardson; Rhonda Bassel-Duby; Eric N Olson
Journal:  J Clin Invest       Date:  2012-05-01       Impact factor: 14.808

8.  Desmin splice variants causing cardiac and skeletal myopathy.

Authors:  K Y Park; M C Dalakas; H H Goebel; V J Ferrans; C Semino-Mora; S Litvak; K Takeda; L G Goldfarb
Journal:  J Med Genet       Date:  2000-11       Impact factor: 6.318

9.  Intermediate filament diseases: desminopathy.

Authors:  Lev G Goldfarb; Montse Olivé; Patrick Vicart; Hans H Goebel
Journal:  Adv Exp Med Biol       Date:  2008       Impact factor: 2.622

Review 10.  Distal myopathies.

Authors:  Mazen M Dimachkie; Richard J Barohn
Journal:  Neurol Clin       Date:  2014-05-15       Impact factor: 3.806

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