Literature DB >> 8242173

Desmin pathology in neuromuscular diseases.

H H Goebel1, A Bornemann.   

Abstract

Desmin is an intermediate filament protein that in striated muscle is normally located at Z-bands, beneath the sarcolemma, and prominently at neuromuscular junctions. It is abundant during myogenesis and in regenerating fibers, but decreases in amount with maturation; in regenerating and denervated muscle fibers it is co-expressed with vimentin. Aggregates of desmin occur as nonspecific cytoplasmic bodies or cytoplasmic spheroid complexes, similar to the aggregates of keratin filaments in Mallory bodies or the neurofilament aggregates in Lewy bodies. In all three instances, alpha-B crystallin may be associated with desmin. There are now increasing numbers of neuromuscular disorders in which abnormal amounts of desmin, some abnormally phosphorylated, feature prominently in muscle fibres. Several of these diseases, including spheroid body myopathy, granulo-filamentous body myopathy and the dystrophinopathies, are familial. Ultrastructural and immunohistochemical studies of desmin have considerably broadened our understanding of the pathology of the cytoskeleton in muscle fibers and in certain hereditary neuromuscular diseases.

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Year:  1993        PMID: 8242173     DOI: 10.1007/bf02915105

Source DB:  PubMed          Journal:  Virchows Arch B Cell Pathol Incl Mol Pathol        ISSN: 0340-6075


  9 in total

Review 1.  Intermediate filaments as dynamic structures.

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

2.  Hepatocyte cytokeratins are hyperphosphorylated at multiple sites in human alcoholic hepatitis and in a mallory body mouse model.

Authors:  C Stumptner; M B Omary; P Fickert; H Denk; K Zatloukal
Journal:  Am J Pathol       Date:  2000-01       Impact factor: 4.307

3.  Pi-Pi contacts are an overlooked protein feature relevant to phase separation.

Authors:  Robert McCoy Vernon; Paul Andrew Chong; Brian Tsang; Tae Hun Kim; Alaji Bah; Patrick Farber; Hong Lin; Julie Deborah Forman-Kay
Journal:  Elife       Date:  2018-02-09       Impact factor: 8.140

4.  A mutation in desmin makes skeletal muscle less vulnerable to acute muscle damage after eccentric loading in rats.

Authors:  Henning T Langer; Agata A Mossakowski; Alec M Avey; Ross P Wohlgemuth; Lucas R Smith; Herman Zbinden-Foncea; Keith Baar
Journal:  FASEB J       Date:  2021-09       Impact factor: 5.834

5.  Suspected myofibrillar myopathy in Arabian horses with a history of exertional rhabdomyolysis.

Authors:  S J Valberg; E C McKenzie; L V Eyrich; J Shivers; N E Barnes; C J Finno
Journal:  Equine Vet J       Date:  2015-09-07       Impact factor: 2.888

6.  Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle.

Authors:  Z Li; M Mericskay; O Agbulut; G Butler-Browne; L Carlsson; L E Thornell; C Babinet; D Paulin
Journal:  J Cell Biol       Date:  1997-10-06       Impact factor: 10.539

7.  Disruption of muscle architecture and myocardial degeneration in mice lacking desmin.

Authors:  D J Milner; G Weitzer; D Tran; A Bradley; Y Capetanaki
Journal:  J Cell Biol       Date:  1996-09       Impact factor: 10.539

8.  Differential organization of desmin and vimentin in muscle is due to differences in their head domains.

Authors:  R B Cary; M W Klymkowsky
Journal:  J Cell Biol       Date:  1994-07       Impact factor: 10.539

9.  Generation of desminopathy in rats using CRISPR-Cas9.

Authors:  Henning T Langer; Agata A Mossakowski; Brandon J Willis; Kristin N Grimsrud; Joshua A Wood; Kevin C K Lloyd; Hermann Zbinden-Foncea; Keith Baar
Journal:  J Cachexia Sarcopenia Muscle       Date:  2020-09-07       Impact factor: 12.910

  9 in total

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