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10.1007/BF00430870Virchows Arch. (Pathol. Anat.), 393
- Publisher
- Wiley
- Copyright
- © 2015 Federation of European Biochemical Societies
- eISSN
- 1873-3468
- DOI
- 10.1016/0014-5793(88)80863-9
- Publisher site
- See Article on Publisher Site
Abstract
The quantity and the electrophoretic characteristics of desmin were analyzed in a familial skeletal muscle disorder, characterized by the intra‐sarcoplasmic accumulation of an electron‐dense granulo‐filamentous material facing the Z‐lines and reacting strongly with polyclonal anti‐desmin antibodies. The analysis was performed on biopsies from the deltoid muscles of 4 patients, members of 2 families. In the 4 biopsies, an increase in the relative amount of desmin compared to that of actin or insoluble proteins (3 fold) and in the number of isovariants (6 instead of 3) was observed. The isovariants of desmin were similar to those described in Purkinje fibres of the heart as a phosphorylated form of the protein [(1987) Eur. J. Cell Biol. 44, 68–781]. Therefore, post‐translational events could affect both the polymerization and the amount of desmin filaments in this autosomal dominant familial myopathy.
Journal
Febs Letters – Wiley
Published: Apr 25, 1988
Keywords: ; ; ;