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Lower active force generation and improved fatigue resistance in skeletal muscle from desmin deficient mice.

Balogh, Johanna LU ; Li, Z; Paulin, D and Arner, Anders LU (2003) In Journal of Muscle Research and Cell Motility 24(7). p.453-459
Abstract
The mechanical effects of the intermediate filament protein desmin was examined in desmin deficient mice (Des-/-) and their wild type control (Des+/+). Active force generation was determined in intact soleus muscles and in skinned single fibres from soleus and psoas. A decreased force generation of skinned muscle fibres from Des-/- mice and a tendency towards decreased active force in intact soleus muscle were detected. Concentrations of the contractile protein actin and myosin were not altered in Des-/- muscles. Ca(2+)-sensitivity of skinned single fibres in Des-/- muscles was unchanged compared to Des+/+. Using a protocol with repeated short tetani an increased fatigue resistance was found in the intact soleus muscles from Des-/- mice.... (More)
The mechanical effects of the intermediate filament protein desmin was examined in desmin deficient mice (Des-/-) and their wild type control (Des+/+). Active force generation was determined in intact soleus muscles and in skinned single fibres from soleus and psoas. A decreased force generation of skinned muscle fibres from Des-/- mice and a tendency towards decreased active force in intact soleus muscle were detected. Concentrations of the contractile protein actin and myosin were not altered in Des-/- muscles. Ca(2+)-sensitivity of skinned single fibres in Des-/- muscles was unchanged compared to Des+/+. Using a protocol with repeated short tetani an increased fatigue resistance was found in the intact soleus muscles from Des-/- mice. In conclusion, desmin intermediate filaments are required for optimal generation or transmission of active force in skeletal muscle. Although other studies have shown that the desmin intermediate filaments appear to influence Ca(2+)-handling, the Ca(2+)-sensitivity of the contractile filaments is not altered in skeletal muscle of Des-/- mice. Previous studies have reported a switch towards slower myosin isoforms in slow skeletal muscle of Des-/- mice. The increased fatigue resistance show that this change is reflected in the physiological function of the muscle. (Less)
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type
Contribution to journal
publication status
published
subject
in
Journal of Muscle Research and Cell Motility
volume
24
issue
7
pages
453 - 459
publisher
Springer
external identifiers
  • wos:000186410900008
  • pmid:14677648
  • scopus:0344826002
ISSN
0142-4319
DOI
10.1023/A:1027353930229
language
English
LU publication?
yes
id
16fddba6-8c2e-41fd-8561-f53f9e271045 (old id 119601)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=14677648&dopt=Abstract
date added to LUP
2007-07-10 09:53:54
date last changed
2017-09-17 07:52:34
@article{16fddba6-8c2e-41fd-8561-f53f9e271045,
  abstract     = {The mechanical effects of the intermediate filament protein desmin was examined in desmin deficient mice (Des-/-) and their wild type control (Des+/+). Active force generation was determined in intact soleus muscles and in skinned single fibres from soleus and psoas. A decreased force generation of skinned muscle fibres from Des-/- mice and a tendency towards decreased active force in intact soleus muscle were detected. Concentrations of the contractile protein actin and myosin were not altered in Des-/- muscles. Ca(2+)-sensitivity of skinned single fibres in Des-/- muscles was unchanged compared to Des+/+. Using a protocol with repeated short tetani an increased fatigue resistance was found in the intact soleus muscles from Des-/- mice. In conclusion, desmin intermediate filaments are required for optimal generation or transmission of active force in skeletal muscle. Although other studies have shown that the desmin intermediate filaments appear to influence Ca(2+)-handling, the Ca(2+)-sensitivity of the contractile filaments is not altered in skeletal muscle of Des-/- mice. Previous studies have reported a switch towards slower myosin isoforms in slow skeletal muscle of Des-/- mice. The increased fatigue resistance show that this change is reflected in the physiological function of the muscle.},
  author       = {Balogh, Johanna and Li, Z and Paulin, D and Arner, Anders},
  issn         = {0142-4319},
  language     = {eng},
  number       = {7},
  pages        = {453--459},
  publisher    = {Springer},
  series       = {Journal of Muscle Research and Cell Motility},
  title        = {Lower active force generation and improved fatigue resistance in skeletal muscle from desmin deficient mice.},
  url          = {http://dx.doi.org/10.1023/A:1027353930229},
  volume       = {24},
  year         = {2003},
}