Journal article
Analysis of excitation‐contraction‐coupling components in chronically stimulated canine skeletal muscle
European journal of biochemistry, Vol.202(3), pp.739-747
12/1991
DOI: 10.1111/j.1432-1033.1991.tb16428.x
PMID: 1662614
Abstract
The chronic stimulation of predominantly fast‐twitch mammalian skeletal muscle causes a transformation to physiological characteristics of slow‐twitch skeletal muscle. Here, we report the effects of chronic stimulation on the protein components of the sarcoplasmic reticulum and transverse tubular membranes which are directly involved in excitation‐contraction coupling. Comparison of protein composition of microsomal fractions from control and chronically stimulated muscle was performed by immunoblot analysis and also by staining with Coomassie blue or the cationic carbocyanine dye Stains‐all. Consistent with previous experiments, a greatly reduced density was observed for the fast‐twitch isozyme of Ca2+‐ATPase, while the expression of the slow‐twitch Ca2+‐ATPase was found to be greatly enhanced. Components of the sarcolemma (Na+/K+‐ATPase, dystrophin‐glycoprotein complex) and the free sarcoplasmic reticulum (Ca2+‐binding protein sarcalumenin and a 53‐k Da glycoprotein) were not affected by chronic stimulation. The relative abundance of calsequestrin was slightly reduced in transformed skeletal muscle. However, the expression of the ryanodine receptor/Ca2+‐release channel from junctional sarcoplasmic reticulum and the transverse tubular dihydropyridine‐sensitive Ca2+ channel, as well as two junctional sarcoplasmic reticulum protiens of 90 kDa and 94 kDa, was greatly suppressed in transformed muscle. Thus, the expression of the major protein components of the triad junction involved in excitation‐contraction coupling is suppressed, while the expression of other muscle membrane proteins is not affected in chronically stimulated muscle.
Details
- Title: Subtitle
- Analysis of excitation‐contraction‐coupling components in chronically stimulated canine skeletal muscle
- Creators
- Kay OHLENDIECKF. Norman BRIGGSK. Francis LEEAndrew W WECHSLERKevin P CAMPBELL
- Resource Type
- Journal article
- Publication Details
- European journal of biochemistry, Vol.202(3), pp.739-747
- DOI
- 10.1111/j.1432-1033.1991.tb16428.x
- PMID
- 1662614
- NLM abbreviation
- Eur J Biochem
- ISSN
- 0014-2956
- eISSN
- 1432-1033
- Publisher
- Blackwell Publishing Ltd; Oxford, UK
- Number of pages
- 9
- Language
- English
- Date published
- 12/1991
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068386402771
Metrics
30 Record Views