Correlation of dystrophin-glycoprotein complex and focal adhesion complex with myosin heavy chain isoforms in rat skeletal muscle
- PMID: 19040708
- DOI: 10.1111/j.1748-1716.2008.01944.x
Correlation of dystrophin-glycoprotein complex and focal adhesion complex with myosin heavy chain isoforms in rat skeletal muscle
Abstract
Aim: The dystrophin-glycoprotein complex (DGC) and focal adhesion complex (FAC) are transmembrane structures in muscle fibres that link the intracellular cytoskeleton to the extracellular matrix. DGC and FAC proteins are abundant in slow-type muscles, indicating the structural reinforcement which play a pivotal role in continuous force output to maintain posture for long periods. The aim of the present study was to examine the expression of these structures across fast-type muscles containing different myosin heavy chain (MHC) isoform patterns which reflect the fatigue-resistant characteristics of skeletal muscle.
Methods: We measured the expression of dystrophin and beta1 integrin (representative proteins of DGC and FAC respectively) in plantaris, extensor digitorum longus, tibialis anterior, red and white portions of gastrocnemius, superficial portion of vastus lateralis and diaphragm, in comparison with soleus (SOL) and cardiac muscle from rats.
Results: The expression of dystrophin and beta1 integrin correlated positively with the percentage of type I, IIa and IIx MHC isoforms and negatively with that of type IIb MHC isoform in fast-type skeletal muscles, and their expression was abundant in SOL and cardiac muscle.
Conclusion: Our results support the idea that DGC and FAC are among the factors that explain the fatigue-resistant property not only of slow-type but also of fast-type skeletal muscles.
Comment in
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Special gears for full-time engines: association of dystrophin-glycoprotein complex and focal adhesion complex with myosin heavy chain isoforms in rat skeletal muscle.Acta Physiol (Oxf). 2009 Apr;195(4):405. doi: 10.1111/j.1748-1716.2009.01959_2.x. Acta Physiol (Oxf). 2009. PMID: 19291146 No abstract available.
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