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1 Department of Integrative Biology and Pharmacology, University of Texas-Houston Health Science Center, Houston, Texas 77030; and 2 Department of Veterinary Biomedical Sciences, University of Missouri, Columbia, Missouri 65211
This
investigation examined the effect of mechanical loading state on focal
adhesion kinase (FAK), paxillin, and serum response factor (SRF) in rat
skeletal muscle. We found that FAK concentration and tyrosine
phosphorylation, paxillin concentration, and SRF concentration are all
lower in the lesser load-bearing fast-twitch plantaris and
gastrocnemius muscles compared with the greater load-bearing
slow-twitch soleus muscle. Of these three muscles, 7 days of mechanical
unloading via tail suspension elicited a decrease in FAK tyrosine
phosphorylation only in the soleus muscle and decreases in FAK and
paxillin concentrations only in the plantaris and gastrocnemius
muscles. Unloading decreased SRF concentration in all three muscles.
Mechanical overloading (via bilateral gastrocnemius ablation) for 1 or
8 days increased FAK and paxillin concentrations in the soleus and
plantaris muscles. Additionally, whereas FAK tyrosine phosphorylation
and SRF concentration were increased by
1 day of overloading in the
soleus muscle, these increases did not occur until somewhere between 1 and 8 days of overloading in the plantaris muscle. These data indicate
that, in the skeletal muscles of rats, the focal adhesion complex
proteins FAK and paxillin and the transcription factor SRF are
generally modulated in association with the mechanical loading state of
the muscle. However, the somewhat different patterns of adaptation of
these proteins to altered loading in slow- vs. fast-twitch skeletal
muscles indicate that the mechanisms and time course of adaptation may
partly depend on the prior loading state of the muscle.
compensatory hypertrophy; atrophy; mechanical stress; fiber type; muscle growth
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