The intrinsic activating factors that induce transcription of heat shock protein 72 (HSP72) in skeletal muscle following exercise remain unclear. We hypothesized that the cytosolic Ca2+ transient that occurs with depolarization is a determinant. We utilized intact, single skeletal muscle fibers from Xenopus laevis to test the role of the cytosolic Ca2+ transient and several other exercise-related factors (fatigue, hypoxia, AMP kinase, and cross-bridge cycling) on the activation of HSP72 transcription. HSP72 and HSP60 mRNA levels were assessed with real-Time quantitative PCR; cytosolic Ca2+ concentration ([Ca2+]cyt) was assessed with fura-2. Both fatiguing and nonfatiguing contractions resulted in a significant increase in HSP72 mRNA. As expected, peak [Ca2+]cyt remained tightly coupled with peak developed tension in contracting fibers. Pretreatment with N-benzyl-ptoluene sulfonamide (BTS) resulted in depressed peak developed tension with stimulation, while peak [Ca2+]cyt remained largely unchanged from control values. Despite excitation-contraction uncoupling, BTS-Treated fibers displayed a significant increase in HSP72 mRNA. Treatment of fibers with hypoxia (PO2: <3 mmHg) or AMP kinase activation had no effect on HSP72 mRNA levels. These results suggest that the intermittent cytosolic Ca2+ transient that occurs with skeletal muscle depolarization provides a sufficient activating stimulus for HSP72 transcription. Metabolic or mechanical factors associated with fatigue development and cross-bridge cycling likely play a more limited role.
CITATION STYLE
Stary, C. M., & Hogan, M. C. (2016). Cytosolic calcium transients are a determinant of contraction-induced HSP72 transcription in single skeletal muscle fibers. Journal of Applied Physiology, 120(10), 1260–1266. https://doi.org/10.1152/japplphysiol.01060.2015
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