The Depressive Effect of Pi on the Force-pCa Relationship in Skinned Single Muscle Fibers Is Temperature Dependent

Document Type




Format of Original

10 p.

Publication Date



American Physiological Society

Source Publication

American Journal of Physiology - Cell Physiology

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Increases in Pi combined with decreases in myoplasmic Ca2+ are believed to cause a significant portion of the decrease in muscular force during fatigue. To investigate this further, we determined the effect of 30 mM Pion the force-Ca2+ relationship of chemically skinned single muscle fibers at near-physiological temperature (30°C). Fibers isolated from rat soleus (slow) and gastrocnemius (fast) muscle were subjected to a series of solutions with an increasing free Ca2+ concentration in the presence and absence of 30 mM Piat both low (15°C) and high (30°C) temperature. In slow fibers, 30 mM Pi significantly increased the Ca2+ required to elicit measurable force, referred to as the activation threshold at both low and high temperatures; however, the effect was twofold greater at the higher temperature. In fast fibers, the activation threshold was unaffected by elevating Pi at 15°C but was significantly increased at 30°C. At both low and high temperatures, 30 mM Pi increased the Ca2+ required to elicit half-maximal force (pCa50) in both slow and fast fibers, with the effect of Pi twofold greater at the higher temperature. These data suggest that during fatigue, reductions in the myoplasmic Ca2+ and increases in Pi act synergistically to reduce muscular force. Consequently, the combined changes in these ions likely account for a greater portion of fatigue than previously predicted based on studies at lower temperatures or high temperatures at saturating Ca2+ levels.


American Journal of Physiology - Cell Physiology, Volume 29, (November 2005): C1041-C1050. DOI.