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Human skinned muscle fibers were used to investigate the effects of bovine serum albumin (BSA) on the tension/pCa relationship and on the functional properties of the Ca(2+)-release channel of the sarcoplasmic reticulum (SR). In both fast- and slow-type fibers, identified by their tension response to pSr 5.0, BSA (0.7-15 microM) had no effect on the Ca2+ affinity of the contractile proteins and elicited no tension per se in Ca(2+)-loaded fibers. In contrast, BSA (&gt; 1.0 microM) potentiated the caffeine-induced tension in Ca(2+)-loaded fibers, this effect being more intense in slow-type fibers. Thus, BSA reduced the threshold caffeine concentration required for eliciting detectable tension, and increased the amplitude, the rate of rise and the area under the curve of caffeine-induced tension. BSA also potentiated the tension elicited in Ca(2+)-loaded fibers by low-Mg2+ solutions containing 1.0 mM free ATP. These results suggest that BSA modulates the response of the human skeletal muscle SR Ca(2+)-release channel to activators such as caffeine and ATP.

Bovine serum albumin potentiates caffeine- or ATP-induced tension in human skinned skeletal muscle fibers