Regulation of glycogenolysis in human skeletal muscle

JM Ren, E Hultman - Journal of Applied Physiology, 1989 - journals.physiology.org
JM Ren, E Hultman
Journal of Applied Physiology, 1989journals.physiology.org
The role of inorganic phosphate on the regulation of glycogenolysis in resting and
contracting muscle was studied in human quadriceps muscle. Increased Pi content was
achieved by intermittent electrical stimulation of the muscle followed by occlusion of the
blood flow. Occlusion resulted in the maintenance of a high Pi content over a 60-s
observation period during which the muscle was either at rest or was stimulated electrically.
The study was performed with and without infusion of epinephrine (EPI). In the absence of …
The role of inorganic phosphate on the regulation of glycogenolysis in resting and contracting muscle was studied in human quadriceps muscle. Increased Pi content was achieved by intermittent electrical stimulation of the muscle followed by occlusion of the blood flow. Occlusion resulted in the maintenance of a high Pi content over a 60-s observation period during which the muscle was either at rest or was stimulated electrically. The study was performed with and without infusion of epinephrine (EPI). In the absence of EPI the phosphorylase a fraction was 50% immediately at the end of the initial stimulation period, declining to 22% after 60 s. With EPI corresponding values for phosphorylase a were 91% initially, 56% after 30 s, and 33% after 60 s, respectively. In both cases the Pi content was increased by approximately 35 mmol/kg dry muscle during the stimulation and remained constant during the occlusion. In neither of these situations was significant degradation of glycogen observed during the occlusion. In the study performed with electrical stimulation during the occlusion period, muscle glycogen degradation was observed both with and without EPI. Phosphorylase a fractions and Pi contents in this study were similar to those observed when muscle was rested over the 60-s occlusion period. The paradox of a high Pi content and extensive transformation of phosphorylase to the a form but low glycogenolytic activity points to additional factors in the regulation of glycogen breakdown.
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