Abstract

The localization of reduced glutathione in skeletal muscle fibres of patients with inherited or acquired neuromuscular diseases and of subjects with no apparent disease of the neuromuscular system was studied histochemically. In healthy human skeletal muscle fibres, the level of reduced glutathione is higher in aerobic type I fibres than in anaerobic type II fibres. This finding suggests that glutathione in these healthy fibres is held in the reduced state chiefly by the activity of the decarboxylating and NADPH regenerating enzyme NADP(+)-dependent isocitrate dehydrogenase. In diseased muscle fibres, there is generally a positive relationship between the activity of the NADPH producing enzymes glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase and the level of reduced glutathione. This positive relationship suggests that glutathione in these diseased fibres is held in the reduced state chiefly by the activity of both enzymes of the pentose phosphate pathway.

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