Journal of Applied Physiology AJP: Endocrinology and Metabolism
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J Appl Physiol 68: 2369-2372, 1990;
8750-7587/90 $5.00
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Journal of Applied Physiology, Vol 68, Issue 6 2369-2372, Copyright © 1990 by American Physiological Society


ARTICLES

Is hypoxia a stimulus for synthesis of oxidative enzymes and myoglobin?

N. Terrados, E. Jansson, C. Sylven and L. Kaijser
Department of Clinical Physiology, Karolinska Hospital, Stockholm, Sweden.

To compare two situations with similar magnitudes of mitochondrial substrate flux but different blood oxygen contents, one-legged training was employed. Ten healthy subjects trained one leg under normobaric conditions and the other under hypobaric conditions. At each session the subjects trained each leg for 30 min. The absolute work intensity was the same for both legs and was chosen to correspond to 65% of the average (right and left) pretraining one-legged maximal work capacity. There were three to four training sessions per week for 4 wk. Muscle biopsies from each leg were taken before and after training and analyzed for fiber types, capillaries, myoglobin, and oxidative and glycolytic enzymes. The most striking finding was a greater increase of citrate synthase activity under hypobaric conditions than under normobaric conditions. In addition, the myoglobin content increased in the leg trained under hypobaric conditions, whereas it tended to decrease in the normobarically trained leg. Because both legs were trained at the same intensity, the oxygen turnover and the substrate flux through the carboxylic acid cycle and the respiratory chain must have been of similar magnitude. Thus a difference in substrate flux is less likely to have caused the differences in enzyme activities and myoglobin content between training under normobaric and hypobaric conditions. Instead, the stimulus seems to be related to the blood oxygen content or tension.


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