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Division of Pulmonary/Critical Care Medicine, Department of Medicine, The Burns and Allen Research Institute, Cedars-Sinai Medical Center, and the University of California Los Angeles School of Medicine, Los Angeles, California 90048
The aim of this study was to evaluate the
cellular response of the diaphragm, extensor digitorum longus (EDL),
and soleus (Sol) muscles to clinically relevant doses of cyclosporine
administered to male rats over 4 wk. Control rats were
provided with vehicle only. Muscle fiber types, cross-sectional areas,
indexes of capillarity, and succinate dehydrogenase (SDH) activity were
determined by quantitative histochemistry. Myosin heavy chain isoforms
were identified by SDS-PAGE, and their proportions were measured by scanning densitometry. Serum cyclosporine level, 20-24 h after the
last dose of cyclosporine, was 145 ± 81 ng/ml. Final body weight
and muscle mass were similar between the cyclosporine and control
groups. In the diaphragm, EDL, and Sol, no differences were observed
between the groups with regard to fiber type proportions, fiber
cross-sectional areas, and proportions of myosin heavy chain isoforms.
In the EDL, reductions, both in SDH activity in type I, IIx, and IIb
fibers (
26 to 37%) and in indexes of capillarity (18
to 37%), were noted. In the Sol, SDH activity and capillarity were
similar between the groups. In the diaphragm of cyclosporine-treated rats, there was significant reduction in the number of capillaries around individual fibers (5%), whereas levels of SDH activity tended to be lower. This suggests that activation history may in part
determine muscle-specific responses to cyclosporine. We speculate that
reduced oxidative activity and capillarity of some limb muscles
contribute to reduced exercise capacity and the "deconditioned state" observed in patients receiving cyclosporine after successful solid-organ transplantation.
immunosuppressive agents; mitochondria; microcirculation; solid-organ transplantation; aerobic capacity; quantitative histochemistry; myosin heavy chain isoforms
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