Adaptations in metabolic capacity of rat soleus after paralysis.
To determine whether long-term reductions in neuromuscular activity result in alterations in metabolic capacity, the activities of oxidative, i.e., succinate dehydrogenase (SDH) and citrate synthase (CS), and glycolytic, i.e., alpha-glycerophosphate dehydrogenase (GPD), enzyme markers were quantified in rat soleus muscles 1, 3, and 6 mo after a complete spinal cord transection (ST). In addition, the proportional content of lactate dehydrogenase (LDH) isozymes was used as a marker for oxidative and glycolytic capacities. The myosin heavy chain (MHC) isoform content of a fiber served as a marker of phenotype. In general, MHC isoforms shifted from MHC1 toward MHC2, particularly MHC2x, after ST. Mean SDH and CS activities were higher in ST than control at all time points. The elevated SDH and CS activities were indicative of an enhanced oxidative capacity. GPD activities were higher in ST than control rats at all time points. The increase in activity of SDH was larger than GPD. Thus the GPD-to-SDH (glycolytic-to-oxidative) ratio was decreased after ST. Compared with controls, total LDH activity increased transiently, and the LDH isozyme profile shifted from LDH-1 toward LDH-5, indicative of an enhanced glycolytic capacity. Combined, these results indicate that 1) the metabolic capacities of soleus fibers were not compromised, but the interrelationships among oxidative and glycolytic capacity and MHC content were apparently dissociated after ST; 2) enhancements in oxidative and glycolytic enzyme activities are not mutually exclusive; and 3) chronic reductions in skeletal muscle activity do not necessarily result in a reduced oxidative capacity.
Otis
Jeffrey S
JS
Muscle Function Laboratory, Virginia Polytechnic Institute and State University, Blacksburg 24061, USA.
Roy
Roland R
RR
Edgerton
V Reggie
VR
Talmadge
Robert J
RJ
D000222:Adaptation, Physiological / Q000502:physiology*; D000818:Animals; D002950:Citrate (si)-Synthase / Q000378:metabolism; D005260:Female; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D006019:Glycolysis / Q000502:physiology; D018763:Muscle Fatigue / Q000502:physiology; D018656:Muscle Fibers, Fast-Twitch / Q000201:enzymology; D018657:Muscle Fibers, Slow-Twitch / Q000201:enzymology; D018482:Muscle, Skeletal / Q000166:cytology / Q000378:metabolism*; D018995:Myosin Heavy Chains / Q000378:metabolism; D010085:Oxidative Phosphorylation; D010243:Paralysis / Q000378:metabolism* / Q000503:physiopathology*; D051381:Rats; D017207:Rats, Sprague-Dawley; D013385:Succinate Dehydrogenase / Q000378:metabolism
D005993:Glycerolphosphate Dehydrogenase; D013385:Succinate Dehydrogenase; D002950:Citrate (si)-Synthase; D018995:Myosin Heavy Chains