Increased response to insulin of glucose metabolism in the 6-day unloaded rat soleus muscle.
Hind leg muscles of female rats (85-99 g) were unloaded by tail cast suspension for 6 days. In the fresh-frozen unloaded soleus, the significantly greater concentration of glycogen correlated with a lower activity ratio of glycogen phosphorylase (p less than 0.02). The activity ratio of glycogen synthase also was lower (p less than 0.001), possibly due to the higher concentration of glycogen. In isolated unloaded soleus, insulin (0.1 milliunit/ml) increased the oxidation of D-[U-14C]glucose, release of lactate and pyruvate, incorporation of D-[U-14C]glucose into glycogen, and the concentration of glucose 6-phosphate more (p less than 0.05) than in the weight-bearing soleus. At physiological doses of insulin, the percent of maximal uptake of 2-deoxy-D-[1,2-3H]glucose/muscle also was greater in the unloaded soleus. Unloading of the soleus increased by 50% the concentration of insulin receptors, due to no decrease in total receptor number during muscle atrophy. This increase may account for the greater response of glucose metabolism to insulin in this muscle. The extensor digitorum longus, which generally shows little response to unloading, displayed no differential response of glucose metabolism to insulin.
D000818:Animals; D002250:Carbon Radioisotopes; D005260:Female; D005947:Glucose / Q000378:metabolism*; D006006:Glycogen Synthase / Q000378:metabolism; D007328:Insulin / Q000494:pharmacology*; D007700:Kinetics; D009132:Muscles / Q000187:drug effects / Q000378:metabolism* / Q000502:physiology; D006005:Phosphorylases / Q000378:metabolism; D005082:Physical Exertion; D051381:Rats; D011919:Rats, Inbred Strains
D002250:Carbon Radioisotopes; D007328:Insulin; D006005:Phosphorylases; D006006:Glycogen Synthase; D005947:Glucose