Early biochemical consequences of denervation in fast and slow skeletal muscles and their relationship to neural control over muscle differentiation.
1. One week after denervation several biochemical characteristics of the fast extensor digitorum longus and slow soleus muscles from adult rats were investigated and compared with the characteristics of the corresponding unoperated contralateral muscles. 2. After these short periods of denervation-induced atrophy, the isolated myosins showed unchanged ATPase (adenosine triphosphatase) activities, but there was the expected difference between fast and slow muscle. 3. The specific activities of several soluble enzymes and their characteristic patterns were found to be only slightly modified in both the extensor and soleus muscles after denervation, as were most of the activities measured in the isolated mitochondria. 4. The most significant modifications were in the isolated sarcoplasmic reticulum, and appeared to be specific to either slow or fast muscle. 5. Denervation of slow muscle led to a marked increase of Ca(2+)-transport rates, and of the specific activity of the Mg(2+)-activated K(+)-modulated Ca(2+)-stimulated ATPase, together with changes in the polyacrylamide-electrophoretic profiles of the microsomal membrane protein. Transformation of these several properties of slow muscle sarcoplasmic reticulum to those of fast muscle sarcoplasmic reticulum was further substantiated by electron-microscopic analysis after negative staining. Control experiments with tenotomized soleus muscle gave negative results. 6. The isolated sarcoplasmic reticulum from fast muscle showed a slight diminution of ATPase-linked Ca(2+)-transport activity and a selective increase of rotenone-insensitive NADH-cytochrome c reductase activity, in addition to a greater emphasis on slow-type electrophoretic components of the structural membrane protein. 7. The significance of these results in relation to specific differentiating influences from motor nerves is discussed.
D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D001693:Biological Transport, Active; D002118:Calcium; D004586:Electrophoresis; D066298:In Vitro Techniques; D008274:Magnesium; D008297:Male; D008854:Microscopy, Electron; D008861:Microsomes; D008931:Mitochondria, Muscle / Q000201:enzymology; D009121:Muscle Denervation; D009132:Muscles / Q000201:enzymology*; D009218:Myosins / Q000032:analysis; D011188:Potassium; D051381:Rats; D012519:Sarcoplasmic Reticulum / Q000201:enzymology
D000251:Adenosine Triphosphatases; D009218:Myosins; D008274:Magnesium; D011188:Potassium; D002118:Calcium