Ultrastructural localization of acid phosphatase in denervated and diabetic striated muscles.
Catabolism in denervated and diabetic rat skeletal muscle undergoing accelerated protein degradation has been investigated with methods for demonstrating acid phosphatase ultrastructurally. Control muscles displayed strong acid phosphatase activity in lateral sacs and in sparse secondary hysosomes distributed mainly near nuclear poles. Muscles from diabetic rats and, to a lesser extent, 2-day denervated rats, revealed increased secondary lysosomes apparently derived from fusion of mitochondria with acid-phosphatase-reactive vesicles and cisternae. The latter were interpreted as possibly originating from T tubules. Reaction product was also noted in the junctional folds of the motor end plate of a denervated muscle. At the longer post denervation intervals studied, deposits indicative of acid phosphatase were dispersed throughout the sarcoplasm with greater concentration in the I band and appeared more abundant in denervated than in contralateral control muscles. The enzymatic basis for the sarcoplasmic deposits and other deposits was confirmed by their absence from cytochemical controls, which included incubation in substrate-free medium, heat or NaF inactivation of enzyme, and exposure sequentially to PbNO3 and NaH2PO or PbNO3 and beta-glycerophosphate.
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D006651:Histocytochemistry; D008297:Male; D009045:Motor Endplate / Q000201:enzymology; D009121:Muscle Denervation; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000201:enzymology / Q000648:ultrastructure*; D051381:Rats
D009124:Muscle Proteins; D000135:Acid Phosphatase