Skeletal muscle lysosomes: comparison of lysosomes from normal and dystrophic avian pectoralis muscle as a function of age.
The properties of skeletal muscle lysosomes from normal and dystrophic chickens were studied to assess their involvement in the dystrophic process. A method is described for isolation of a three-to-sevenfold purified lysosome fraction with 29-33% yield. Lysosomal enzymes in crude homogenates and isolated lysosome-enriched fractions from dystrophic muscle exhibit decreased latency for N-acetyl beta-D-glucosaminidase, acid phosphatase, and cathepsin D. However, no differences in the fragility of lysosomes in isolated lysosome-enriched fractions from normal and dystrophic muscle were observed using shear, sonication and detergent stress. Lower percent recovery, enrichment factor and percent latency of acid phosphatase compared to N-acetyl-beta-D-glucosaminidase and cathepsin D were observed from both normal and dystrophic muscle. These results are consistent with the presence of a significant amount of nonlysosomal acid phosphatase activity in skeletal muscle.
D000118:Acetylglucosaminidase / Q000378:metabolism; D000135:Acid Phosphatase / Q000378:metabolism; D000375:Aging; D000818:Animals; D002402:Cathepsin D; D002403:Cathepsins / Q000378:metabolism; D002645:Chickens; D008247:Lysosomes / Q000502:physiology*; D009132:Muscles / Q000201:enzymology*; D009137:Muscular Dystrophy, Animal / Q000201:enzymology*; D010369:Pectoralis Muscles / Q000201:enzymology; D011201:Poultry Diseases / Q000201:enzymology
D000135:Acid Phosphatase; D000118:Acetylglucosaminidase; D002403:Cathepsins; D002402:Cathepsin D