PMID: 4327573May 1, 1970

Lysosomes in skeletal muscle tissue. Zonal centrifugation evidence for multiple cellular sources

The Journal of Cell Biology
P G Canonico, J W Bird

Abstract

Postnuclear supernates from homogenates of skeletal muscle from rats subjected to starvation, injections of Triton WR-1339, dextran-500, and dextran + corticosterone were fractionated by means of rate and isopycnic zonal centrifugation in sucrose-0.02 M KCl gradients. Zonal fractions were analyzed for protein, RNA, cytochrome oxidase, and up to six acid hydrolases. The results indicate the presence of two groups of lysosome-like particles. One group contributes approximately 95% of the cathepsin D and acid phosphatase activity and 75% of the acid ribonuclease, beta-glucuronidase, and arylsulfatase activity in muscle. It is characterized by a modal equilibrium density of 1.18 that is decreased by starvation, but is not shifted by dextran-500 or Triton WR-1339. The second group has a higher proportion of acid ribonuclease, beta-glucuronidase, and arylsulftase; the equilibrium density can be shifted by dextran-500 and Triton WR-1339. It is suggested that this group of lysosomes is derived from macrophages and other connective tissue cells, whereas the former group represents lysosome-like particles from muscle cells.

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Citations

Nov 1, 1969·The Journal of Cell Biology·P G Canonico, J W Bird
Nov 1, 1967·Analytical Biochemistry·N G Anderson, E Rutenberg
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Related Concepts

Corticosterone Assay
Acid Phosphatase
Cytochrome C Oxidase
Cytochrome c Oxidase Subunit VIa
Lysosome Assembly Pathway
Study, Methodological
Muscle Cells
Gene Products, Protein
Beta-glucuronidase
Tissue Extracts

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