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. 1970 May 1;45(2):321–333. doi: 10.1083/jcb.45.2.321

LYSOSOMES IN SKELETAL MUSCLE TISSUE

Zonal Centrifugation Evidence for Multiple Cellular Sources

Peter G Canonico 1, John W C Bird 1
PMCID: PMC2107900  PMID: 4327573

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, β-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, β-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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Selected References

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  1. Anderson N. G., Rutenberg E. Analytical techniques for cell fractions. VII. A simple gradient-forming apparatus. Anal Biochem. 1967 Nov;21(2):259–265. doi: 10.1016/0003-2697(67)90187-x. [DOI] [PubMed] [Google Scholar]
  2. Baggiolini M., Hirsch J. G., De Duve C. Resolution of granules from rabbit heterophil leukocytes into distinct populations by zonal sedimentation. J Cell Biol. 1969 Feb;40(2):529–541. doi: 10.1083/jcb.40.2.529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bird J. W., Berg T., Leathem J. H. Cathepsin activity of liver and muscle fractions of adrenalectomized rats. Proc Soc Exp Biol Med. 1968 Jan;127(1):182–188. doi: 10.3181/00379727-127-32651. [DOI] [PubMed] [Google Scholar]
  4. Bird J. W., Berg T., Milanesi A., Stauber W. T. Lysosomal enzymes in aquatic species. I. Distribution and particle properties of muscle lysosomes of the goldfish. Comp Biochem Physiol. 1969 Aug 1;30(3):457–468. doi: 10.1016/0010-406x(69)92015-5. [DOI] [PubMed] [Google Scholar]
  5. Bowers W. E., de Duve C. Lysosomes in lymphoid tissue. II. Intracellular distribution of acid hydrolases. J Cell Biol. 1967 Feb;32(2):339–348. doi: 10.1083/jcb.32.2.339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bowers W. E., de Duve C. Lysosomes in lymphoid tissue. III. Influence of various treatments of the animals on the distribution of acid hydrolases. J Cell Biol. 1967 Feb;32(2):349–364. doi: 10.1083/jcb.32.2.349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. COHN Z. A., WIENER E. THE PARTICULATE HYDROLASES OF MACROPHAGES. I. COMPARATIVE ENZYMOLOGY, ISOLATION, AND PROPERTIES. J Exp Med. 1963 Dec 1;118:991–1008. doi: 10.1084/jem.118.6.991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Canonico P. G., Bird J. W. The use of acridine orange as a lysosomal marker in rat skeletal muscle. J Cell Biol. 1969 Nov;43(2):367–371. doi: 10.1083/jcb.43.2.367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. DE DUVE C., PRESSMAN B. C., GIANETTO R., WATTIAUX R., APPELMANS F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem J. 1955 Aug;60(4):604–617. doi: 10.1042/bj0600604. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Deter R. L., De Duve C. Influence of glucagon, an inducer of cellular autophagy, on some physical properties of rat liver lysosomes. J Cell Biol. 1967 May;33(2):437–449. doi: 10.1083/jcb.33.2.437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. HOWES E. L., Jr, PRICE H. M., BLUMBERG J. M. THE EFFECTS OF A DIET PRODUCING LIPOCHROME PIGMENT (CEROID) ON THE ULTRASTRUCTURE OF SKELETAL MUSCLE IN THE RAT. Am J Pathol. 1964 Oct;45:599–631. [PMC free article] [PubMed] [Google Scholar]
  12. Heyde E., Morrison J. F. The interaction of Mg2+ and ATP4- with ATP: creatine phosphotransferase. Biochim Biophys Acta. 1969 Mar 18;178(1):47–60. doi: 10.1016/0005-2744(69)90130-2. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Maeir D. M., Zaiman H. The development of lysosomes in rat skeletal muscle in trichinous myositis. J Histochem Cytochem. 1966 May;14(5):396–400. doi: 10.1177/14.5.396. [DOI] [PubMed] [Google Scholar]
  15. NOVIKOFF A. B., ESSNER E., QUINTANA N. GOLGI APPARATUS AND LYSOSOMES. Fed Proc. 1964 Sep-Oct;23:1010–1022. [PubMed] [Google Scholar]
  16. Neil M. W., Horner M. W. Studies on acid hydrolases in adult and foetal tissues. Acid rho-nitrophenyl phosphate phosphohydrolases of adult guinea-pig liver. Biochem J. 1964 Jul;92(1):217–224. doi: 10.1042/bj0920217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Pollack M. S., Bird J. W. Distribution and particle properties of acid hydroase in denervated muscle. Am J Physiol. 1968 Sep;215(3):716–722. doi: 10.1152/ajplegacy.1968.215.3.716. [DOI] [PubMed] [Google Scholar]
  18. SHIBKO S., TAPPEL A. L. Acid phosphatase of the lysosomal and soluble fraction of rat liver. Biochim Biophys Acta. 1963 May 7;73:76–86. doi: 10.1016/0006-3002(63)90361-5. [DOI] [PubMed] [Google Scholar]
  19. SHIBKO S., TAPPEL A. L. RAT-KIDNEY LYSOSOMES: ISOLATION AND PROPERTIES. Biochem J. 1965 Jun;95:731–741. doi: 10.1042/bj0950731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SMITH B. HISTOLOGICAL AND HISTOCHEMICAL CHANGES IN THE MUSCLES OF RABBITS GIVEN THE CORTICOSTEROID TRIAMCINOLONE. Neurology. 1964 Sep;14:857–863. doi: 10.1212/wnl.14.9.857. [DOI] [PubMed] [Google Scholar]
  21. SWIFT H., HRUBAN Z. FOCAL DEGRADATION AS A BIOLOGICAL PROCESS. Fed Proc. 1964 Sep-Oct;23:1026–1037. [PubMed] [Google Scholar]
  22. Sellinger O. Z., Hiatt R. A. Cerebral lysosomes. IV. The regional and intracellular distribution of arylsulfatase and evidence for two populations of lysosomes in rat brain. Brain Res. 1968 Feb;7(2):191–200. doi: 10.1016/0006-8993(68)90097-8. [DOI] [PubMed] [Google Scholar]
  23. Stagni N., De Bernard B. Lysosomal enzyme activity in rat and beef skeletal muscle. Biochim Biophys Acta. 1968 Nov 12;170(1):129–139. doi: 10.1016/0304-4165(68)90167-0. [DOI] [PubMed] [Google Scholar]
  24. TAPPEL A. L., ZALKIN H., CALDWELL K. A., DESAI I. D., SHIBKO S. Increased lysosomal enzymes in genetic muscular dystrophy. Arch Biochem Biophys. 1962 Feb;96:340–346. doi: 10.1016/0003-9861(62)90418-6. [DOI] [PubMed] [Google Scholar]
  25. Van Vleet J. F., Hall B. V., Simon J. Vitamin E deficiency. A sequential light and electron microscopic study of skeletal muscle degeneration in weanling rabbits. Am J Pathol. 1968 May;52(5):1067–1079. [PMC free article] [PubMed] [Google Scholar]
  26. Wannemacher R. W., Jr, Banks W. L., Jr, Wunner W. H. Use of a single tissue extract to determine cellular protein and nucleic acid concentrations and rate of amino acid incorporation. Anal Biochem. 1965 May;11(2):320–326. doi: 10.1016/0003-2697(65)90020-5. [DOI] [PubMed] [Google Scholar]
  27. ZALKIN H., TAPPEL A. L., CALDWELL K. A., SHIBKO S., DESAI I. D., HOLLIDAY T. A. Increased lysosomal enzymes in muscular dystrophy of vitamin E-deficient rabbits. J Biol Chem. 1962 Aug;237:2678–2682. [PubMed] [Google Scholar]

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