J Cell Biol. 1970 May 1; 45(2):
321–333. Article Zonal Centrifugation Evidence for Multiple Cellular Sources 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. The Full Text of this article is available as a
PDF (886K).Abstract
Full Text
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Anderson NG, Rutenberg E. Analytical techniques for cell fractions. VII. A simple gradient-forming apparatus. Anal Biochem. 1967 Nov;21(2):259–265. [PubMed] [Google Scholar]
- Baggiolini M, Hirsch JG, 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. [PMC free article] [PubMed] [Google Scholar]
- Bird JW, Berg T, Leathem JH. Cathepsin activity of liver and muscle fractions of adrenalectomized rats. Proc Soc Exp Biol Med. 1968 Jan;127(1):182–188. [PubMed] [Google Scholar]
- Bird JW, Berg T, Milanesi A, Stauber WT. 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. [PubMed] [Google Scholar]
- Bowers WE, de Duve C. Lysosomes in lymphoid tissue. II. Intracellular distribution of acid hydrolases. J Cell Biol. 1967 Feb;32(2):339–348. [PMC free article] [PubMed] [Google Scholar]
- Bowers WE, 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. [PMC free article] [PubMed] [Google Scholar]
- Canonico PG, Bird JW. The use of acridine orange as a lysosomal marker in rat skeletal muscle. J Cell Biol. 1969 Nov;43(2):367–371. [PMC free article] [PubMed] [Google Scholar]
- COHN ZA, WIENER E. THE PARTICULATE HYDROLASES OF MACROPHAGES. I. COMPARATIVE ENZYMOLOGY, ISOLATION, AND PROPERTIES. J Exp Med. 1963 Dec 1;118:991–1008. [PMC free article] [PubMed] [Google Scholar]
- DE DUVE C, PRESSMAN BC, 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. [PMC free article] [PubMed] [Google Scholar]
- Deter RL, 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. [PMC free article] [PubMed] [Google Scholar]
- HOWES EL, Jr, PRICE HM, BLUMBERG JM. 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]
- LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Maeir DM, Zaiman H. The development of lysosomes in rat skeletal muscle in trichinous myositis. J Histochem Cytochem. 1966 May;14(5):396–400. [PubMed] [Google Scholar]
- Neil MW, Horner MW. 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. [PMC free article] [PubMed] [Google Scholar]
- NOVIKOFF AB, ESSNER E, QUINTANA N. GOLGI APPARATUS AND LYSOSOMES. Fed Proc. 1964 Sep-Oct;23:1010–1022. [PubMed] [Google Scholar]
- Pollack MS, Bird JW. Distribution and particle properties of acid hydroase in denervated muscle. Am J Physiol. 1968 Sep;215(3):716–722. [PubMed] [Google Scholar]
- Heyde E, Morrison JF. The interaction of Mg2+ and ATP4- with ATP: creatine phosphotransferase. Biochim Biophys Acta. 1969 Mar 18;178(1):47–60. [PubMed] [Google Scholar]
- Sellinger OZ, Hiatt RA. 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. [PubMed] [Google Scholar]
- SHIBKO S, TAPPEL AL. Acid phosphatase of the lysosomal and soluble fraction of rat liver. Biochim Biophys Acta. 1963 May 7;73:76–86. [PubMed] [Google Scholar]
- SHIBKO S, TAPPEL AL. RAT-KIDNEY LYSOSOMES: ISOLATION AND PROPERTIES. Biochem J. 1965 Jun;95:731–741. [PMC free article] [PubMed] [Google Scholar]
- SMITH B. HISTOLOGICAL AND HISTOCHEMICAL CHANGES IN THE MUSCLES OF RABBITS GIVEN THE CORTICOSTEROID TRIAMCINOLONE. Neurology. 1964 Sep;14:857–863. [PubMed] [Google Scholar]
- Stagni N, De Bernard B. Lysosomal enzyme activity in rat and beef skeletal muscle. Biochim Biophys Acta. 1968 Nov 12;170(1):129–139. [PubMed] [Google Scholar]
- SWIFT H, HRUBAN Z. FOCAL DEGRADATION AS A BIOLOGICAL PROCESS. Fed Proc. 1964 Sep-Oct;23:1026–1037. [PubMed] [Google Scholar]
- TAPPEL AL, ZALKIN H, CALDWELL KA, DESAI ID, SHIBKO S. Increased lysosomal enzymes in genetic muscular dystrophy. Arch Biochem Biophys. 1962 Feb;96:340–346. [PubMed] [Google Scholar]
- Van Vleet JF, Hall BV, 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]
- Wannemacher RW, Jr, Banks WL, Jr, Wunner WH. 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. [PubMed] [Google Scholar]
- ZALKIN H, TAPPEL AL, CALDWELL KA, SHIBKO S, DESAI ID, HOLLIDAY TA. Increased lysosomal enzymes in muscular dystrophy of vitamin E-deficient rabbits. J Biol Chem. 1962 Aug;237:2678–2682. [PubMed] [Google Scholar]
Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press