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Extensive Release. Excessive Storage

  • Chapter
Lysosomes

Part of the book series: Cellular Organelles ((CORG))

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Abstract

This chapter concerns important “exaggerations” of lysosomal function observed in specialized cell types or in particular developmental or pathological states. Cases will be considered in which the contents of lysosomes are released in quantity from cells or within cells, or in which lysosomal accumulations build up as a consequence of the failure of digestion.

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Further Reading

  • Barnes, D. M. (1987) Close encounters with an osteoclast, Science 236: 914–916.

    Article  PubMed  CAS  Google Scholar 

  • Baron, R., Neff, L., Louvard, D., and Courtoy, P. J. (1985) Cell mediated extracellular acidification and bone resorption: Evidence for a low pH in resorbing lacunae and localization of a 100kD lysosomal membrane protein in the osteoclast ruffled border, J. Cell Biol. 101: 2210–2222. (See also J. Cell Biol. 106: 1863-1872, 1988.)

    Article  PubMed  CAS  Google Scholar 

  • Barranger, J. A., and Brady, R. O. (eds.) (1984) Molecular Basis of Lysosomal Storage Disorders, Academic Press, New York.

    Google Scholar 

  • Baumbach, G. A., Saunders, D. T., Bazer, F. W., and Roberts, R. M. (1984) Uteroferrin has Nasparagine linked high mannose type oligosaccharides that contain mannose 6 phosphate, Proc. Natl. Acad. Sci. USA 81: 2985–2989.

    Article  PubMed  CAS  Google Scholar 

  • Bowen, I. D., and Lockshin, R. A. (eds.) (1981) Cell Death in Biology and Pathology, Chapman & Hall, London.

    Google Scholar 

  • Brands, R., Slot, J. W., and Geuze, H. J. (1982) Immunocytochemical localization of β-glucuronidase in the male rat preputial gland, Eur. J. Cell Biol. 27: 213–220.

    PubMed  CAS  Google Scholar 

  • Brown, J. A., Novack, E. K., and Swank, R. J. (1985) Effects of ammonia on processing and secretion of precursor and mature lysosomal enzymes from macrophages of normal and pale ear mice: Evidence for two distinct pathways, J. Cell Biol. 100: 1894–1904.

    Article  PubMed  CAS  Google Scholar 

  • Callahan, J. W., and Lowden, J. A. (eds.) (1981) Lysosomes and Lysosomal Storage Diseases, Raven Press, New York.

    Google Scholar 

  • Campbell, D. J. (1987) Circulating and tissue angiotensin systems, J. Clin. Invest. 79: 1–6.

    Article  PubMed  CAS  Google Scholar 

  • Davidson, H. W., Rhodes, C. J., and Hutton, J. C. (1988) Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic β-cell two distinct site-specific endopeptidases, Nature 333: 93–96.

    Article  PubMed  CAS  Google Scholar 

  • Davies, I., and Sigee, D. C. (eds.) (1984) Ageing and Cell Death, Cambridge University Press, London.

    Google Scholar 

  • Dean, M. F., and Diament, S. (1984) Exchange of lysosomal enzymes between cells, Biochem. Soc. Trans. 12: 524–526.

    CAS  Google Scholar 

  • Dean, R. T., and Stahl, P. (eds.) (1985) Developments in Cell Biology 1: Secretory Processes, Butterworths, London.

    Google Scholar 

  • de Hostos, E. L., Togasaki, R. K., and Grossman, R. (1988) Purification and biosynthesis of a derepressible aryl sulfatase from ChJamydomonas reinhardtii, J. Cell Biol. 106: 21–28.

    Google Scholar 

  • Dimond, R. L., Burns, R. A., and Jordan, K. B. (1981) Secretion of lysosomal enzymes in the cellular slime mold, Dictyostelium, J. Biol. Chem. 256: 6565–6572. (See also J. Cell Biol. 100: 1777-1787, 1985)

    PubMed  CAS  Google Scholar 

  • Docherty, K., Hutton, J. E., and Steiner, D. F. (1984) Cathepsin B-related proteases in the insulin secretory granule, J. Biol. Chem. 259: 6041–6044.

    PubMed  CAS  Google Scholar 

  • Faust, P. L., Chirgwin, J. M., and Kornfeld, S. (1987) Renin, a secretory glycoprotein. acquires phosphomannosyl residues, J. Cell Biol. 105: 1947–1956.

    Article  PubMed  CAS  Google Scholar 

  • Gainer, H., Russell, J. T., and Loh, Y. P. (1985) The enzymology and intracellular organization of peptide precursor processing: The secretory vesicle hypothesis, Neuroendocrinology 40: 171–184.

    Article  PubMed  CAS  Google Scholar 

  • Gal, S., and Gottesman, M. M. (1986) The major excreted protein of transformed fibroblasts is an activatable acid protease, J. Biol. Chem. 261: 1760–1765. (See also J. Biol. Chem. 263: 254, 1988 and J. Cell Biol. 106: 1879-1884, 1988.)

    PubMed  CAS  Google Scholar 

  • Ghosh, P. (1978) Lysosomal enzymes in joint disease, Aust. N.Z. J. Med. 8(suppl. 1): 12–15.

    Article  PubMed  Google Scholar 

  • Glew, R. H., Basu, A., Prence, E. M., and Remaley, A. T. (1985) Biology of disease: Lysosomal storage disease, Lab. Invest. 53: 250–269.

    PubMed  CAS  Google Scholar 

  • Glynn, L. E. (ed.) (1981) Tissue Repair and Regeneration, North-Holland, Amsterdam.

    Google Scholar 

  • Goldstein, P. (1987) Cytolytic T cell melodrama, Nature 327: 12.

    Article  Google Scholar 

  • Kane, A. B., Stanton, R. P., Raymond, E. G., Dobson, M. E., Knafele, M. E., and Farber, J. L. (1980) Dissociation of intracellular lysosomal rupture from the cell death caused by silica, J. Cell Biol. 87: 643–651.

    Article  PubMed  CAS  Google Scholar 

  • Kornberg, S., and Sly, W. S. (1985) Lysosomal storage defects, Hosp. Pract. 20(8): 71–82.

    Google Scholar 

  • Kuettner, K. E., Scheyerbach, R., and Hascall, V. C. (eds.) (1986) Articular Cell Biochemistry, Raven Press, New York.

    Google Scholar 

  • Lew, P. D., Monod, A., Waldvogel, F. A., Dewald, B., Baggiolini, M, and Pozzan, T. (1986) Quantitative analysis of the cytosolic free calcium dependency of exocytosis from three subcellular compartments in rabbit and human neutrophils, J. Cell Biol. 102: 2197–2204.

    Article  PubMed  CAS  Google Scholar 

  • Li, S-C., Sonnino, S., Tettamanti, G., and Li, Y-T. (1988) Characterization of a nonspecific activator protein for the enzymatic hydrolysis of glycolipids, J. Biol. Chem. 263: 6588–6591.

    PubMed  CAS  Google Scholar 

  • Neufeld, E. (1981) Recognition and processing of lysosomal enzymes in cultured fibroblasts, in Lysosomes and Lysosomal Storage Diseases (J. W. Callahan and J. A. Lowden, eds.), Raven Press, New York, pp. 115–130.

    Google Scholar 

  • Orci, L. (1987) Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying, clathrin coated secretory vesicles, Cell 49: 865–868.

    Article  PubMed  CAS  Google Scholar 

  • Paw, B. H., and Neufeld, E. F. (1988) Normal transcription of the β-hexosaminidase α-chain gene in the Ashkenazi Tay-Sachs mutation, J. Biol. Chem. 263: 3012–3018.

    PubMed  CAS  Google Scholar 

  • Scher, W. (1987) The role of extracellular proteases in cell proliferation and differentiation, Lab. Invest. 57: 607–623.

    PubMed  CAS  Google Scholar 

  • Silver, I. A., Murrib, R. J., and Etherington, D. J. (1988) Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts, Exp. Cell Res. 175: 266–276.

    Article  PubMed  CAS  Google Scholar 

  • Spring-Mills, E., and Hafez, E. S. E. (eds.) (1980) Male Accessory Sex Glands, Elsevier, Amsterdam.

    Google Scholar 

  • Stanbury, J. B., Wyngaarden, J. B., Frederickson, D. S., Goldstein, J. L., and Brown, M. S. (eds.) (1983) The Metabolic Basis of Inherited Disease (5th ed.), McGraw-Hill, New York.

    Google Scholar 

  • Tager, J. M. (1985) Biosynthesis and deficiency of lysosomal enzymes, Trends Biochem. Sci. 10: 324–326.

    Article  CAS  Google Scholar 

  • Takemura, R., and Werb, Z. (1984) Secretory products of macrophages and their physiological functions, Am. J. Physiol. 246: C1–C9. [See also Werb, Z. (1987) In Basic and Clinical Immunology (6th ed.) (D. P. Sittes, J. D. Stobo, and J. V. Wells, eds.), Appleton & Lange, Los Angeles.]

    PubMed  CAS  Google Scholar 

  • Taugner, R., Buhrle, C. P., Nobiling, R., and Kirschke, H. (1985) Coexistence of renin and cathepsin B in epitheloid cell secretory granules, Histochemistry 83: 103–108. (See also Cell Tissue Res. 239: 575-587, 1985.)

    Article  PubMed  CAS  Google Scholar 

  • Tiedke, A., Hunster, P., Florin-Christensen, J., and Florin-Christensen, M. (1988) Exocytosis, endocytosis and membrane cycling in Tetrahymena thermophila, J. Cell Sci. 89: 515–520.

    Google Scholar 

  • Travis, J., and Salvsen, G. S. (1983) Human plasma proteinase inhibitors, Annu. Rev. Biochem. 52: 655–709.

    Article  PubMed  CAS  Google Scholar 

  • Tsuchiya, M., Perez-Tamayo, R. Okazaki, I., and Maruyama, K. (eds.) (1982) Collagen Degradation and MammaJian Collagenases, Excerpta Medica, Amsterdam.

    Google Scholar 

  • Vaes, G. (1980) Collagenase, lysosomes and osteoclastic bone resorption, in Collagenases in Normal and Pathological Connective Tissues (D. E. Wooley and J. M. Evanson, eds.), Wiley, New York, 185–207.

    Google Scholar 

  • Van Golde, L. M. G., Batenberg, J. J., and Robertson, B. (1988) The pulmonary surfactant system: Biochemical aspects and functional significance, Physiol. Rev. 68: 374–455.

    PubMed  Google Scholar 

  • Wassarman, P. M. (1987) The biology and chemistry of fertilization, Science 235: 553–564.

    Article  PubMed  CAS  Google Scholar 

  • Watts, R. W. E., and Gibbs, D. A. (1986) Lysosomal Storage Diseases, Taylor & Francis, London.

    Google Scholar 

  • Wood, L., and Kaplan A. (1985) Transit of α-mannosidase during its maturation in Dictyostelium discoideum, J. Cell Biol. 101: 2063–2069.

    Article  PubMed  CAS  Google Scholar 

  • Williams, M. C. (1984) Endocytosis in alveolar type II cells: Effects of change and size of tracer, Proc. Natl. Acad. Sci. USA 81: 6054–6058.

    Article  PubMed  CAS  Google Scholar 

  • Wright, S. D., and Silverstein, S. C. (1984) Phagocytosing macrophages exclude proteins from the zone of contact with opsonized targets, Nature 309: 259–261.

    Google Scholar 

  • Young, J. D. E., and Chon, Z. A. (1986) Cell mediated killing: A common mechanism? Cell 46: 641–642. (See also J. Exp. Med. 166: 1894, 1987.)

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Columbia University, New York, New York, USA

    Eric Holtzman

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  1. Eric Holtzman
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© 1989 Springer Science+Business Media New York

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Holtzman, E. (1989). Extensive Release. Excessive Storage. In: Lysosomes. Cellular Organelles. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2540-4_6

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  • DOI: https://doi.org/10.1007/978-1-4899-2540-4_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-306-43126-5

  • Online ISBN: 978-1-4899-2540-4

  • eBook Packages: Springer Book Archive

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