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Lysosomal Metabolism of Proteins

  • Chapter
Biology of the Lysosome

Part of the book series: Subcellular Biochemistry ((SCBI,volume 27))

Abstract

The lysosome is a major site of mammalian protein degradation and is calculated to be capable of degrading as much protein as the digestive tract (Barrett and Kirschke, 1981). Detailed characteristics are known for several of the enzymes involved in lysosomal proteolysis, although recent data suggest that the current catalog of enzymes involved in protein degradation is by no means complete. Although the enzymes are the necessary tools for hydrolysis, they are only effective in the right environment. In this chapter the relationship between the different enzymes and their environment is discussed, including mechanisms by which lysosomal proteolysis is controlled. Delivery of substrates to the lysosome, the pH in the lysosome, and removal of products from the lysosome are discussed in depth elsewhere in this volume (Chapters 3, 4, 5, 10, and 11), so discussion of these topics will be restricted to how they relate specifically to protein turnover. This chapter focuses on how the proteases function to hydrolyze proteins in the lysosome (for information on the pathological roles and the chemistry of the lysosomal proteases, see Lee and Marzella, 1994, and Mason and Wilcox, 1993).

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Authors and Affiliations

  1. Division of Developmental Biology, Nemours Research Programs, Wilmington, Delaware, 19899, USA

    Robert W. Mason

  2. Department of Pediatrics, Jefferson Medical College, Philadelphia, Pennsylvania, 19107, USA

    Robert W. Mason

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  1. Robert W. Mason
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Editors and Affiliations

  1. Thomas Jefferson University, Philadelphia, Pennsylvania, USA

    John B. Lloyd  & Robert W. Mason  & 

  2. Nemours Research Programs, Wilmington, Delaware, USA

    John B. Lloyd  & Robert W. Mason  & 

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© 1996 Springer Science+Business Media New York

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Mason, R.W. (1996). Lysosomal Metabolism of Proteins. In: Lloyd, J.B., Mason, R.W. (eds) Biology of the Lysosome. Subcellular Biochemistry, vol 27. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5833-0_6

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  • DOI: https://doi.org/10.1007/978-1-4615-5833-0_6

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