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Biosynthesis and Intracellular Targeting of the Lysosomal Aspartic Proteinase Cathepsin D

  • Chapter
Aspartic Proteinases

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 436))

Abstract

Lysosomal proteinases participate in cellular protein turnover and in the degradation of proteins which enter the cell by endocytosis. To serve this physiological role, a lysosomal enzyme must not only be synthesized with a functional catalytic site, it must move along a precise intracellular pathway to reach its site of action. Transport to lysosomes is not a default pathway but rather requires that biosynthetic forms of the lysosomal enzymes be recognized by specific intracellular processing enzymes and receptors in a complex sequence. If a lysosomal enzyme undergoes a mutation that prevents correct cellular target-ing, it will either be degraded or secreted from the cell. The resulting absence of a specific enzymatic activity within the lysosomes usually produces a fatal lysosomal storage disorder.

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Author information

Authors and Affiliations

  1. Department of Biochemistry and Biophysics, The University of North Carolina, Chapel Hill, North Carolina, 27599-7260, USA

    Gene D. Godbold, Kyujeong Ahn, Susan Yeyeodu & Ann H. Erickson

  2. Lineberger Comprehensive Cancer Center, The University of North Carolina, Chapel Hill, North Carolina, 27599-7260, USA

    Li-Fen Lee & Jenny P.-Y. Ting

Authors
  1. Gene D. Godbold
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  2. Kyujeong Ahn
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  3. Susan Yeyeodu
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  4. Li-Fen Lee
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  5. Jenny P.-Y. Ting
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  6. Ann H. Erickson
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Editors and Affiliations

  1. University of Alberta, Edmonton, Alberta, Canada

    Michael N. G. James

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© 1998 Springer Science+Business Media New York

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Godbold, G.D., Ahn, K., Yeyeodu, S., Lee, LF., Ting, J.PY., Erickson, A.H. (1998). Biosynthesis and Intracellular Targeting of the Lysosomal Aspartic Proteinase Cathepsin D. In: James, M.N.G. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 436. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5373-1_21

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  • DOI: https://doi.org/10.1007/978-1-4615-5373-1_21

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7452-7

  • Online ISBN: 978-1-4615-5373-1

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