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Localization of Cathepsin D in Endosomes: Characterization and Biological Importance

  • Janice S. Blum
  • Maria L. Fiani
  • Philip D. Stahl
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 306)

Abstract

Proteases were initially identified in endosomes through studies of receptor-ligand transport.1 During receptor-mediated endocytosis, cell surface receptors bind exogenous ligands (Figure 1). These receptor-ligand complexes are internalized by clathrin-coated vesicles, which give rise to endosomes. Shortly after endosome formation, the internal pH of these vesicles drops to between pH 5–6.2 Many internalized receptor-ligand complexes dissociate upon endosome acidification, with the released receptors recycling back to the cell surface. Ligands delivered into endosomes undergo a variety of fates including transport back to the cell surface3 or sorting to different intracellular compartments such as lysosomes and the Golgi.4,5 Susceptible protein ligands are cleaved in endosomes indicating that these vesicles also serve as a processing compartment.1,6,8

Keywords

Cysteine Protease Lysosomal Enzyme Antigen Processing Aspartic Protease Endosome Acidification 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Janice S. Blum
    • 1
  • Maria L. Fiani
    • 2
  • Philip D. Stahl
    • 1
  1. 1.Department of Cell Biology and PhysiologyWashington University School of MedicineSaint LouisUSA
  2. 2.Laboratorio di Biologia CellularIstituto Superiore di SanitaRomeItaly

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