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PMID: 1740187 Published · ppublish English Journal Article Review

Proteases and proteolysis in the lysosome.

Experientia ·Vol. 48 ·No. 2 ·1992-02-15 ·Pages 151-7

Bohley P, Seglen PO

Abstract

Proteins sequestered by a non-selective bulk process within the lysosomes turn over with an apparent half-life of about 8 minutes and this rapid lysosomal proteolysis is initiated by endopeptidases, in particular by the cathepsins D and L. We describe also the cathepsins B and H which show mainly exopeptidase and only low endopeptidase activity. Especially cathepsin H is most probably the only lysosomal aminopeptidase in many cell types. Additionally, the properties of other mammalian lysosomal endo- and exopeptidases are compared. Finally, we discuss some of the conditions for the action of lysosomal proteases as the low intralysosomal pH, the high part of lysosomal thiol groups and the absence of intralysosomal proteinase inhibitors.

MeSH Terms
Animals Cathepsins/metabolism Endopeptidases/metabolism Lysosomes/enzymology Proteins/metabolism
Chemicals
Proteins Cathepsins Endopeptidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bohley P
Institute for Physiological Chemistry, University of Tübingen, Germany.
Seglen P O
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Article Info
Journal
Experientia
Abbr.
Experientia
ISSN
0014-4754
Published
1992-02-15
Pages
151-7
Language
English
Region
Switzerland
NLM ID
0376547
Subset
IM
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