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Proteases and proteolysis in the lysosome

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  • Proteases as Biological Regulators
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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.

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  1. Institute for Physiological Chemistry, University of Tübingen, D-7400, Tübingen, Germany

    P. Bohley

  2. Department of Tissue Culture, Institute for Cancer Research, The Norwegian Radium Hospital, Montebello, N-0310, Oslo 3, Norway

    P. O. Seglen

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Bohley, P., Seglen, P.O. Proteases and proteolysis in the lysosome. Experientia 48, 151–157 (1992). https://doi.org/10.1007/BF01923508

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