Cited by 403Cell death mechanisms and regulationAutophagy in Disease and TherapyProtease and Inhibitor Mechanisms

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Cysteine Cathepsins Trigger Caspase-dependent Cell Death through Cleavage of Bid and Antiapoptotic Bcl-2 Homologues

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Droga-Mazovec, Gabriela, Bojič, Lea, Petelin, Ana, Ivanova, Saška, Romih, Rok, Repnik, Urska, Salvesen, Guy S., Stoka, Veronika, Turk, Vito, Turk, Boris·2008·Journal of Biological Chemistry

DOI 10.1074/jbc.m802513200

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Abstract

As a model for defining the role of lysosomal cathepsins in apoptosis, we characterized the action of the lysosomotropic agent LeuLeuOMe using distinct cellular models. LeuLeuOMe induces lysosomal membrane permeabilization, resulting in release of lysosomal cathepsins that cleave the proapoptotic Bcl-2 family member Bid and degrade the antiapoptotic member Bcl-2, Bcl-xL, or Mcl-1. The papain-like cysteine protease inhibitor E-64d largely prevented apoptosis, Bid cleavage, and Bcl-2/Bcl-xL/Mcl-1 degradation. The pancaspase inhibitor N-benzyloxycarbonyl-Val-Ala-Asp(OMe)fluoromethyl ketone failed to prevent Bid cleavage and degradation of anti-apoptotic Bcl-2 homologues but substantially decreased cell death, suggesting that cathepsin-mediated apoptosis in these cellular models mostly follows a caspase-dependent pathway. Moreover, in vitro experiments showed that one or more of the cysteine cathepsins B, L, S, K, and H could cleave Bcl-2, Bcl-xL, Mcl-1, Bak, and BimEL, whereas no Bax cleavage was observed. On the basis of inhibitor studies, we demonstrate that lysosomal disruption triggered by LeuLeuOMe occurs before mitochondrial damage. We propose that degradation of anti-apoptotic Bcl-2 family members by lysosomal cathepsins synergizes with cathepsin-mediated activation of Bid to trigger a mitochondrial pathway to apoptosis. Moreover, XIAP (X-chromosome-linked inhibitor of apoptosis) was also found to be a target of cysteine cathepsins, suggesting that cathepsins can mediate caspase-dependent apoptosis also downstream of mitochondria.

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Authors: Droga-Mazovec, G., Bojič, L., Petelin, A., Ivanova, S., Romih, R., Repnik, U., Salvesen, G. S., Stoka, V., Turk, V., & Turk, B.
Affiliations: Jožef Stefan Institute (SI)
University of Ljubljana (SI)
Sanford Burnham Prebys Medical Discovery Institute (US)
Corresponding author: Turk, Boris
ORCID: Petelin, Ana
Ivanova, Saška
Romih, Rok
Salvesen, Guy S.
Stoka, Veronika
Turk, Boris
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2008-07
Volume: 283
Issue: 27
Pages: 19140-19150
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m802513200
OpenAlex: W2006193439
Cited by: 399
References: 67
Citations by year: 2026: 13 · 2025: 17 · 2024: 21 · 2023: 21 · 2022: 22 · 2021: 22 · 2020: 23 · 2019: 23 · 2018: 26 · 2017: 22 · 2016: 22 · 2015: 20 · 2014: 24 · 2013: 27 · 2012: 26
FWCI: 9.59
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4483 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords: cysteine cathepsins, lysosomal cathepsins, apoptosis, Bid cleavage, Bcl-2 family proteins, Bcl-xL, Mcl-1, Bax, BimEL, Bak, lysosomal membrane permeabilization, E64d, XIAP, mitochondrial apoptosis, caspase-dependent cell death, lysosomal disruption
MeSH terms: Bcl-2-Like Protein 11, Cathepsins, Humans, Lysosomes, Membrane Proteins, Mitochondria, Protease Inhibitors, Proto-Oncogene Proteins, Apoptosis, Caco-2 Cells, Proto-Oncogene Proteins c-bcl-2, bcl-2 Homologous Antagonist-Killer Protein, Apoptosis Regulatory Proteins, bcl-X Protein, BH3 Interacting Domain Death Agonist Protein, X-Linked Inhibitor of Apoptosis Protein, Myeloid Cell Leukemia Sequence 1 Protein

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Cysteine Cathepsins Trigger Caspase-dependent Cell Death through Cleavage of Bid and Antiapoptotic Bcl-2 Homologues

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