Cited by 579Cell death mechanisms and regulationCancer-related Molecular PathwaysFlavonoids in Medical Research

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Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome

Marsden, Vanessa S., O'Connor, Liam, O'Reilly, Lorraine A., Silke, John, Metcalf, Donald, Ekert, Paul G., Huang, David C. S., Cecconi, Francesco, Kuida, Keisuke, Tomaselli, Kevin J., Roy, Sophie, Nicholson, Don W., Vaux, David L., Bouillet, Philippe, Adams, Jerry M., Strasser, Andreas·2002·Nature

DOI 10.1038/nature01101

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Abstract

Apoptosis is an evolutionarily conserved cell suicide process executed by cysteine proteases (caspases) and regulated by the opposing factions of the Bcl-2 protein family. Mammalian caspase-9 and its activator Apaf-1 were thought to be essential, because mice lacking either of them display neuronal hyperplasia and their lymphocytes and fibroblasts seem resistant to certain apoptotic stimuli. Because Apaf-1 requires cytochrome c to activate caspase-9, and Bcl-2 prevents mitochondrial cytochrome c release, Bcl-2 is widely believed to inhibit apoptosis by safeguarding mitochondrial membrane integrity. Our results suggest a different, broader role, because Bcl-2 overexpression increased lymphocyte numbers in mice and inhibited many apoptotic stimuli, but the absence of Apaf-1 or caspase-9 did not. Caspase activity was still discernible in cells lacking Apaf-1 or caspase-9, and a potent caspase antagonist both inhibited apoptosis and retarded cytochrome c release. We conclude that Bcl-2 regulates a caspase activation programme independently of the cytochrome c/Apaf-1/caspase-9 'apoptosome', which seems to amplify rather than initiate the caspase cascade.

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Authors: Marsden, V. S., O'Connor, L., O'Reilly, L. A., Silke, J., Metcalf, D., Ekert, P. G., Huang, D. C. S., Cecconi, F., Kuida, K., Tomaselli, K. J., Roy, S., Nicholson, D. W., Vaux, D. L., Bouillet, P., Adams, J. M., & Strasser, A.
Affiliations: Walter and Eliza Hall Institute of Medical Research (AU)
University of Rome Tor Vergata (IT)
Vertex Pharmaceuticals (United States) (US)
Merck Canada Inc. (Canada) (CA)
Corresponding author: Strasser, Andreas
ORCID: Silke, John
Ekert, Paul G.
Huang, David C. S.
Cecconi, Francesco
Kuida, Keisuke
Vaux, David L.
Bouillet, Philippe
Adams, Jerry M.
Strasser, Andreas
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2002-09-25
Volume: 419
Issue: 6907
Pages: 634-637
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature01101
OpenAlex: W1978093163
Cited by: 578
References: 30
Citations by year: 2026: 13 · 2025: 7 · 2024: 17 · 2023: 13 · 2022: 14 · 2021: 22 · 2020: 13 · 2019: 17 · 2018: 18 · 2017: 26 · 2016: 24 · 2015: 18 · 2014: 24 · 2013: 15 · 2012: 20
FWCI: 21.90
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Health Sciences › Medicine › Pharmacology (medical) › Flavonoids in Medical Research
Keywords: apoptosis, Bcl-2, caspase activation, caspase-9, Apaf-1, cytochrome c release, apoptosome, Bcl-2 family proteins, lymphocyte proliferation, mitochondrial membrane integrity
MeSH terms: Animals, B-Lymphocytes, Cells, Cultured, Cytochrome c Group, Enzyme Activation, Hematopoiesis, Mice, Inbred C57BL, Proteins, T-Lymphocytes, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Caspases, Mice, Caspase 9, Apoptotic Protease-Activating Factor 1

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Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome

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