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Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome
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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“Accordingly, blocking post-mitochondrial caspase activation by genetic means or with specific pharmacological inhibitors, such as to N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethylketone (Z-VAD-fmk) and (3S)-5-(2,6-difluorophenoxy)-3-[[(2S)-3-methyl-1-oxo-2-[(2-quinolinylcarbonyl)amino]butyl]amino]-4-oxo-pentanoic acid hydrate (Q-VD-OPh), generally delays (but does not prevent) intrinsic apopt”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [225]
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Cites
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 9,051
Hengartner, M. O. (2000) · Nature · doi:10.1038/35037710 · Cited by 5,779
The Bcl2 family: regulators of the cellular life-or-death switch
Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032
Self-citationIdentification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
Nicholson, D. W., Ali, A., Thornberry, N. A., Vaillancourt, J. P., Ding, C. K., Gallant, M., Gareau, Y., Griffin, P. R., Labelle, M., Lazebnik, Y. A., et al. (1995) · Nature · doi:10.1038/376037a0 · Cited by 3,980
Self-citationBCL-2 family members and the mitochondria in apoptosisPreprint
Gross, A., McDonnell, J. M., & Korsmeyer, S. J. (1999) · Genes & Development · doi:10.1101/gad.13.15.1899 · Cited by 3,642
A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., & Nagata, S. (1998) · Nature · doi:10.1038/34112 · Cited by 3,239
(2001) · PubMed · Cited by 2,381
Liu, X., Zou, H., Slaughter, C. A., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80197-x · Cited by 1,835
Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9
Kuida, K., Haydar, T. F., Kuan, C.-Y., Gu, Y., Taya, C., Karasuyama, H., Su, M. S.-S., Rakic, P., & Flavell, R. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81476-2 · Cited by 1,643
Self-citationBouillet, P., Metcalf, D., Huang, D. C. S., Tarlinton, D. M., Kay, T. W. H., Köntgen, F., Adams, J. M., & Strasser, A. (1999) · Science · doi:10.1126/science.286.5445.1735 · Cited by 1,504
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Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Self-citationThe BCL-2 protein family: opposing activities that mediate cell death
Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,806
Self-citationDanial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
Regulation of apoptosis in health and disease: the balancing act of BCL-2 family proteins
Singh, R., Letai, A., & Sarosiek, K. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0089-8 · Cited by 2,111
The Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987
The Bcl-2 family: roles in cell survival and oncogenesis
Cory, S., Huang, D. C. S., & Adams, J. M. (2003) · Oncogene · doi:10.1038/sj.onc.1207102 · Cited by 1,474
Self-citationFridman, J. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1207116 · Cited by 1,401
How does p53 induce apoptosis and how does this relate to p53-mediated tumour suppression
Aubrey, B. J., Kelly, G. L., Janic, A., Herold, M. J., & Strasser, A. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.169 · Cited by 1,395
Self-citationCytochrome C -Mediated Apoptosis
Jiang, X., & Wang, X. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073706 · Cited by 1,374
Caspases 3 and 7: Key Mediators of Mitochondrial Events of Apoptosis
Lakhani, S. A., Masud, A. J., Kuida, K., Porter, G. A., Jr., Booth, C. J., Mehal, W. Z., Inayat, I., & Flavell, R. A. (2006) · Science · doi:10.1126/science.1115035 · Cited by 1,175
Self-citationHaupt, S., Berger, M., Goldberg, Z., & Haupt, Y. (2003) · Journal of Cell Science · doi:10.1242/jcs.00739 · Cited by 1,136
Degterev, A., Boyce, M., & Yuan, J. (2003) · Oncogene · doi:10.1038/sj.onc.1207107 · Cited by 1,146
Toxic proteins released from mitochondria in cell death
Saelens, X., Festjens, N., Walle, L. V., van Gurp, M., Loo, G., & Vandenabeele, P. (2004) · Oncogene · doi:10.1038/sj.onc.1207523 · Cited by 1,021
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White, M. J., McArthur, K., Metcalf, D., Lane, R. M., Cambier, J. C., Herold, M. J., van Delft, M. F., Bedoui, S., Lessene, G., Ritchie, M. E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.036 · Cited by 983
“In contrast, Apaf-1- or caspase-deficient cells exhibit only short-term resistance to apoptotic stimuli and do not retain clonogenic potential (Ekert et al., 2004; Marsden et al., 2002; van Delft et al., 2010).”
Self-citationCaspase function in programmed cell death
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Death receptor-induced cell killing
Thorburn, A. M. (2003) · Cellular Signalling · doi:10.1016/j.cellsig.2003.08.007 · Cited by 787
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Adams, J. M. (2003) · Genes & Development · doi:10.1101/gad.1126903 · Cited by 789
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Self-citationBoehning, D. F., Patterson, R. L., Sedaghat, L., Glebova, N. O., Kurosaki, T., & Snyder, S. H. (2003) · Nature Cell Biology · doi:10.1038/ncb1063 · Cited by 636
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Strasser, A. (2005) · Nature reviews. Immunology · doi:10.1038/nri1568 · Cited by 642
Self-citationBax and Bak can localize to the endoplasmic reticulum to initiate apoptosis
Zong, W., Li, C., Hatzivassiliou, G., Lindsten, T., Yu, Q., Yuan, J., & Thompson, C. B. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302084 · Cited by 611
Roca, H., Varsos, Z. S., Sud, S., Craig, M. J., Chi, Y., & Pienta, K. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.042671 · Cited by 587
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Vila, M., & Przedborski, S. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1100 · Cited by 566
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Strasser, A., Cory, S., & Adams, J. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.307 · Cited by 543
Self-citationApoptosis in the development and maintenance of the immune system
Opferman, J. T., & Korsmeyer, S. J. (2003) · Nature Immunology · doi:10.1038/ni0503-410 · Cited by 544
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Hori, M., & Nishida, K. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn335 · Cited by 531
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Debatin, K., & Krammer, P. H. (2004) · Oncogene · doi:10.1038/sj.onc.1207558 · Cited by 505
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Ren, D., Tu, H.-C., Kim, H., Wang, G. X., Bean, G. R., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H. Y. (2010) · Science · doi:10.1126/science.1190217 · Cited by 472
Olsson, M., & Zhivotovsky, B. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.30 · Cited by 419
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Bras, M., Queenan, B., & Susín, S. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0105-4 · Cited by 412
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Boya, P., Gonzalez-Polo, R.-A., Poncet, D., Andreau, K., Vieira, H. L., Roumier, T., Perfettini, J.-L., & Kroemer, G. (2003) · Oncogene · doi:10.1038/sj.onc.1206622 · Cited by 385
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Marsden, V. S., & Strasser, A. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.141029 · Cited by 390
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Self-citationApoptosome dysfunction in human cancer
Hajra, K. M., & Liu, J. R. (2004) · APOPTOSIS · doi:10.1023/b:appt.0000045786.98031.1d · Cited by 291
Hao, Z., Duncan, G. S., Chang, C., Elia, A., Fang, M., Wakeham, A. C., Okada, H., Calzascia, T., Jang, Y., You-Ten, A. J., et al. (2005) · Cell · doi:10.1016/j.cell.2005.03.016 · Cited by 281
Role of Caspases in Ox-LDL–Induced Apoptotic Cascade in Human Coronary Artery Endothelial Cells
Chen, J., Mehta, J. L., Haider, N., Zhang, X., Narula, J., & Li, D. (2003) · Circulation Research · doi:10.1161/01.res.0000113782.07824.be · Cited by 272
McComb, S., Chan, P. K., Guinot, A., Hartmannsdottir, H., Jenni, S., Dobay, M. P., Bourquin, J., & Bornhauser, B. C. (2019) · Science Advances · doi:10.1126/sciadv.aau9433 · Cited by 269
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Self-citationASC is a Bax adaptor and regulates the p53–Bax mitochondrial apoptosis pathway
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Zhang, G.-S., Wang, Y., Zhang, Y., Wan, X., Li, J., Liu, K., Wang, F., Liu, Q., Yang, C., Yu, P., et al. (2012) · Current Molecular Medicine · doi:10.2174/156652412798889063 · Cited by 173
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Simpson, D. S., Pang, J., Weir, A. L., Kong, I. Y., Fritsch, M., Rashidi, M., Cooney, J. P., Davidson, K. C., Speir, M., Djajawi, T. M., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.01.003 · Cited by 146
Self-citationApoptosis in cancer—implications for therapy
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Troy, C. M., & Shelanski, M. L. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401175 · Cited by 128
Li, Y., Wang, J., Xiao, H., Xiao, C., Wang, Y., & Liu, X. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.09.022 · Cited by 127
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Wilson-Annan, J., O’Reilly, L. A., Crawford, S., Hausmann, G., Beaumont, J. G., Parma, L. P., Chen, L., Lackmann, M., Lithgow, T. J., Hinds, M. G., et al. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302144 · Cited by 118
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Metadata
- 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
- Venue
- Nature
- Published
- 2002-09-25
- Volume
- 419
- Issue
- 6907
- Pages
- 634-637
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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