The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity
Open accessAbstract
Through direct interaction with the voltage-dependent anion channel (VDAC), proapoptotic Bcl-2 family members such as Bax and Bak induce apoptogenic mitochondrial cytochrome c release and membrane potential (Δψ) loss in isolated mitochondria. Using isolated mitochondria, we showed that Bid and Bik, BH3-only proteins from the Bcl-2 family, induced cytochrome c release but not Δψ loss. Unlike Bax/Bak, the cytochrome c release induced by Bid/Bik was Ca 2+-independent, cyclosporin A-insensitive, and respiration-independent. Furthermore, in contrast to Bax/Bak, Bid/Bik neither interacted with VDAC nor directly affected the VDAC activity in liposomes. Consistently, Bid/Bik induced apoptosis without Δψ loss, whereas Bax induced apoptosis with Δψ loss. These findings indicated the involvement of a different mechanism in BH3-only, protein-induced apoptogenic cytochrome c release.
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Cites
Molecular characterization of mitochondrial apoptosis-inducing factor
Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060
Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81589-5 · Cited by 3,626
Two CD95 (APO‐1/Fas) signaling pathways
Scaffidi, C., Fulda, S., Srinivasan, A., Friesen, C., Li, F., Tomaselli, K. J., Debatin, K., Krammer, P. H., & Peter, M. E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1675 · Cited by 3,000
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
Self-citationBax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis
Marzo, I., Brenner, C., Zamzami, N., Jürgensmeier, J. M., Susin, S. A., Vieira, H. L. A., Prévost, M.-C., Xie, Z., Matsuyama, S., Reed, J. C., et al. (1998) · Science · doi:10.1126/science.281.5385.2027 · Cited by 1,168
Banki, K., Hutter, E., Gonchoroff, N. J., & Perl, A. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.3.1466 · Cited by 276
Cited by
A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072
Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
Zhang, J., & Ney, P. A. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2009.16 · Cited by 1,021
The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet
van Loo, G., Saelens, X., van Gurp, M., MacFarlane, M., Martin, S. J., & Vandenabeele, P. (2002) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401088 · Cited by 665
Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario
Chipuk, J. E., Bouchier-Hayes, L., & Green, D. R. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401963 · Cited by 631
Caspase-2 Induces Apoptosis by Releasing Proapoptotic Proteins from Mitochondria
Guo, Y., Srinivasula, S. M., Druilhe, A., Fernandes-Alnemri, T., & Alnemri, E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108029200 · Cited by 521
Metadata
- Authors
- Shimizu, S., & Tsujimoto, Y.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-01-18
- Volume
- 97
- Issue
- 2
- Pages
- 577-582
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2081690888
- Cited by
- 273
- References
- 6
- FWCI
- 14.64
- Type
- journal article
- Language
- en
- Open access
- green
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- Shimizu, S., & Tsujimoto, Y. (2000). Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.2.577
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