The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A tumor suppressor function for caspase-2
Open accessAbstract
Apoptosis is mediated by the caspase family of proteases that act as effectors of cell death by cleaving many cellular substrates. Caspase-2 is one of the most evolutionarily conserved caspases, yet its physiological function has remained enigmatic because caspase-2-deficient mice develop normally and are viable. We report here that the caspase-2 −/− mouse embryonic fibroblasts (MEFs) show increased proliferation. When transformed with E1A and Ras oncogenes, caspase-2 −/− MEFs grew significantly faster than caspase-2 +/+ MEFs and formed more aggressive and accelerated tumors in nude mice. To assess whether the loss of caspase-2 predisposes animals to tumor development, we used the mouse Eμ- Myc lymphoma model. Our findings suggest that loss of even a single allele of caspase-2 resulted in accelerated tumorigenesis, and this was further enhanced in caspase-2 −/− mice. The caspase-2 −/− cells showed resistance to apoptosis induced by chemotherapeutic drugs and DNA damage. Furthermore, caspase-2 −/− MEFs had a defective apoptotic response to cell-cycle checkpoint regulation and showed abnormal cycling following γ-irradiation. These data show that loss of caspase-2 results in an increased ability of cells to acquire a transformed phenotype and become malignant, indicating that caspase-2 is a tumor suppressor protein.
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Cites
Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,218 · cited 2×
“When transformed with E1A and Ras oncogenes, caspase-2 / MEFs grew significantly faster than caspase-2 / MEFs and formed more aggressive and accelerated tumors in nude mice.”
MethodDanial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
BH3-only Bcl-2 family member Bim is required for apoptosis of autoreactive thymocytes
Bouillet, P., Purton, J. F., Godfrey, D. I., Zhang, L.-C., Coultas, L., Puthalakath, H., Pellegrini, M., Cory, S., Adams, J. M., & Strasser, A. (2002) · Nature · doi:10.1038/415922a · Cited by 782
Self-citation
Cited by
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-citationCaspase Functions in Cell Death and Disease
McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,594
Old, new and emerging functions of caspases
Shalini, S., Dorstyn, L., Dawar, S., & Kumar, S. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.216 · Cited by 1,267
Self-citationMitotic catastrophe: a mechanism for avoiding genomic instability
Vitale, I., Galluzzi, L., Castedo, M., & Kroemer, G. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3115 · Cited by 834
Targeting apoptotic caspases in cancer
Boice, A., & Bouchier-Hayes, L. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118688 · Cited by 391
Metadata
- Authors
- Ho, L. H., Taylor, R., Dorstyn, L., Cakouros, D., Bouillet, P., & Kumar, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-03-31
- Volume
- 106
- Issue
- 13
- Pages
- 5336-5341
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1993572137
- Cited by
- 167
- References
- 3
- FWCI
- 6.00
- Type
- journal article
- Language
- en
- Open access
- green
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- Ho, L. H., Taylor, R., Dorstyn, L., Cakouros, D., Bouillet, P., & Kumar, S. (2009). A tumor suppressor function for caspase-2. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0811928106
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