The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death.
Open accessAbstract
Proteolysis mediated by the interleukin 1 beta-converting enzyme (ICE) homologues is an important mechanism of the apoptotic process. The ICE homologue apopain/CPP-32/Yama (subsequently referred to as apopain) cleaves poly(ADP-ribose)polymerase (PARP) early during apoptosis. Additional apoptosis-specific protein cleavages have been observed in which the direct involvement of ICE-like proteases has been postulated. These substrates include the 70-kD protein component of the U1-ribonucleoprotein (U1-70kD), and the catalytic subunit of the DNA-dependent protein kinase (DNA-PKcs). The present studies demonstrate that U1-70kD and DNA-PKcs are excellent substrates for apopain, with cleavage occurring at sites that are highly similar to the cleavage site within PARP. The fragments generated from isolated protein substrates by apopain are identical to those observed in intact apoptotic cells, in apoptotic cell extracts, and in normal cell extracts to which apopain has been added. Like PARP, cleavage of these substrates in apoptotic cell extracts is abolished by nanomolar concentrations of Ac-DEVD-CHO and micromolar amounts of Ac-YVAD-CHO, confirming the involvement of apopain or an apopain-like activity. We propose that a central function of apopain or similar homologues in apoptosis is the cleavage of nuclear repair proteins, thereby abolishing their critical homeostatic functions.
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Cites
A Single Ataxia Telangiectasia Gene with a Product Similar to PI-3 Kinase
Savitsky, K., Bar-Shira, A., Gilad, S., Rotman, G., Ziv, Y., Vanagaite, L., Tagle, D. A., Smith, S., Uziel, T., Sfez, S., et al. (1995) · Science · doi:10.1126/science.7792600 · Cited by 2,785
Cited by
Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,911
Caspases: the executioners of apoptosis
COHEN, G. M. (1997) · Biochemical Journal · doi:10.1042/bj3260001 · Cited by 4,719
Mammalian Caspases: Structure, Activation, Substrates, and Functions During Apoptosis
Earnshaw, W. C., Martins, L. M., & Kaufmann, S. H. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.383 · Cited by 2,760
A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B
Thornberry, N. A., Rano, T. A., Peterson, E. P., Rasper, D. M., Timkey, T., Garcia-Calvo, M., Houtzager, V. M., Nordstrom, P. A., Roy, S., Vaillancourt, J. P., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.29.17907 · Cited by 2,068
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Metadata
- Authors
- Casciola-Rosen, L., Nicholson, D. W., Chong, T., Rowan, K. R., Thornberry, N. A., Miller, D. K., & Rosen, A.
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1996-05-01
- Volume
- 183
- Issue
- 5
- Pages
- 1957-1964
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- OpenAlex
- W2100915449
- Cited by
- 613
- References
- 1
- FWCI
- 30.18
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Casciola-Rosen, L., Nicholson, D. W., Chong, T., Rowan, K. R., Thornberry, N. A., Miller, D. K., & Rosen, A. (1996). Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death. The Journal of experimental medicine. https://doi.org/10.1084/jem.183.5.1957
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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