The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Studies of the lamin proteinase reveal multiple parallel biochemical pathways during apoptotic execution.
Open accessAbstract
Although specific proteinases play a critical role in the active phase of apoptosis, their substrates are largely unknown. We previously identified poly(ADP-ribose) polymerase (PARP) as an apoptosis-associated substrate for proteinase(s) related to interleukin 1 beta-converting enzyme (ICE). Now we have used a cell-free system to characterize proteinase(s) that cleave the nuclear lamins during apoptosis. Lamin cleavage during apoptosis requires the action of a second ICE-like enyzme, which exhibits kinetics of cleavage and a profile of sensitivity to specific inhibitors that is distinct from the PARP proteinase. Thus, multiple ICE-like enzymes are required for apoptotic events in these cell-free extracts. Inhibition of the lamin proteinase with tosyllysine "chloromethyl ketone" blocks nuclear apoptosis prior to the packaging of condensed chromatin into apoptotic bodies. Under these conditions, the nuclear DNA is fully cleaved to a nucleosomal ladder. Our studies reveal that the lamin proteinase and the fragmentation nuclease function in independent parallel pathways during the final stages of apoptotic execution. Neither pathway alone is sufficient for completion of nuclear apoptosis. Instead, the various activities cooperate to drive the disassembly of the nucleus.
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Self-citationMechanisms and Functions of Cell Death
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Self-citationAltered Cytokine Export and Apoptosis in Mice Deficient in Interleukin-1β Converting Enzyme
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Cited by
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Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
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Self-citation
Metadata
- Authors
- Lazebnik, Y. A., Takahashi, A., Moir, R. D., Goldman, R. D., Poirier, G. G., Kaufmann, S. H., & Earnshaw, W. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1995-09-26
- Volume
- 92
- Issue
- 20
- Pages
- 9042-9046
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2085351407
- Cited by
- 512
- References
- 31
- FWCI
- 26.29
- Type
- journal article
- Language
- en
- Open access
- green
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