The Absence of Oligonucleosomal DNA Fragmentation during Apoptosis of IMR-5 Neuroblastoma Cells
Issue date
2001Author
Yuste Mateos, Víctor J. (Víctor José)
Bayascas Ramírez, José Ramón
Llecha Cano, Núria
Sánchez-López, Isabel
Comella i Carnicé, Joan Xavier
Suggested citation
Yuste Mateos, Víctor J. (Víctor José);
Bayascas Ramírez, José Ramón;
Llecha Cano, Núria;
Sánchez-López, Isabel;
Boix Torras, Jacint;
Comella i Carnicé, Joan Xavier;
.
(2001)
.
The Absence of Oligonucleosomal DNA Fragmentation during Apoptosis of IMR-5 Neuroblastoma Cells.
Journal of Biological Chemistry, 2001, vol. 276, núm. 25, p. 22323-22331.
https://doi.org/10.1074/jbc.M100072200.
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Show full item recordAbstract
Caspase-activated DNase is responsible for the oligonucleosomal
DNA degradation during apoptosis. DNA
degradation is thought to be important for multicellular
organisms to prevent oncogenic transformation or as a
mechanism of viral defense. It has been reported that
certain cells, including some neuroblastoma cell lines
such as IMR-5, enter apoptosis without digesting DNA in
such a way. We have analyzed the causes for the absence
of DNA laddering in staurosporine-treated IMR-5 cells,
and we have found that most of the molecular mechanisms
controlling apoptosis are well preserved in this
cell line. These include degradation of substrates for
caspases, blockade of cell death by antiapoptotic genes
such as Bcl-2 or Bcl-XL, or normal levels and adequate
activation of caspase-3. Moreover, these cells display
normal levels of caspase-activated DNase and its inhibitory
protein, inhibitor of caspase-activated DNase, and
their cDNA sequences are identical to those reported
previously. Nevertheless, IMR-5 cells lose caspase-activated
DNase during apoptosis and recover their ability
to degrade DNA when human recombinant caspase-activated
DNase is overexpressed. Our results lead to the
conclusion that caspase-activated DNase is processed
during apoptosis of IMR-5 cells, making these cells a
good model to study the relevance of this endonuclease
in physiological or pathological conditions.
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Journal of Biological Chemistry, 2001, vol. 276, núm. 25, p. 22323-22331European research projects
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