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Title:
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The Absence of Oligonucleosomal DNA Fragmentation during Apoptosis of IMR-5 Neuroblastoma Cells
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Author:
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Yuste Mateos, Víctor J. (Víctor José); Bayascas Ramírez, José Ramón; Llecha Cano, Núria; Sánchez-López, Isabel; Boix Torras, Jacint; Comella i Carnicé, Joan Xavier
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Notes:
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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.
This work was supported by Proyectos FEDER Grant 1FD97-0514- 002-01 and Plan Nacional Salud y Farmacia Grant SAF 2000-0164-002-01) from the Spanish Government and grants from Telemarató de TV3 (Edició 1999) and Generalitat de Catalunya |
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Rights:
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(c) The American Society for Biochemistry and Molecular Biology, Inc., 2001
info:eu-repo/semantics/restrictedAccess |
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Document type:
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article
publishedVersion |
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Published by:
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American Society for Biochemistry and Molecular Biology
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