Caspase activation in response to cytotoxic Rana catesbeiana ribonuclease in MCF‐7 cells

Rana catesbeiana ribonuclease (RC‐RNase) and onconase were proven to own anti‐tumor activity. While molecular determinants of onconase‐induced cell death have become more explicit, the RC‐RNase‐induced death pathway remains presently unknown. Here we demonstrated that RC‐RNase‐induced molecular casc...

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Bibliographic Details
Published in:FEBS letters 2001-08, Vol.503 (1), p.65-68
Main Authors: Hu, Chih-Chi Andrew, Tang, Chih-Hang Anthony, Wang, Jaang-Jiun
Format: Article
Language:English
Subjects:
Amphibian Proteins
Animals
Antineoplastic Agents - isolation & purification
Antineoplastic Agents - pharmacology
Apoptosis
bcl-X Protein
Bcl-XL
Caspase
Caspases - metabolism
CpG, cytidylyl(3′→5′)guanosine
Endoribonucleases - isolation & purification
Endoribonucleases - pharmacology
Enzyme Activation
Female
Humans
MCF-7
Onconase
PARP, poly(ADP-ribose) polymerase
Proto-Oncogene Proteins c-bcl-2 - metabolism
Rana catesbeiana
Rana catesbeiana ribonuclease
RC-RNase, Rana catesbeiana ribonuclease
Ribonucleases - metabolism
Tumor Cells, Cultured
XTT, sodium 3′-[1-(phenylaminocarbonyl)-3,4-tetrazolium]-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate
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Summary:Rana catesbeiana ribonuclease (RC‐RNase) and onconase were proven to own anti‐tumor activity. While molecular determinants of onconase‐induced cell death have become more explicit, the RC‐RNase‐induced death pathway remains presently unknown. Here we demonstrated that RC‐RNase‐induced molecular cascades in caspase‐3‐deficient MCF‐7 cells did not include activation of initiation caspase‐8 and ‐9. Cleavage timing suggested that procaspase‐2 and ‐6 might be processed by active caspase‐7 in MCF‐7 cells. Caspase‐7 was also responsible for cleavage of the poly(ADP‐ribose) polymerase. Furthermore, we reported that overexpression of Bcl‐XL could raise the survival rates of MCF‐7 cells treated with RC‐RNase and onconase.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(01)02691-6