Document Detail


UV-induced apoptosis is mediated independent of caspase-9 in MCF-7 cells: a model for cytochrome c resistance.
MedLine Citation:
PMID:  12954616     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The importance of the mitochondria in UV-induced apoptosis has become increasingly apparent. Following DNA damage cytochrome c and other pro-apoptotic factors are released from the mitochondria, allowing for formation of the apoptosome and subsequent cleavage and activation of caspase-9. Active caspase-9 then activates downstream caspases-3 and/or -7, which in turn cleave poly(ADP)-ribose polymerase (PARP) and other down-stream targets, resulting in apoptosis. In an effort to understand the mechanisms of Akt-mediated cell survival in breast cancer, we studied the effects of insulin-like growth factor (IGF)-I treatment on UV-treated MCF-7 human breast cancer cells. Apoptosis was induced in MCF-7 cells after UV treatment, as measured by caspase-7 and PARP cleavage, and IGF-I co-treatment protected against this response. Surprisingly caspase-9 cleavage was unchanged with UV and/or IGF-I treatment. Using MCF-7 cells overexpressing caspase-3 we have shown that resistance of caspase-9 to cleavage was not altered by the expression of caspase-3. Furthermore, overexpression of caspase-9 did not enhance PARP or caspase-7 cleavage after UV treatment. Because caspase-8 was activated with UV treatment alone, we believe that UV-induced apoptosis in MCF-7 cells occurs independently of cytochrome c and caspase-9, supporting the existence of a cytoplasmic inhibitor of cytochrome c in MCF-7 cells. We anticipate that such inhibitors may be overexpressed in cancer cells, allowing for treatment resistance.
Authors:
Heather A Ferguson; Peter M Marietta; Carla L Van Den Berg
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.     Date:  2003-09-03
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  278     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2003 Nov 
Date Detail:
Created Date:  2003-11-10     Completed Date:  2003-12-24     Revised Date:  2008-05-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  45793-800     Citation Subset:  IM    
Affiliation:
School of Pharmacy, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA.
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MeSH Terms
Descriptor/Qualifier:
1-Phosphatidylinositol 3-Kinase / metabolism
Apoptosis*
Blotting, Western
Breast Neoplasms / metabolism
Caspase 3
Caspase 7
Caspase 9
Caspases / metabolism,  physiology*
Cell Line
Cell Line, Tumor
Cell Survival
Cytochromes c / metabolism*
Enzyme Activation
Humans
Insulin-Like Growth Factor I / metabolism
Microscopy, Fluorescence
Poly(ADP-ribose) Polymerases / metabolism
Precipitin Tests
Proteins / metabolism
Proto-Oncogene Proteins c-bcl-2 / metabolism
RNA / metabolism
Time Factors
Transfection
Ultraviolet Rays
X-Linked Inhibitor of Apoptosis Protein
Grant Support
ID/Acronym/Agency:
CA89288A/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Proteins; 0/Proto-Oncogene Proteins c-bcl-2; 0/X-Linked Inhibitor of Apoptosis Protein; 0/XIAP protein, human; 63231-63-0/RNA; 67763-96-6/Insulin-Like Growth Factor I; 9007-43-6/Cytochromes c; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/CASP7 protein, human; EC 3.4.22.-/CASP9 protein, human; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspase 7; EC 3.4.22.-/Caspase 9; EC 3.4.22.-/Caspases

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