| Caspase-3 inhibits the growth of breast cancer cells independent of protease activity. | |
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MedLine Citation:
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PMID: 15316934 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In this study, the MCF-7 breast cancer cells that lack caspase-3 were transfected with a wild type (WT) or mutant caspase-3 cDNA. Expression of the WT, but not of the mutant, caspase-3 was associated with increased caspase activity and susceptibility to staurosporine (STS)-induced apoptosis. Both derivatives displayed inhibition of cell growth compared with vector control cells. Growth inhibition was associated with increased expression of the cyclin dependent kinase (CDK) inhibitor p27Kip1 in the WT, but not in the mutant caspase-3 expressing cells. Cyclin D1 expression level was not affected by caspase-3 expression. Phosphorylation of the Akt protein was decreased in both WT and mutant caspase transfected cells, although Akt expression level remained unchanged. These results suggest that caspase-3 might have biological functions independent of its protease activity and that its loss might contribute to tumor development by increasing the growth potential of cancer cells. |
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Authors:
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Beatrice Faraglia; Alessia Bonsignore; Franco Scaldaferri; Alma Boninsegna; Achille Cittadini; Cesare Mancuso; Alessandro Sgambato |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of cellular physiology Volume: 202 ISSN: 0021-9541 ISO Abbreviation: J. Cell. Physiol. Publication Date: 2005 Feb |
Date Detail:
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Created Date: 2004-11-30 Completed Date: 2005-02-18 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0050222 Medline TA: J Cell Physiol Country: United States |
Other Details:
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Languages: eng Pagination: 478-82 Citation Subset: IM |
Copyright Information:
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2004 Wiley-Liss, Inc. |
Affiliation:
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Istituto di Patologia Generale, Centro di Ricerche Oncologiche Giovanni XXIII, Rome, Italy. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis Breast Neoplasms / enzymology*, pathology* Caspase 3 Caspases / pharmacology* Cell Cycle Proteins / metabolism Cell Division / drug effects Cell Line, Tumor Cyclin-Dependent Kinase Inhibitor p27 Cyclin-Dependent Kinases / antagonists & inhibitors Enzyme Inhibitors / metabolism Female Humans Phosphorylation / drug effects Protein-Serine-Threonine Kinases / metabolism Proto-Oncogene Proteins / metabolism Proto-Oncogene Proteins c-akt Rats Staurosporine / pharmacology Transfection Tumor Suppressor Proteins / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Cdkn1b protein, rat; 0/Cell Cycle Proteins; 0/Enzyme Inhibitors; 0/Proto-Oncogene Proteins; 0/Tumor Suppressor Proteins; 147604-94-2/Cyclin-Dependent Kinase Inhibitor p27; 62996-74-1/Staurosporine; EC 2.7.1.37/AKT1 protein, human; EC 2.7.1.37/Akt1 protein, rat; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 2.7.11.22/Cyclin-Dependent Kinases; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/Casp3 protein, rat; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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