Document Detail


Contribution of death receptor and mitochondrial pathways to Fas-mediated apoptosis in the prostatic carcinoma cell line PC3.
MedLine Citation:
PMID:  11987151     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Two main pathways of apoptosis in mammalian cells have been described: the death receptor pathway and the mitochondrial pathway. Two different cell types have been identified for Fas-mediated apoptosis, each using almost exclusively one of two different signaling pathways. Human prostatic carcinoma cell line, PC3 is sensitive to Fas-mediated apoptosis, but relation of receptor and mitochondrial pathways is not clear. METHODS: Cell viability was estimated by calcein assay. Apoptosis was determined by preparation of DNA ladder. Expression of Fas-associated death domain-dominant negative (FADD-DN) and Bcl-2, activation of caspases, PARP, DFF45, Bid cleavage, and cytochrome c release were assessed using Western blotting techniques. [(35)S] Methionine-labeled caspase-3 was transcribed in vitro and translated using the TNT kit (Promega). A vector containing caspase-3 was prepared by the ligation of EcoR I/BamHI flanked PCR fragment of full size caspase-3 cDNA into pBlusckript II SK(+/-) (Stratagen). RESULTS: Overexpression of both FADD-DN and Bcl-2 genes prevent Fas-mediated apoptosis in PC3. As predicted, overexpression of FADD-DN prevented activation of caspase-8 and Bid cleavage and attenuated the release of cytochrome c and activation of caspases -2, -7, and -9. Bcl-2 overexpression did not affect caspase-8 activation and cleavage of Bid but blocked the release of cytochrome c and activation of mitochondria localized caspases -2, -7, and-9. Overexpression of FADD-DN and Bcl-2 affected the activation of caspase-3 and PARP cleavage differently: FADD-DN attenuated the activation of caspase-3 and PARP cleavage whereas Bcl-2 overexpression prevented caspase-3 activation and completely blocked cleavage of PARP. CONCLUSIONS: These data suggest that activation of caspase-8 is necessary but not sufficient to complete Fas-mediated apoptosis in PC3 cells without activation of the mitochondrial pathway. In addition, caspase-3 activation after Fas-receptor ligation involves two steps and is dependent on mitochondrial activation.
Authors:
Natalya V Guseva; Agshin F Taghiyev; Oskar W Rokhlin; Michael B Cohen
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Prostate     Volume:  51     ISSN:  0270-4137     ISO Abbreviation:  Prostate     Publication Date:  2002 Jun 
Date Detail:
Created Date:  2002-05-23     Completed Date:  2002-06-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8101368     Medline TA:  Prostate     Country:  United States    
Other Details:
Languages:  eng     Pagination:  231-40     Citation Subset:  IM    
Copyright Information:
Copyright 2002 Wiley-Liss, Inc.
Affiliation:
Department of Pathology, The University of Iowa, Iowa City, Iowa 52242-1087, USA.
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MeSH Terms
Descriptor/Qualifier:
Antigens, CD95 / physiology*
Apoptosis*
Blotting, Western
Caspase 8
Caspase 9
Caspases / pharmacology
Gene Expression Regulation, Neoplastic*
Humans
Male
Mitochondria / physiology*
Polymerase Chain Reaction
Prostatic Neoplasms / pathology*
Proto-Oncogene Proteins c-bcl-2 / biosynthesis,  pharmacology*
Chemical
Reg. No./Substance:
0/Antigens, CD95; 0/Proto-Oncogene Proteins c-bcl-2; EC 3.4.22.-/CASP8 protein, human; EC 3.4.22.-/CASP9 protein, human; EC 3.4.22.-/Caspase 8; EC 3.4.22.-/Caspase 9; EC 3.4.22.-/Caspases

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