Document Detail


Caspase-3 activation and induction of PARP cleavage by cyclic dipeptide cyclo(Phe-Pro) in HT-29 cells.
MedLine Citation:
PMID:  16309216     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Cyclo(Phe-Pro) has been shown to inhibit cancer cell growth and induce apoptosis in HT-29 colon cancer cells. MATERIALS AND METHODS: The molecular mechanisms mediating cyclo(Phe-Pro)-induced apoptosis in HT-29 cells were investigated. Cells were treated with 5 mM or 10 mM cyclo(Phe-Pro) for varying times. Immunoblot analysis was used to detect poly(ADP-ribose)polymerase (PARP) cleavage. A fluorescence-based enzymatic assay was used to measure caspase-3 activity. RESULTS: Cyclo(Phe-Pro) (10 mM) induced time-dependent cleavage of PARP, detected as early as 8 hours post treatment. PARP cleavage was blocked by co-administration with the broad-range caspase inhibitor Z-VAD-FMK Cyclo(Phe-Pro) also induced a time-dependent increase (p < 0.01) in caspase-3 activity. This increase in activity was blocked in the presence of the caspase-3 inhibitor Ac-DEVD-CHO. CONCLUSION: These results provide evidence that cyclo(Phe-Pro)-induced apoptosis in HT-29 cells is mediated by a caspase cascade. These findings warrant further investigation into the potential antitumour activity of cyclo(Phe-Pro) and its related cyclic dipeptide derivatives.
Authors:
Seth Clint Brauns; Gill Dealtry; Pieter Milne; Ryno Naudé; Maryna Van de Venter
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Anticancer research     Volume:  25     ISSN:  0250-7005     ISO Abbreviation:  Anticancer Res.     Publication Date:    2005 Nov-Dec
Date Detail:
Created Date:  2005-11-28     Completed Date:  2006-01-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8102988     Medline TA:  Anticancer Res     Country:  Greece    
Other Details:
Languages:  eng     Pagination:  4197-202     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Microbiology, Nelson Mandela Metropolitan University, Port Elizabeth, 6031, South Africa.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Chloromethyl Ketones / pharmacology
Caco-2 Cells
Caspase 3
Caspases / antagonists & inhibitors,  biosynthesis,  metabolism*
Cysteine Proteinase Inhibitors / pharmacology
Dipeptides / pharmacology*,  toxicity
Enzyme Activation / drug effects
Enzyme Induction / drug effects
HT29 Cells
Humans
Peptides, Cyclic / pharmacology*,  toxicity
Poly(ADP-ribose) Polymerases / metabolism*
Chemical
Reg. No./Substance:
0/Amino Acid Chloromethyl Ketones; 0/Cysteine Proteinase Inhibitors; 0/Dipeptides; 0/Peptides, Cyclic; 0/benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone; 0/cyclo(phenylalanyl-prolyl); EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 3.4.22.-/CASP3 protein, human; 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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