Document Detail


Dykellic acid inhibits drug-induced caspase-3-like protease activation.
MedLine Citation:
PMID:  12615068     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Dykellic acid is a novel microbial metabolite isolated from the broth of Westerdykella multispora F50733. Investigations on the molecular function of dykellic acid revealed that this compound partially inhibits calcium influx, resulting in a decrease in Ca(2+)-dependent endonuclease activation and DNA fragmentation induced by camptothecin. In our experiments, active caspase-3-like protease cleavage of procaspase-3, PARP, and cytosolic cytochrome c was inhibited by dykellic acid in a concentration-dependent manner when the apoptosis was induced by camptothecin as well as doxorubicin. We confirmed that dykellic acid did not bind to camptothecin using surface plasmon resonance analysis. These results suggest that dykellic acid inhibits drug-induced apoptosis via a caspase-3-like protease-suppressing mechanism. Our data provide important information on the mechanism of action of dykellic acid and indicate that this compound may be employed in the treatment of specific caspase-3-like protease-mediated diseases.
Authors:
Sang-Han Lee; Eun-Soo Youk; Ho-Jae Lee; Yung-Hee Kho; Hwan Mook Kim; Sung-Uk Kim
Related Documents :
2172028 - The biological activity of retinoids in melanoma cells. induction of expression of reti...
19814868 - Enhanced anticancer activity of glutamate prodrugs of all-trans retinoic acid.
15601608 - A retinoic-acid critical period in the early postnatal mouse brain.
7305988 - The effect of all-trans-retinoic acid on the synthesis of epidermal cell-surface-associ...
17383068 - Inhibitory action of polyunsaturated fatty acids on imp dehydrogenase.
7175628 - Ammonia metabolism in dogs with portacaval shunts.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  302     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2003 Mar 
Date Detail:
Created Date:  2003-03-04     Completed Date:  2003-05-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  539-44     Citation Subset:  IM    
Affiliation:
Korea Research Institute of Bioscience & Biotechnology, Taejon 305-333, Republic of Korea. sang@mail.kribb.re.kr
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Apoptosis
Blotting, Western
Calcium / metabolism
Camptothecin / metabolism,  pharmacology
Caspase 3
Caspases / metabolism*
Cell Line
Cytochrome c Group / metabolism
Cytosol / enzymology
DNA Fragmentation
Dose-Response Relationship, Drug
Endonucleases / metabolism
Enzyme Activation
Enzyme Precursors / metabolism
HL-60 Cells
Humans
Jurkat Cells
Microscopy, Electron, Scanning
Models, Chemical
Poly(ADP-ribose) Polymerases / metabolism
Propionates / pharmacology*
Pyrones / pharmacology*
Spectrometry, Fluorescence
Surface Plasmon Resonance
Time Factors
U937 Cells
Chemical
Reg. No./Substance:
0/Cytochrome c Group; 0/Enzyme Precursors; 0/Propionates; 0/Pyrones; 0/dykellic acid; 7440-70-2/Calcium; 7689-03-4/Camptothecin; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 3.1.-/Endonucleases; 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


Previous Document:  The yeast model for Batten disease: a role for Btn2p in the trafficking of the Golgi-associated vesi...
Next Document:  Nuclear localization of Galectin-3 in transformed thyroid cells: a role in transcriptional regulatio...