Source:http://linkedlifedata.com/resource/pubmed/id/11282109
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2001-4-3
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pubmed:abstractText |
Esculetin, a coumarin compound, has been shown to exhibit antioxidant and anti-inflammatory effects. In the present study, esculetin was found to inhibit the survival of human promyelocytic leukemia HL-60 cells in a concentration-dependent and time-dependent manner. HL-60 cells underwent internucleosomal DNA fragmentation and morphological changes characteristic of apoptosis after a 24-h treatment with esculetin (100 microM). Flow cytometric analysis showed that the hypodiploid nuclei of HL-60 cells were increased to 40.93% after a 36-h treatment with esculetin (100 microM). Further investigation showed that esculetin induced the release of cytochrome c from mitochondria into cytosol in a time-dependent and concentration-dependent manner. Moreover, esculetin application reduced Bcl-2 protein expression to 58% after 9 h as compared with that time at 0. Cysteine protease 32 kDa proenzyme (CPP32), a caspase 3, was activated and its substrate, poly (adenosine diphosphate-ribose) polymerase, was cleaved after a 24-h treatment of HL-60 cells with esculetin. These data suggest that esculetin induces apoptosis in human leukemia cells by increasing cytosolic translocation of cytochrome c and activation of CPP32.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/Umbelliferones,
http://linkedlifedata.com/resource/pubmed/chemical/esculetin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-2999
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
416
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11282109-Antioxidants,
pubmed-meshheading:11282109-Apoptosis,
pubmed-meshheading:11282109-Caspase 3,
pubmed-meshheading:11282109-Caspases,
pubmed-meshheading:11282109-Cell Survival,
pubmed-meshheading:11282109-Cytochrome c Group,
pubmed-meshheading:11282109-DNA Fragmentation,
pubmed-meshheading:11282109-Dose-Response Relationship, Drug,
pubmed-meshheading:11282109-HL-60 Cells,
pubmed-meshheading:11282109-Humans,
pubmed-meshheading:11282109-Poly(ADP-ribose) Polymerases,
pubmed-meshheading:11282109-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:11282109-Time Factors,
pubmed-meshheading:11282109-Umbelliferones
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pubmed:year |
2001
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pubmed:articleTitle |
Induction of apoptosis by esculetin in human leukemia cells.
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pubmed:affiliation |
Department and Institute of Biochemistry, Chung Shan Medical and Dental College, No. 110, Section 1, Chien Kuo N. Road, 402, Taichung, Taiwan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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