Source:http://linkedlifedata.com/resource/pubmed/id/10081494
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rdf:type | |
lifeskim:mentions |
umls-concept:C0013470,
umls-concept:C0017337,
umls-concept:C0162638,
umls-concept:C0205263,
umls-concept:C0376515,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C0680022,
umls-concept:C0683598,
umls-concept:C1366587,
umls-concept:C1552599,
umls-concept:C1704259,
umls-concept:C1704787,
umls-concept:C1705987,
umls-concept:C1708811
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pubmed:issue |
12
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pubmed:dateCreated |
1999-4-2
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pubmed:abstractText |
EAT/mcl-1 showed increased expression during the differentiation of a multipotent human embryonic carcinoma cell line, NCR-G3, and of myeloblastic cells "ML-1," and has sequence similarity to Bcl-2. In this present study, we determined whether the apoptotic cell death induced by chemotherapeutic agents could be inhibited by EAT/mcl-1, as has been found with Bcl-2. Cells transfected with EAT/mcl-1 showed higher resistance to cis-diammine dichloroplatinum (II) (CDDP) and carboplatin compared with the parental line (10)1 and neomycin-resistance gene-transfected clone, (10)1/neo. There was, however, no difference in sensitivity to etoposide, N,N-bis-(2-chloroethyl)-N'-(3-hydroxypropyl) phosphordiamidic acid cyclic ester monohydrate, adriamycin or other chemotherapeutic agents tested. DNA fragmentation of the parental cells following treatment with CDDP and carboplatin was observed in a concentration-dependent manner. In contrast, cells transfected with EAT/mcl-1 did not show DNA fragmentation following treatment with the same concentration of these drugs. EAT/mcl-1 was capable of delaying the onset of p53-independent apoptosis, although it could not inhibit apoptosis completely. Since CDDP and carboplatin damage DNA and then activate c-abl and the JNK/SAPK pathway, EAT/mcl-1 may inhibit p53-independent apoptosis through a c-abl/JNK (SAPK)-dependent mechanism. EAT/mcl-1 has functional homology to Bcl-2 in that it can enhance cell viability under conditions which otherwise cause apoptosis and increase resistance to chemotherapeutic agents.
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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/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Cisplatin,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53,
http://linkedlifedata.com/resource/pubmed/chemical/myeloid cell leukemia sequence 1...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0910-5050
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1326-33
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pubmed:dateRevised |
2008-7-9
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pubmed:meshHeading |
pubmed-meshheading:10081494-Animals,
pubmed-meshheading:10081494-Antineoplastic Agents,
pubmed-meshheading:10081494-Apoptosis,
pubmed-meshheading:10081494-Cisplatin,
pubmed-meshheading:10081494-DNA Fragmentation,
pubmed-meshheading:10081494-Fibroblasts,
pubmed-meshheading:10081494-Genes, bcl-2,
pubmed-meshheading:10081494-Mice,
pubmed-meshheading:10081494-Multigene Family,
pubmed-meshheading:10081494-Neoplasm Proteins,
pubmed-meshheading:10081494-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:10081494-Recombinant Fusion Proteins,
pubmed-meshheading:10081494-Signal Transduction,
pubmed-meshheading:10081494-Transfection,
pubmed-meshheading:10081494-Tumor Suppressor Protein p53
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pubmed:year |
1998
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pubmed:articleTitle |
EAT/mcl-1, a member of the bcl-2 related genes, confers resistance to apoptosis induced by cis-diammine dichloroplatinum (II) via a p53-independent pathway.
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pubmed:affiliation |
Department of Pathology, Keio University School of Medicine, Tokyo.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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