Source:http://linkedlifedata.com/resource/pubmed/id/18695676
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
53
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| pubmed:dateCreated |
2008-11-13
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| pubmed:abstractText |
Cyclin D1 is involved in cell-cycle arrest in DNA-damage response. This study tested the hypothesis that cyclin D1 regulates mitochondrial apoptosis. Cyclin D1 was induced by low-dose ionizing radiation (LDIR; 10-cGy X-ray) in human keratinocytes with an adaptive radioresistance that can be inhibited by short interfering RNA (siRNA)-mediated cyclin D1 inhibition. Cyclin D1 was found to form complex with chaperon 14-3-3zeta in unstressed cells and mutation of 14-3-3zeta Ser-58 to Asp (S58D) significantly impaired 14-3-3zeta binding to cyclin D1. The formation of cyclin D1/14-3-3zeta complex was differently regulated by exposure to low (10-cGy X-ray) versus high (5-Gy gamma-ray) doses of radiation. Unlike exposure to 5-Gy that predominantly enhanced cyclin D1 nuclear accumulation, LDIR induced the dissociation of the cyclin D1/14-3-3zeta complex without nuclear translocation, indicating that cytosolic accumulation of cyclin D1 was required for LDIR-induced adaptive response. Further studies revealed a direct interaction of cyclin D1 with proapoptotic Bax and an improved mitochondrial membrane potential (Deltapsi(m)) in LDIR-treated cells. Consistently, blocking cyclin D1/Bax formation by cyclin D1 siRNA reversed Deltapsi(m) and inhibited the LDIR-associated antiapoptotic response. These results demonstrate the evidence that cytosolic cyclin D1 is able to regulate apoptosis by interaction with Bax in LDIR-induced adaptive resistance.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BAX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CCND1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D1,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-2-Associated X Protein
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
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| pubmed:issn |
1476-5594
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| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:day |
4
|
| pubmed:volume |
27
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
6738-48
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| pubmed:meshHeading |
pubmed-meshheading:18695676-14-3-3 Proteins,
pubmed-meshheading:18695676-Active Transport, Cell Nucleus,
pubmed-meshheading:18695676-Amino Acid Substitution,
pubmed-meshheading:18695676-Apoptosis,
pubmed-meshheading:18695676-Cell Line,
pubmed-meshheading:18695676-Cell Nucleus,
pubmed-meshheading:18695676-Cyclin D1,
pubmed-meshheading:18695676-Dose-Response Relationship, Radiation,
pubmed-meshheading:18695676-Gamma Rays,
pubmed-meshheading:18695676-Humans,
pubmed-meshheading:18695676-Membrane Potential, Mitochondrial,
pubmed-meshheading:18695676-Mitochondria,
pubmed-meshheading:18695676-Molecular Chaperones,
pubmed-meshheading:18695676-Multiprotein Complexes,
pubmed-meshheading:18695676-Mutation, Missense,
pubmed-meshheading:18695676-RNA, Small Interfering,
pubmed-meshheading:18695676-X-Rays,
pubmed-meshheading:18695676-bcl-2-Associated X Protein
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| pubmed:year |
2008
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| pubmed:articleTitle |
Cyclin D1 in low-dose radiation-induced adaptive resistance.
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| pubmed:affiliation |
Division of Molecular Radiobiology and Graduate Program of Radiation and Cancer Biology, Purdue University School of Health Sciences, West Lafayette, IN 47907, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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