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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1991-5-14
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pubmed:abstractText |
The rate of the degradation of interleukin 2 (IL-2) mRNA produced in stimulated human tonsillar lymphocytes was found to be significantly decreased in cells continuously stimulated with a calcium ionophore, A23187, and a phorbol ester, phorbol 12, 13-dibutylate (PDB) as compared with that in unstimulated cells. When the lymphocytes were stimulated with A23187 and PDB, IL-2 mRNA reached a maximum level at 8 h and gradually decreased to almost the base line by 27 h. IL-2 mRNA produced was rapidly degraded when the stimulants were washed out at 12 h and the cells further cultured in the presence of actinomycin D, which stops mRNA synthesis. However, the stability of IL-2 mRNA was increased by the addition of PDB or A23187. A maximal effect was observed when both were added. The effect of PDB was dose-dependent and inhibited by the inhibitors of protein kinase C (PKC), staurosporine, and K252a, suggesting the involvement of PKC in the control of IL-2 mRNA stability. The involvement of protein phosphorylation in the regulating mechanism of IL-2 mRNA stability was supported by the fact that the addition of okadaic acid, which inhibits serine/threonine protein phosphatases, resulted in an increase in the stability of IL-2 mRNA. Further study demonstrated that the rate of degradation of 32P-labeled IL-2 mRNA, which was prepared by cell-free transcription of IL-2 cDNA, in the polysomal fraction obtained from PDB-stimulated lymphocytes was decreased compared with that obtained from unstimulated lymphocytes. These results indicate the presence of a mechanism controlling the stability of IL-2 mRNA that is regulated by PKC.
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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/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Phorbol 12,13-Dibutyrate,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:issn |
0953-8178
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1073-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1964589-Calcimycin,
pubmed-meshheading:1964589-Cell-Free System,
pubmed-meshheading:1964589-Cells, Cultured,
pubmed-meshheading:1964589-Humans,
pubmed-meshheading:1964589-Interleukin-2,
pubmed-meshheading:1964589-Kinetics,
pubmed-meshheading:1964589-Phorbol 12,13-Dibutyrate,
pubmed-meshheading:1964589-Phosphoprotein Phosphatases,
pubmed-meshheading:1964589-Protein Kinase C,
pubmed-meshheading:1964589-RNA, Messenger,
pubmed-meshheading:1964589-T-Lymphocytes
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pubmed:year |
1990
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pubmed:articleTitle |
Stability of IL-2 mRNA in T lymphocytes is controlled by a protein kinase C-regulated mechanism.
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pubmed:affiliation |
Department of Biochemistry, Kumamoto University Medical School, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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