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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1996-11-27
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pubmed:abstractText |
Cloudman S-91 mouse melanoma cells respond to alpha-melanocyte-stimulating hormone) by demonstrating a marked increase in tyrosinase activity (O-diphenol-O2 oxidoreductase, EC 1.14.18.1). This increase is the result of increased levels of tyrosinase mRNA with a subsequent increase in tyrosinase abundance. Our studies were carried out to determine the effect of melanocyte-stimulating hormone on tyrosinase gene transcription and to measure the kinetics of the hormone-induced increase in tyrosinase mRNA. When melanoma cells were exposed continuously to melanocyte-stimulating hormone for 6 d, a large but transient increase in both tyrosinase mRNA abundance and enzyme activity were observed. The maximum increase in tyrosinase mRNA occurred 60 h after melanocyte-stimulating hormone stimulation and was followed by a decline in message levels even though cells were continuously exposed to hormone. Results of nuclear run-off transcription assays showed that melanocyte-stimulating hormone caused a slow increase in the rate of transcription of the tyrosinase gene with a maximal 6-fold stimulation occurring at 48 h. In cells treated with the ribonucleic acid synthesis inhibitor, 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole, tyrosinase mRNA levels decayed with a half-life of 4-5 h. This decay rate was unaffected by treatment of cells with melanocyte-stimulating hormone, indicating that the hormone does not act to stabilize tyrosinase ribonucleic acid. Inhibition of protein synthesis by treatment with cycloheximide had no effect on the melanocyte-stimulating hormone-induced increase in tyrosinase messenger ribonucleic acid levels suggesting that ongoing protein synthesis is not required for, at least, the initial stimulation of tyrosinase gene transcription by melanocyte-stimulating hormone.
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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/Chloramphenicol O-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/Melanocyte-Stimulating Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Monophenol Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-202X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
107
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
689-93
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:8875950-Animals,
pubmed-meshheading:8875950-Chloramphenicol O-Acetyltransferase,
pubmed-meshheading:8875950-Cyclic AMP,
pubmed-meshheading:8875950-Cycloheximide,
pubmed-meshheading:8875950-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:8875950-Melanocyte-Stimulating Hormones,
pubmed-meshheading:8875950-Melanoma, Experimental,
pubmed-meshheading:8875950-Mice,
pubmed-meshheading:8875950-Monophenol Monooxygenase,
pubmed-meshheading:8875950-RNA, Messenger,
pubmed-meshheading:8875950-Transcription, Genetic
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pubmed:year |
1996
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pubmed:articleTitle |
Regulation of tyrosinase mRNA in mouse melanoma cells by alpha-melanocyte-stimulating hormone.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Oklahoma, Health Science Center, Oklahoma City, USA.
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pubmed:publicationType |
Journal Article
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