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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2003-2-4
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pubmed:abstractText |
Human epidermal melanocytes hold the full capacity for autocrine de novo synthesis/regulation/recycling of the essential cofactor 6-tetrahydrobiopterin (6BH(4)) for conversion of L-phenylalanine via phenylalanine hydroxylase to L-tyrosine and for production of L-Dopa via tyrosine hydroxylase to initiate both pigmentation and catecholamine synthesis in these neural crest-derived cells. Earlier we have demonstrated pterin-4a-carbinolamine dehydratase (PCD) mRNA and enzyme activities in epidermal melanocytes and keratinocytes. This protein dimerises also the transcription factor hepatocyte nuclear factor 1 (HNF-1), leading to activation of multiple genes. This study demonstrates for the first time DCoH/HNF-1 alpha expression and transcriptional activity in human epidermal melanocytes in vitro and in situ and identified tyrosinase, the key enzyme for pigmentation, as a new transcriptional target. Specific binding of DCoH/HNF-1 complex to the human tyrosinase promoter was confirmed by gel shift analysis. These results provide a novel mechanism in the regulation of skin pigmentation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HNF1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/HNF1B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Nuclear Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Nuclear Factor 1-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Nuclear Factor 1-beta,
http://linkedlifedata.com/resource/pubmed/chemical/Hydro-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Monophenol Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/pterin-4a-carbinolamine dehydratase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
301
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
610-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12565907-Amino Acid Sequence,
pubmed-meshheading:12565907-Binding Sites,
pubmed-meshheading:12565907-Cells, Cultured,
pubmed-meshheading:12565907-DNA-Binding Proteins,
pubmed-meshheading:12565907-Epidermis,
pubmed-meshheading:12565907-Hepatocyte Nuclear Factor 1,
pubmed-meshheading:12565907-Hepatocyte Nuclear Factor 1-alpha,
pubmed-meshheading:12565907-Hepatocyte Nuclear Factor 1-beta,
pubmed-meshheading:12565907-Humans,
pubmed-meshheading:12565907-Hydro-Lyases,
pubmed-meshheading:12565907-Melanocytes,
pubmed-meshheading:12565907-Models, Molecular,
pubmed-meshheading:12565907-Molecular Sequence Data,
pubmed-meshheading:12565907-Monophenol Monooxygenase,
pubmed-meshheading:12565907-Nuclear Proteins,
pubmed-meshheading:12565907-Promoter Regions, Genetic,
pubmed-meshheading:12565907-Protein Conformation,
pubmed-meshheading:12565907-Transcription, Genetic,
pubmed-meshheading:12565907-Transcription Factors
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pubmed:year |
2003
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pubmed:articleTitle |
In situ and in vitro evidence for DCoH/HNF-1 alpha transcription of tyrosinase in human skin melanocytes.
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pubmed:affiliation |
Clinical and Experimental Dermatology, Department of Biomedical Sciences, University of Bradford, Bradford, West Yorkshire BD7 1DP, UK. K.Schallreuter@bradford.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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