rdf:type |
|
lifeskim:mentions |
umls-concept:C0013879,
umls-concept:C0021641,
umls-concept:C0031586,
umls-concept:C0032214,
umls-concept:C0035820,
umls-concept:C0037083,
umls-concept:C0065558,
umls-concept:C0085828,
umls-concept:C0086860,
umls-concept:C0162326,
umls-concept:C0449255,
umls-concept:C0962754,
umls-concept:C1514562,
umls-concept:C1554080,
umls-concept:C1706198,
umls-concept:C1710082
|
pubmed:issue |
31
|
pubmed:dateCreated |
2002-7-29
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pubmed:abstractText |
Insulin stimulates malic enzyme (ME)-chloramphenicol acetyltransferase (CAT) and collagenase-1-CAT fusion gene expression in H4IIE cells through identical activator protein-1 (AP-1) motifs. In contrast, insulin and phorbol esters only stimulate collagenase-1-CAT and not ME-CAT fusion gene expression in HeLa cells. The experiments in this article were designed to explore the molecular basis for this differential cell type- and gene-specific regulation. The results highlight the influence of three variables, namely promoter context, AP-1 flanking sequence, and accessory elements that modulate insulin and phorbol ester signaling through the AP-1 motif. Thus, fusion gene transfection and proteolytic clipping gel retardation assays suggest that the AP-1 flanking sequence affects the conformation of AP-1 binding to the collagenase-1 and ME AP-1 motifs such that it selectively binds the latter in a fully activated state. However, this influence of ME AP-1 flanking sequence is dependent on promoter context. Thus, the ME AP-1 motif will mediate both an insulin and phorbol ester response in HeLa cells when introduced into either the collagenase-1 promoter or a specific heterologous promoter. But even in the context of the collagenase-1 promoter, the effects of both insulin and phorbol esters, mediated through the ME AP-1 motif are dependent on accessory factors.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol O-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Collagenases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Malate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Phorbol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase,
http://linkedlifedata.com/resource/pubmed/chemical/collagenase 1
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
|
pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
277
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
27935-44
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:12032154-Base Sequence,
pubmed-meshheading:12032154-Cell Line,
pubmed-meshheading:12032154-Chloramphenicol O-Acetyltransferase,
pubmed-meshheading:12032154-Collagenases,
pubmed-meshheading:12032154-DNA Primers,
pubmed-meshheading:12032154-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:12032154-HeLa Cells,
pubmed-meshheading:12032154-Humans,
pubmed-meshheading:12032154-Insulin,
pubmed-meshheading:12032154-Malate Dehydrogenase,
pubmed-meshheading:12032154-Mutagenesis,
pubmed-meshheading:12032154-Oligodeoxyribonucleotides,
pubmed-meshheading:12032154-Phorbol Esters,
pubmed-meshheading:12032154-Polymerase Chain Reaction,
pubmed-meshheading:12032154-Promoter Regions, Genetic,
pubmed-meshheading:12032154-Recombinant Proteins,
pubmed-meshheading:12032154-Transcription Factor AP-1,
pubmed-meshheading:12032154-Transcription Factors,
pubmed-meshheading:12032154-Transfection,
pubmed-meshheading:12032154-beta-Galactosidase
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pubmed:year |
2002
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pubmed:articleTitle |
Accessory elements, flanking DNA sequence, and promoter context play key roles in determining the efficacy of insulin and phorbol ester signaling through the malic enzyme and collagenase-1 AP-1 motifs.
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pubmed:affiliation |
Department of Molecular Physiology and Biophysics, Vanderbilt University Medical School, Nashville, Tennessee 37232, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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