Transcriptional regulation of the mouse fatty acid amide hydrolase gene

Fatty acid amide hydrolase (FAAH) is a membrane-bound enzyme that inactivates a family of fatty acid amide molecules which are implicated in physiological processes such as pain and sleep. We cloned a 1.9 kb fragment of the 5'-untranslated region of the mouse FAAH gene into the pGL3 basic lucif...

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Bibliographic Details
Published in:Gene 2002-05, Vol.291 (1-2), p.203-210
Main Authors: Waleh, N S, Cravatt, B F, Apte-Deshpande, A, Terao, A, Kilduff, T S
Format: Article
Language:English
Subjects:
5' Flanking Region - genetics
Amidohydrolases - genetics
Animals
Base Sequence
Binding Sites - genetics
CHO Cells
COS Cells
Cricetinae
DNA - chemistry
DNA - genetics
Estrogens - pharmacology
Gene Expression - drug effects
Gene Expression Regulation, Enzymologic
Glucocorticoids - pharmacology
Humans
Luciferases - drug effects
Luciferases - genetics
Luciferases - metabolism
Mice
Molecular Sequence Data
Plasmids - genetics
Promoter Regions, Genetic - genetics
Recombinant Fusion Proteins - drug effects
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Sequence Analysis, DNA
Transcription Initiation Site
Transcription, Genetic
Transfection
Tumor Cells, Cultured
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Summary:Fatty acid amide hydrolase (FAAH) is a membrane-bound enzyme that inactivates a family of fatty acid amide molecules which are implicated in physiological processes such as pain and sleep. We cloned a 1.9 kb fragment of the 5'-untranslated region of the mouse FAAH gene into the pGL3 basic luciferase reporter vector and showed that this sequence has promoter activity in vitro. By primer extension analysis, we have determined the transcription start site to be 200 bases upstream of the ATG initiation codon and found that a TATA motif was absent. A number of putative response elements, including those for estrogen and glucocorticoids, were identified in this sequence. We have demonstrated that the estrogen and glucocorticoid receptors down-regulate transcriptional activity independent of their ligand. These data should help in understanding the mechanisms of FAAH gene transcription.
ISSN:0378-1119
DOI:10.1016/S0378-1119(02)00598-X