Characterisation of gamma-glutamylcysteine synthetase-heavy subunit promoter: a critical role for AP-1.
The 5'-flanking region of human gamma-glutamylcysteine synthetase-heavy subunit (gamma-GCS-HS) was characterised by creating a series of chloramphenicol acetyl transferase (CAT) reporter deletion constructs. Analysis of various deleted CAT constructs revealed that a putative AP-1 consensus sequence is required to direct the constitutive and oxidant-mediated promoter activity. Gel mobility shift and mutation analysis of the sequence (-269 to -263 bp), showed binding of AP-1 is involved in the oxidant-mediated regulation of gamma-GCS-HS promoter activity.
Rahman
I
I
Department of Medicine, University of Edinburgh, Royal Infirmary, UK.
Smith
C A
CA
Antonicelli
F
F
MacNee
W
W
D002478:Cells, Cultured; D004847:Epithelial Cells / Q000502:physiology; D005721:Glutamate-Cysteine Ligase / Q000302:isolation & purification*; D006490:Hemostatics / Q000494:pharmacology; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D016877:Oxidants / Q000494:pharmacology; D018808:Transcription Factor AP-1 / Q000187:drug effects / Q000502:physiology*; D014812:Vitamin K / Q000494:pharmacology
D006490:Hemostatics; D016877:Oxidants; D018808:Transcription Factor AP-1; D014812:Vitamin K; D006861:Hydrogen Peroxide; D005721:Glutamate-Cysteine Ligase