1: Mol Pharmacol. 2001 Apr;59(4):852-9. 

Regulation of human monoamine oxidase B gene by Sp1 and Sp3.

Wong WK, Chen K, Shih JC.

Department of Cell and Neurobiology, School of Medicine, University of Southern
California, Los Angeles, California, USA.

The human monoamine oxidase (MAO) B plays a major role in the degradation of
biogenic and dietary amines such as phenylethylamine, benzylamine, dopamine, and
tyramine. We previously showed that the -246/-99 MAO B promoter region exhibited
the highest activity and contained two clusters of overlapping Sp1 sites, a
CACCC element and a TATA box. Here, using a series of 10 deletion constructs of
the 2-kilobase pair 5'-flanking sequence, we identified additional potential
regulatory elements, including activator proteins 1 and 4, CAAT, GATA, upstream
stimulatory factor (USF), estrogen receptor (ER), and sex-determining region
Y-box 5 (SOX5). Analysis of nine site-directed mutations of -246/-99 region
reveals that both clusters of Sp1 sites contribute positively whereas the CACCC
element contributes negatively to the transcriptional activity. Gel shift
analysis demonstrates that in addition to Sp1, Sp3 can interact with both
clusters of Sp1 sites. Cotransfection experiments show that Sp1 and its closely
related family member Sp4 can trans-activate MAO B promoter activity through the
proximal cluster of Sp1 sites and its activation can be repressed by the
over-expression of Sp3 and a related family member BTEB2. These results suggest
that the binding to the overlapping Sp1 sites by various members of Sp family is
important for the regulation of the MAO B gene expression.

PMID: 11259630 [PubMed - indexed for MEDLINE]


---------------------------------------------------------------