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Vol. 59, Issue 4, 852-859, April 2001
Department of Cell and Neurobiology, School of Medicine (W.K.W.,
J.C.S.) and Department of Molecular Pharmacology and Toxicology, School
of Pharmacy (K.C., J.C.S.), University of Southern California, Los
Angeles, California
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.
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