The main characteristic of Alzheimer's disease (AD) is brain deposition of the beta-amyloid (Abeta) peptide, generated endoproteolytically from Abeta precursor protein (APP) by beta- and gamma-secretases. A transmembrane aspartyl protease, beta-APP-cleaving enzyme (BACE1), was identified as beta-secretase. Although BACE1 cleaves APP at the beta-secretase site, the role of its homolog, beta-secretase 2 (BACE2) is poorly understood. We report the mRNA expression profile, DNA sequence, and molecular characterization of the BACE2 gene, located on chromosome 21q22.3. The BACE2 gene expresses more strongly in peripheral tissues, although BACE2 mRNA is found in the majority of brain regions, including the postcentral gyrus and temporal lobe. Characterization of 2932 bp of the BACE2 5'-flanking region (GC content of 55%), reveals the absence of canonical CCAAT and TATA boxes within 1 kb of the transcription start site (TSS). The sequence lacks significant internal repeats and has a housekeeping gene structure. Two active regions of the BACE2 promoter determine its basal expression and cell-type specificity. The proximal region (-31/+238) likely determines general basal expression, and the distal region (-2618/-1513), cell-type specificity. Several putative transcription factor sites, particularly SP1, Oct-1, and HES-1, are predicted to be within 1 kb of the TSS. On either side of the proximal promoter region, two negative regulatory domains might reduce BACE2 expression under an induced condition. The BACE2 5'-flanking region is likely to be highly regulated and expressed in a tissue type-specific manner.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1385/JMN:29:1:81 | DOI Listing |
Brain Res
February 2009
Department of Neurology, Xuan Wu Hospital of the Capital Medical University, Key Neurodegenerative Laboratory of Ministry of Education of the People's Republic of China, Beijing 100053, PR China.
Amyloid beta-peptide (A beta) plays a central role in the pathogenesis of Alzheimer's disease (AD). A beta is produced by sequential cleavage of the amyloid precursor protein (APP) by two enzymes referred to as beta- and gamma-secretase. beta-secretase is of more importance, as it catalyses the rate-limiting step in the production of A beta.
View Article and Find Full Text PDFJ Mol Neurosci
March 2007
Laboratory of Molecular Neurogenetics, Department of Psychiatry, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
The main characteristic of Alzheimer's disease (AD) is brain deposition of the beta-amyloid (Abeta) peptide, generated endoproteolytically from Abeta precursor protein (APP) by beta- and gamma-secretases. A transmembrane aspartyl protease, beta-APP-cleaving enzyme (BACE1), was identified as beta-secretase. Although BACE1 cleaves APP at the beta-secretase site, the role of its homolog, beta-secretase 2 (BACE2) is poorly understood.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!