In:
Annals of the New York Academy of Sciences, Wiley, Vol. 1035, No. 1 ( 2004-12), p. 49-67
Abstract:
A bstract : Deposition of amyloid β protein in the brain is the major pathological feature of Alzheimer's disease. Amyloid β protein is generated from β‐amyloid precursor protein by β‐secretase and γ‐secretase. Proteolytic processing of amyloid precursor protein at the β site by BACE1 is essential to generate amyloid β protein. BACE1, the major β‐secretase involved in cleaving amyloid precursor protein, has been identified as a type 1 membrane‐associated aspartyl protease. In this study, we found that BACE1 gene expression is controlled by a TATA‐less promoter. BACE1 gene expression is tightly regulated at the transcriptional level and the transcription factor Sp1 plays an important role in regulation of BACE1 to process amyloid precursor protein generating amyloid β protein. Furthermore, we found that BACE1 protein is ubiquitinated, and the degradation of BACE1 proteins and amyloid precursor protein processing are regulated by the ubiquitin‐proteasome pathway.
Type of Medium:
Online Resource
ISSN:
0077-8923
,
1749-6632
DOI:
10.1196/annals.1332.004
Language:
English
Publisher:
Wiley
Publication Date:
2004
detail.hit.zdb_id:
2834079-6
detail.hit.zdb_id:
211003-9
detail.hit.zdb_id:
2071584-5
SSG:
11
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