Lippincott Williams & Wilkins, Inc., Philadelphia
Coordinated Expression of β-Amyloid Precursor Protein and the Putative β-Secretase BACE and α-Secretase ADAM10 in Mouse and Human Brain
Article first published online: 4 JAN 2002
Journal of Neurochemistry
Volume 75, Issue 5, pages 2133–2143, November 2000
How to Cite
Marcinkiewicz, M. and Seidah, N. G. (2000), Coordinated Expression of β-Amyloid Precursor Protein and the Putative β-Secretase BACE and α-Secretase ADAM10 in Mouse and Human Brain. Journal of Neurochemistry, 75: 2133–2143. doi: 10.1046/j.1471-4159.2000.0752133.x
Abbreviations used: Aβ, β-amyloid; AD, Alzheimer's disease; β-APP, β-amyloid precursor protein; Cx-d, cerebral cortex deep layers; Cx-s, cerebral cortex superficial layers; e, embryonic day; HES, high expression sites; p, postnatal day; PreS, presenile.
- Issue published online: 4 JAN 2002
- Article first published online: 4 JAN 2002
- mRNA colocalization;
- Mouse ontogeny;
- Diffuse amyloid plaques;
- Presenile Alzheimer's subjects;
- Etiology of Alzheimer's disease
Abstract: To define the enzymes involved in the etiology of Alzheimer's disease, we compared in mouse and human brain the mRNA levels and cellular localization of the ubiquitous β-amyloid precursor protein (β-APP) with those of the putative α-secretases ADAM10 and ADAM17 and the β-secretases BACE and BACE2. In situ hybridization performed in mice during prenatal and postnatal development and in adulthood revealed the coexpression of β-APP, BACE, and ADAM10. The patterns of BACE2 and ADAM17 only partially overlapped with that of β-APP. β-APP, BACE, and ADAM10 mRNAs have also been detected by northern blot in human brain cortex of normal subjects and in Alzheimer's disease subjects. In situ hybridization performed using combined biotin- and radiolabeled riboprobes provided evidence for the coexpression of β-APP with BACE and ADAM10 in human cortical neurons. Our data provide cytochemical evidence supporting the role of ADAM10 and BACE as authentic α- and β-secretases.