A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
J. Clin. Invest. Rolf Postina, et al. 113:1456 doi:10.1172/JCI20864 [
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Figure 2Detection and quantitation of human APP processing products in double-transgenic
ADAM10-mo ∞
APP[V717I],
ADAM10-hi ∞
APP[V717I],
ADAM10-hz ∞
APP[V717I], and
ADAM10-dn ∞
APP[V717I] mice as well as in monotransgenic
APP[V717I] (
APP) animals. All analyzed mice were 18 weeks old. (
A) APP processing products detected by Western blot analysis as described in Methods. First row, secreted APPsα; second row, secreted APPsβ; third row, membrane-bound APP C-terminal fragments (CTFα, CTFβ); last row, membrane-bound full-length APP (APP fl). (
B) Quantitative analysis of the APP-processing products APPsα, APPsβ, and APP CTFα from different mouse lines. In all experiments, quantified APP processing products were normalized to APP fl expression. Values are expressed as percentages of values from APP control mice (set to 100%) and are the mean ± SD (
n = 7_8 animals of each line). Significance was determined by the unpaired Student’s
t test. *
P < 0.05;
#P < 0.01;
P < 0.001. (
C) Quantitation of soluble human Aβ40 and Aβ42 peptides isolated from mouse brains by sandwich ELISA.
APP[V717I] mice (
n = 6) were used as control to
ADAM10-hz ∞
APP[V717I] (
n = 7) and
ADAM10-dn ∞
APP[V717I] (
n = 6) animals. Values are the mean ± SEM of the amount of each Aβ peptide per gram of mouse brain. Significance was determined by the unpaired Student’s
t test. *
P < 0.05.
