Cholinergic dysfunction in a mouse model of Alzheimer disease is reversed by an anti-Aβ antibody
J. Clin. Invest. Kelly R. Bales, et al. 116:825 doi:10.1172/JCI27120 [Go to this article.]

Figure 3
Aβ interacts with ChT-1. (A and B) High-affinity choline uptake into rat synaptosomes (A) and a cell line expressing the human ChT-1 (B) was significantly increased after exposure to Aβ₄₂. Data are the percent of choline uptake in untreated, control samples (mean ± SEM of triplicate values) from 1 representative experiment, which was repeated 2–3 times with similar results. *P < 0.05. (C) ChT-1 was coimmunoprecipitated from hippocampal extracts by the anti-Aβ antibody 4G8 followed by Western blot analysis with an anti–ChT-1 antibody. (D) The Aβ peptide was coimmunoprecipitated from hippocampal extracts prepared from PDAPP transgenic mice by an anti–ChT-1 antibody followed by Western blot analysis with biotinylated anti-Aβ antibodies 21F12 and 2G3. (E) The anti-Aβ₄₂ antibody 21F12, but not the anti-Aβ₄₀ antibody 2G3, coimmunoprecipitated ChT-1 from hippocampal extracts prepared from PDAPP transgenic mice followed by Western blot analysis with an anti–ChT-1 antibody. (F) Neither an irrelevant IgG nor an anti–glutamate 1 transporter antibody (EAAT-1) coimmunoprecipitated Aβ from hippocampal extracts prepared from PDAPP mice, whereas Aβ was readily detected following immunoprecipitation with an antibody directed toward ChT-1 followed by Western blot analysis with an anti-Aβ antibody.