Figure 5
From: ApoE-fragment/Aβ heteromers in the brain of patients with Alzheimer’s disease
Co-immunoprecipitation of ApoE and Aβ revealed heteromers of 18 and 16 kDa composed of ApoE fragments and Aβ in the cortex of AD patients. (A) Proteins extracted from human cortex of AD patients (Braak 6, Thal 4) were immunoprecipitated (IP) with an anti-ApoE FL or an anti-ApoE 262–293 antibody and western blotted (WB) with five anti-ApoE or anti-Aβ antibodies. The full length ApoE protein (35 kDa) was found in all samples revealed with anti-ApoE antibodies. In addition the 18, 16 and 12 kDa forms of ApoE were identified in the immunoprecipitates western blotted with appropriate anti-ApoE antibodies. The 18 and 16 kDa of these immunoprecipitates were also identified by PA3 and 6E10 antibodies as summarized in (B). The lanes illustrated in (A) have been cropped from western blots illustrated in Supplementary Fig. S3B. (C) Schematic illustration of ApoE regions involved in interaction with Aβ. In AD patients, ApoE fragments form heteromers with Aβ whose molecular weight are 18 and 16 kDa. In addition ApoE fragments of 12 kDa do not bind Aβ.
