Tissues identified as containing abnormal PrP and/or infectivity in clinical and subclinical vCJD patients.

<p>Tissues identified as containing abnormal PrP and/or infectivity in clinical and subclinical vCJD patients.</p

Summary of the appendix survey results.

<p>Summary of the appendix survey results.</p

Ablation of PrP^C does not affect Aβ deposition in APP_WT mice.

<p>Histopathologic analysis of the hippocampus of hematoxylin-eosin stained sections of WT, APP_WT/PrP⁺⁺ and APP_WT/PrP^-- mice show absence of obvious alterations in the pyramidal cell layer, stratum oriens and lacunosum-molecular (A, D and G). No Aβ deposits are seen in sections probed with antibody 4G8 (B, E and H) or antibody OC (C, F and I). In contrast, APP_Swe,Ind/PrP^+/+ mice show plaques (arrows) in sections stained with hematoxylin-eosin (J) and abundant Aβ-reactive deposits in sections probed with antibody 4G8 (K) and OC (L). All images x20 magnification and scale bar = 100μm.</p

Ablation of PrP^C does not affect APP proteolysis or Aβ peptide levels in APP_WT mice.

<p>Brain hemispheres from 32 week and 75 week old APP_WT/PrP^+/+ and APP_WT/PrP^-/- mice were subjected to two-step homogenisation, and the soluble proteins (SDS extracted) were subjected to SDS-PAGE and immunoblotting. (A) representative immunoblots of PrP^C and APP, with actin as a loading control. (B) Soluble (SDS extracted) sAPPα and sAPPβ detected by MSD ELISA and (C) the ratio of sAPPα to sAPPβ. (D) Soluble (SDS extracted) Aβ_38, Aβ₄₀ and Aβ₄₂ detected by MSD ELISA and (E) the ratio of Aβ₄₂ to Aβ₄₀. Data shown as mean ± SEM (n = 3–6). There was no significant difference between the APP_WT/PrP^+/+ and APP_WT/PrP^-/- at the same time point for any of the APP or Aβ peptides.</p