Figure 1
From: Heteromers of amyloid precursor protein in cerebrospinal fluid
Soluble full-length APP (sAPPf) is present in human CSF. (A) Schematic representation of full-length APP processing by α/γ-secretase (non-amyloidogenic pathway) and β/γ-secretase (amyloidogenic pathway) and the generation of extracellular large sAPPα, sAPPβ fragments, and the shorter Aβ and p3 peptides; as well as fragments containing the C-terminal APP (CTF and ICD) (not drawn in scale). The epitopes for the anti-APP antibodies used in this study are indicated. (B) Western blotting of human CSF samples from non-demented controls (NDC) subjects, resolved with the indicated anti-APP antibodies. (C, D) CSF aliquots (Total, T) were immunoprecipitated with either the anti-C-terminal APP antibody from Sigma (C, Sigma-Ct) or the pan-specific IBL-β antibody (D, IBL-β). Precipitated proteins (bound fraction, B) were immunoblotted with the antibodies as indicated. In the absence of capture-antibody (IPc), no bands were observed.