Association of the carboxy-terminus of beta-amyloid protein precursor with Alzheimer paired helical filaments.
We investigated whether a peptide fragment from the C-terminus of beta-amyloid protein precursor is associated with Alzheimer paired helical filaments (PHFs). Antiserum BR188, to the last 20 amino acids of the precursor, did not cross-react with tau protein, known to be in PHFs. It did react with all five pronase-treated PHF preparations assayed by ELISA and immunogold-labelled the same PHF fibrils that a PHF-specific tau antibody labelled. Neither antibody labelled beta/A4 fibrils. These results suggest that a fragment from the C-terminus of beta-amyloid precursor protein copurifies with pronase-treated PHFs and may play a role in their molecular pathogenesis.
Caputo
C B
CB
Pharmacology Department, ICI Pharmaceuticals Group, ICI Americas, Wilmington, DE 19897.
Sobel
I R
IR
Scott
C W
CW
Brunner
W F
WF
Barth
P T
PT
Blowers
D P
DP
D008841:Actin Cytoskeleton / Q000648:ultrastructure*; D000544:Alzheimer Disease / Q000473:pathology*; D016564:Amyloid beta-Protein Precursor / Q000032:analysis*; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007074:Immunoglobulin G; D016253:Microscopy, Immunoelectron; D010446:Peptide Fragments / Q000032:analysis*
D016564:Amyloid beta-Protein Precursor; D007074:Immunoglobulin G; D010446:Peptide Fragments