Open AccessDifferent configurational states of beta-amyloid and their distributions relative to plaques and tangles in Alzheimer disease.
Author(s) -
Maria Grazia Spillantini,
Michel Goedert,
Ross Jakes,
A. Klug
Publication year - 1990
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.87.10.3947
Subject(s) - senile plaques , tangle , amyloid (mycology) , biochemistry of alzheimer's disease , antibody , alzheimer's disease , beta (programming language) , neurofibrillary tangle , chemistry , pathology , amyloid beta , amyloid precursor protein , microbiology and biotechnology , biology , peptide , biochemistry , medicine , immunology , disease , mathematics , computer science , pure mathematics , programming language
Antibodies have been raised against synthetic peptides corresponding to different parts of the beta-amyloid sequence. These antibodies stain different kinds of amyloid distributions in the hippocampal formation in Alzheimer disease, suggesting the existence of different states of aggregation and/or folding of beta-amyloid molecules. An antibody directed against the middle region of beta-amyloid stained mostly amyloid plaques without cores, whereas an antibody directed against the carboxyl-terminal region of beta-amyloid stained only amyloid plaques with cores. An antiserum directed against the amino terminus of beta-amyloid stained numerous tangle-bearing cells and bodies, as well as the neuritic component of plaques and neuropil threads. These antibodies, in conjunction with anti-tau antibodies, were used to demonstrate a close spatial relationship between amyloid deposits and neurofibrillary tangles.