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Different configurational states of beta-amyloid and their distributions relative to plaques and tangles in Alzheimer disease.

1990; National Academy of Sciences; Volume: 87; Issue: 10 Linguagem: Inglês

10.1073/pnas.87.10.3947

1091-6490

Maria Grazia Spillantini, Michel Goedert, Ross Jakes, A. Klug,

Aluminum toxicity and tolerance in plants and animals

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.