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Different Configurational States of β-Amyloid and Their Distributions Relative to Plaques and Tangles in Alzheimer Disease
Ist Teil von
Proceedings of the National Academy of Sciences - PNAS, 1990-05, Vol.87 (10), p.3947-3951
Ort / Verlag
Washington, DC: National Academy of Sciences of the United States of America
Erscheinungsjahr
1990
Link zum Volltext
Quelle
MEDLINE
Beschreibungen/Notizen
Antibodies have been raised against synthetic peptides corresponding to different parts of the β-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 β-amyloid molecules. An antibody directed against the middle region of β-amyloid stained mostly amyloid plaques without cores, whereas an antibody directed against the carboxyl-terminal region of β-amyloid stained only amyloid plaques with cores. An antiserum directed against the amino terminus of β-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.