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P4‐206: Glutamatergic receptors in the neocortex of Vascular Dementia (VaD) and Mixed Dementia (MIX)
Author(s) -
Mohamed NurEzan,
Lee Jasinda,
Esiri Margaret M.,
Lai Mitchell K.P.,
Chen Christopher P.
Publication year - 2009
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2009.04.672
Subject(s) - ampa receptor , dementia , neocortex , glutamatergic , vascular dementia , neuroscience , alzheimer's disease , nmda receptor , medicine , psychology , glutamate receptor , receptor , disease
in our laboratory. These preparations were characterized for their content in SDS resistant species, binding to thioflavin, aggregation kinetics, ultrastructure and toxicity. They were classified as: i) non-toxic monomers; ii) toxic and amyloidogenic oligomers; iii) highly toxic and highly amyloidogenic oligomers. Monomeric Ab samples were non-toxic and incapable of membrane binding; the restoration of Ab toxicity reestablished the binding activity. Conclusions: We have confirmed that Ab oligomers bind to proteins of cell membranes. This binding was structure-dependent since it only happened when Ab was in an oligomeric form. This approach enabled us to isolate membrane proteins that may be involved in the triggering of Ab140/42 toxicity.