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P3‐413: Reduction of amyloid‐beta formation towards Alzheimer's disease immunotherapy
Author(s) -
Solomon Beka
Publication year - 2010
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.2010.05.1956
Subject(s) - internalization , amyloid precursor protein , genetically modified mouse , antibody , amyloid precursor protein secretase , extracellular , intracellular , endosome , transgene , p3 peptide , microbiology and biotechnology , amyloid beta , chemistry , alpha secretase , amyloid (mycology) , in vivo , alzheimer's disease , biochemistry , peptide , cell , biology , immunology , disease , medicine , pathology , gene , inorganic chemistry
impairment of cognitive function. Conclusions: Our studies provide strong evidence that the N-termini of amyloid peptides influence their characteristics. This is primarily caused by a loss of N-terminal charge and solubility which increases aggregation propensity and, interestingly, influence on LTP. Likewise, novel transgenic animal models overproducing N-truncated Abeta develop an early phenotype. Thus, an accumulation of N-truncated amyloid as described for human AD might contribute to the pathogenesis due to the changes in the molecular properties. The data suggest that suppression of QC-catalyzed pGlu-formation provides potential for development of a treatment paradigm to prevent Aband inflammation-driven pathophysiology in AD, FDD and FBD.