Self-oligomerization of NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer's disease amyloid, observed in the presence of a C-terminal A beta fragment (residues 25-35)

초록

NACP, the precursor protein of the non-amyloid beta/ A4 protein (A beta) component of Alzheimer's disease (AD) amyloid, also known as alpha-synuclein, was suggested to seed amyloid plaque formation in AD by stimulating A beta aggregation, We have demonstrated that NACP experienced self-oligomerization only in the presence of a modified A beta fragment (A beta 25-35) by using dicyclohexylcarbodiimide. This NACP oligomerization, appearing as a discrete ladder on a Tricine SDS-PAGE, was not observed with other A beta peptides such as the reverse peptide A beta 35-25 and A beta 1-40, indicating this process was specific not only for the C-terminal peptide sequence of the A beta but also for its orientation, It might be, therefore, suggested that the NACP self-oligomers formed only in the presence of a N-terminally truncated A beta peptide could act as a nucleation center for plaque formation during AD development, (C) 1998 Federation of European Biochemical Societies.

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