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Enhanced aggregation and β structure of amyloid β peptide after coincubation with C1Q

✍ Scribed by S. Webster; S. O'Barr; Dr. J. Rogers

Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
897 KB
Volume
39
Category
Article
ISSN
0360-4012

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✦ Synopsis

Several lines of evidence now suggest that aggregation of soluble amyloid P peptide (AD) into a cross P sheet configuration may be an important factor in mediating potential neurotoxicity of AP. Synthetic AP has been shown to self aggregate in vitro. Here, we demonstrate that coincubation of freshly solubilized AP with Clq, a complement component known to bind AP in vitro and to colocalize with AP in vivo, results in as much as a 7-fold enhancement of AP aggregation, as well as a 2 4 f o l d enhancement of P structure within aggregates. The addition of Clq to preformed AP aggregates also results in significantly increased resistance to aggregate resolubilization.

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