Enhanced aggregation and beta structure of amyloid beta peptide after coincubation with C1q.
Several lines of evidence now suggest that aggregation of soluble amyloid beta peptide (A beta) into a cross beta sheet configuration may be an important factor in mediating potential neurotoxicity of A beta. Synthetic A beta has been shown to self aggregate in vitro. Here, we demonstrate that coincubation of freshly solubilized A beta with C1q, a complement component known to bind A beta in vitro and to colocalize with A beta in vivo, results in as much as a 7-fold enhancement of A beta aggregation, as well as a 2-4-fold enhancement of beta structure within aggregates. The addition of C1q to preformed A beta aggregates also results in significantly increased resistance to aggregate resolubilization.
Webster
S
S
L.J. Roberts Center, Sun Health Research Institute, Sun City, Arizona 85372.
O'Barr
S
S
Rogers
J
J
D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D000704:Analysis of Variance; D052160:Benzothiazoles; D015922:Complement C1q / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D003224:Congo Red; D004591:Electrophoresis, Polyacrylamide Gel; D005456:Fluorescent Dyes; D012995:Solubility; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013844:Thiazoles
D016229:Amyloid beta-Peptides; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D013844:Thiazoles; C009462:thioflavin T; D003224:Congo Red; D015922:Complement C1q