Peripheral clearance of amyloid beta peptide by complement C3-dependent adherence to erythrocytes.
Brain deposits of amyloid beta peptide (Abeta) have been a diagnostic hallmark of Alzheimer's disease (AD) for nearly a century. Recent studies have demonstrated that Abeta is also present in peripheral blood. Here, we present evidence that circulating Abeta42 is subject to complement C3b-dependent adherence to complement receptor 1 (CR1) on erythrocytes, a classical set of mechanisms by which pathogens and proteins recognized as foreign are cleared from the bloodstream. Levels of Abeta42 targeted by this pathway differ significantly in AD compared to mild cognitive impairment and nondemented elderly controls.
Rogers
Joseph
J
L.J. Roberts Center for Alzheimer's Research, Sun Health Research Institute, 10515 West Santa Fe Drive, P.O. Box 1278, Sun City, AZ 85372, USA. joseph.rogers@sunhealth.org <joseph.rogers@sunhealth.org>
Li
Rena
R
Mastroeni
Diego
D
Grover
Andrew
A
Leonard
Brian
B
Ahern
Geoffrey
G
Cao
Phillip
P
Kolody
Heather
H
Vedders
Linda
L
Kolb
William P
WP
Sabbagh
Marwan
M
D000544:Alzheimer Disease / Q000097:blood; D016229:Amyloid beta-Peptides / Q000097:blood*; D002448:Cell Adhesion / Q000276:immunology; D003176:Complement C3 / Q000502:physiology*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D010446:Peptide Fragments / Q000097:blood*; D021381:Protein Transport / Q000276:immunology
D016229:Amyloid beta-Peptides; D003176:Complement C3; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)