Peripheral clearance of amyloid β peptide by complement C3-dependent adherence to erythrocytes

Joseph Rogers; Rena Li; Diego Mastroeni; Andrew Grover; Brian Leonard; Geoffrey Ahern; Phillip Cao; Heather Kolody; Linda Vedders; William P. Kolb; Marwan Sabbagh

doi:10.1016/j.neurobiolaging.2005.09.043

Peripheral clearance of amyloid β peptide by complement C3-dependent adherence to erythrocytes

Joseph Rogers, Rena Li, Diego Mastroeni, Andrew Grover, Brian Leonard, Geoffrey Ahern, Phillip Cao, Heather Kolody, Linda Vedders, William P. Kolb, Marwan Sabbagh

Research output: Contribution to journal › Article › peer-review

141 Scopus citations

Abstract

Brain deposits of amyloid β peptide (Aβ) have been a diagnostic hallmark of Alzheimer's disease (AD) for nearly a century. Recent studies have demonstrated that Aβ is also present in peripheral blood. Here, we present evidence that circulating Aβ42 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 Aβ42 targeted by this pathway differ significantly in AD compared to mild cognitive impairment and nondemented elderly controls.

Original language	English (US)
Pages (from-to)	1733-1739
Number of pages	7
Journal	Neurobiology of Aging
Volume	27
Issue number	12
DOIs	https://doi.org/10.1016/j.neurobiolaging.2005.09.043
State	Published - Dec 2006
Externally published	Yes

Keywords

Alzheimer's disease
Amyloid β peptide
Blood
Clearance
Complement

ASJC Scopus subject areas

Clinical Neurology
Geriatrics and Gerontology
Aging
General Neuroscience
Developmental Biology

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10.1016/j.neurobiolaging.2005.09.043

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title = "Peripheral clearance of amyloid β peptide by complement C3-dependent adherence to erythrocytes",

abstract = "Brain deposits of amyloid β peptide (Aβ) have been a diagnostic hallmark of Alzheimer's disease (AD) for nearly a century. Recent studies have demonstrated that Aβ is also present in peripheral blood. Here, we present evidence that circulating Aβ42 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 Aβ42 targeted by this pathway differ significantly in AD compared to mild cognitive impairment and nondemented elderly controls.",

keywords = "Alzheimer's disease, Amyloid β peptide, Blood, Clearance, Complement",

author = "Joseph Rogers and Rena Li and Diego Mastroeni and Andrew Grover and Brian Leonard and Geoffrey Ahern and Phillip Cao and Heather Kolody and Linda Vedders and Kolb, {William P.} and Marwan Sabbagh",

note = "Funding Information: We thank Dr. Neil Cooper, Dr. Andrea Tenner, Ms. Bonnie Bradt, Dr. Alexander Roher, Dr. Paul Coleman, and Dr. Douglas Walker for technical advice, and Dr. Steven Snyder for his encouragement. This research was supported directly by NIA AGO7367, and indirectly by NIA P30 AG19610 and the Arizona Alzheimer's Research Consortium.",

year = "2006",

month = dec,

doi = "10.1016/j.neurobiolaging.2005.09.043",

language = "English (US)",

volume = "27",

pages = "1733--1739",

journal = "Neurobiology of Aging",

issn = "0197-4580",

publisher = "Elsevier Inc.",

number = "12",

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TY - JOUR

T1 - Peripheral clearance of amyloid β peptide by complement C3-dependent adherence to erythrocytes

AU - Rogers, Joseph

AU - Li, Rena

AU - Mastroeni, Diego

AU - Grover, Andrew

AU - Leonard, Brian

AU - Ahern, Geoffrey

AU - Cao, Phillip

AU - Kolody, Heather

AU - Vedders, Linda

AU - Kolb, William P.

AU - Sabbagh, Marwan

N1 - Funding Information: We thank Dr. Neil Cooper, Dr. Andrea Tenner, Ms. Bonnie Bradt, Dr. Alexander Roher, Dr. Paul Coleman, and Dr. Douglas Walker for technical advice, and Dr. Steven Snyder for his encouragement. This research was supported directly by NIA AGO7367, and indirectly by NIA P30 AG19610 and the Arizona Alzheimer's Research Consortium.

PY - 2006/12

Y1 - 2006/12

N2 - Brain deposits of amyloid β peptide (Aβ) have been a diagnostic hallmark of Alzheimer's disease (AD) for nearly a century. Recent studies have demonstrated that Aβ is also present in peripheral blood. Here, we present evidence that circulating Aβ42 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 Aβ42 targeted by this pathway differ significantly in AD compared to mild cognitive impairment and nondemented elderly controls.

AB - Brain deposits of amyloid β peptide (Aβ) have been a diagnostic hallmark of Alzheimer's disease (AD) for nearly a century. Recent studies have demonstrated that Aβ is also present in peripheral blood. Here, we present evidence that circulating Aβ42 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 Aβ42 targeted by this pathway differ significantly in AD compared to mild cognitive impairment and nondemented elderly controls.

KW - Alzheimer's disease

KW - Amyloid β peptide

KW - Blood

KW - Clearance

KW - Complement

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U2 - 10.1016/j.neurobiolaging.2005.09.043

DO - 10.1016/j.neurobiolaging.2005.09.043

M3 - Article

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AN - SCOPUS:33750031006

SN - 0197-4580

VL - 27

SP - 1733

EP - 1739

JO - Neurobiology of Aging

JF - Neurobiology of Aging

IS - 12

ER -

Peripheral clearance of amyloid β peptide by complement C3-dependent adherence to erythrocytes

Abstract

Keywords

ASJC Scopus subject areas

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