Research update: Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease

H. Rheinallt Parri; Caterina M. Hernandez; Kelly T. Dineley

doi:10.1016/j.bcp.2011.06.039

Research update: Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease

H. Rheinallt Parri, Caterina M. Hernandez, Kelly T. Dineley

Pharmacology and Toxicology

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

129 Scopus citations

Abstract

Aberrant amyloid-β peptide (Aβ) accumulation along with altered expression and function of nicotinic acetylcholine receptors (nAChRs) stand prominently in the etiology of Alzheimer's disease (AD). Since the discovery that Aβ is bound to α7 nAChRs under many experimental settings, including post-mortem AD brain, much effort has been expended to understand the implications of this interaction in the disease milieu. This research update will review the current literature on the α7 nAChR-Aβ interaction in vitro and in vivo, the functional consequences of this interaction from sub-cellular to cognitive levels, and discuss the implications these relationships might have for AD therapies.

Original language	English (US)
Pages (from-to)	931-942
Number of pages	12
Journal	Biochemical Pharmacology
Volume	82
Issue number	8
DOIs	https://doi.org/10.1016/j.bcp.2011.06.039
State	Published - Oct 15 2011

Keywords

Alzheimer's disease
Amyloid
Cholinergic
Neuroprotection
Oligomer
Review

ASJC Scopus subject areas

Biochemistry
Pharmacology

Access to Document

10.1016/j.bcp.2011.06.039

Fingerprint Dive into the research topics of 'Research update: Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease'. Together they form a unique fingerprint.

Cite this

@article{ddccb997eb8e44c2afe4cc1877c7b6fa,

title = "Research update: Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease",

abstract = "Aberrant amyloid-β peptide (Aβ) accumulation along with altered expression and function of nicotinic acetylcholine receptors (nAChRs) stand prominently in the etiology of Alzheimer's disease (AD). Since the discovery that Aβ is bound to α7 nAChRs under many experimental settings, including post-mortem AD brain, much effort has been expended to understand the implications of this interaction in the disease milieu. This research update will review the current literature on the α7 nAChR-Aβ interaction in vitro and in vivo, the functional consequences of this interaction from sub-cellular to cognitive levels, and discuss the implications these relationships might have for AD therapies.",

keywords = "Alzheimer's disease, Amyloid, Cholinergic, Neuroprotection, Oligomer, Review",

author = "Parri, {H. Rheinallt} and Hernandez, {Caterina M.} and Dineley, {Kelly T.}",

year = "2011",

month = oct,

day = "15",

doi = "10.1016/j.bcp.2011.06.039",

language = "English (US)",

volume = "82",

pages = "931--942",

journal = "Biochemical Pharmacology",

issn = "0006-2952",

publisher = "Elsevier Inc.",

number = "8",

}

TY - JOUR

T1 - Research update

T2 - Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease

AU - Parri, H. Rheinallt

AU - Hernandez, Caterina M.

AU - Dineley, Kelly T.

PY - 2011/10/15

Y1 - 2011/10/15

N2 - Aberrant amyloid-β peptide (Aβ) accumulation along with altered expression and function of nicotinic acetylcholine receptors (nAChRs) stand prominently in the etiology of Alzheimer's disease (AD). Since the discovery that Aβ is bound to α7 nAChRs under many experimental settings, including post-mortem AD brain, much effort has been expended to understand the implications of this interaction in the disease milieu. This research update will review the current literature on the α7 nAChR-Aβ interaction in vitro and in vivo, the functional consequences of this interaction from sub-cellular to cognitive levels, and discuss the implications these relationships might have for AD therapies.

AB - Aberrant amyloid-β peptide (Aβ) accumulation along with altered expression and function of nicotinic acetylcholine receptors (nAChRs) stand prominently in the etiology of Alzheimer's disease (AD). Since the discovery that Aβ is bound to α7 nAChRs under many experimental settings, including post-mortem AD brain, much effort has been expended to understand the implications of this interaction in the disease milieu. This research update will review the current literature on the α7 nAChR-Aβ interaction in vitro and in vivo, the functional consequences of this interaction from sub-cellular to cognitive levels, and discuss the implications these relationships might have for AD therapies.

KW - Alzheimer's disease

KW - Amyloid

KW - Cholinergic

KW - Neuroprotection

KW - Oligomer

KW - Review

UR - http://www.scopus.com/inward/record.url?scp=80052033738&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80052033738&partnerID=8YFLogxK

U2 - 10.1016/j.bcp.2011.06.039

DO - 10.1016/j.bcp.2011.06.039

M3 - Article

C2 - 21763291

AN - SCOPUS:80052033738

VL - 82

SP - 931

EP - 942

JO - Biochemical Pharmacology

JF - Biochemical Pharmacology

SN - 0006-2952

IS - 8

ER -