Beta-amyloid peptide - Nicotinic acetylcholine receptor interaction: The two faces of health and disease

    Research output: Contribution to journalReview articlepeer-review

    72 Scopus citations

    Abstract

    Elevated amyloid-beta peptide (Abeta) and loss of nicotinic acetylcholine receptors (nAChRs) stand prominently in the etiology of Alzheimer's disease (AD). Since the discovery of an Abeta - nAChR interaction, much effort has been expended to understand how this interaction may contribute to normal physiological processes as well as AD. Several researchers have expanded on the initial observation of an Abeta-nAChR interaction to characterize the pertinent factors that confer Abeta sensitivity to nAChRs. Some of which include the following: 1. receptor subunit composition; 2. receptor subunit stoichiometry; 3. regional distribution; 4. presynaptic versus somatic distribution; 5. neuron versus glia expression; 6. in vitro expression system. These aspects of nAChR composition and expression appear to confer the specific functional consequences of Abeta interaction which range from blockade of receptor activation to stimulation of second messenger cascades that provide neuroprotection from Abeta toxicity. This review will discuss the extant literature on the subject in terms of clarifying this apparent dichotomy regarding the consequences of Abeta - nAChR interaction during health and disease.

    Original languageEnglish (US)
    Pages (from-to)5030-5038
    Number of pages9
    JournalFrontiers in Bioscience
    Volume12
    Issue number13
    DOIs
    StatePublished - Sep 1 2007

    Keywords

    • Alpha7
    • Alzheimer's disease
    • Amyloid
    • Cholinergic
    • Neuroprotection
    • Nicotinic
    • Review

    ASJC Scopus subject areas

    • Biochemistry, Genetics and Molecular Biology(all)
    • Immunology and Microbiology(all)

    Fingerprint

    Dive into the research topics of 'Beta-amyloid peptide - Nicotinic acetylcholine receptor interaction: The two faces of health and disease'. Together they form a unique fingerprint.

    Cite this