Abstract
Here, we show that amyloid-beta (Abeta) is capable to prime and activate the respiratory burst of human macrophages. Previously, the N-terminus of Abeta(1-42) has been shown to contain a cell binding domain that is implicated in eliciting neuropathogenic microglia in vitro. To evaluate the role of this domain in the Abeta(1-42)-induced respiratory burst activity, the effect of Abeta subfragments on the Abeta(1-42)-induced superoxide release were studied. On the basis of the antagonistic properties of Abeta(1-16), it is concluded that the N-terminal region of Abeta is critical for the cellular binding and consequent activation of the respiratory burst of human phagocytes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alzheimer Disease / immunology
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Alzheimer Disease / metabolism
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Amyloid beta-Peptides / chemistry*
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Amyloid beta-Peptides / metabolism
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Amyloid beta-Peptides / pharmacology*
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Binding, Competitive / drug effects
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Binding, Competitive / immunology
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Brain Chemistry / immunology
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Flow Cytometry
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Fluorescein-5-isothiocyanate
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Fluorescent Dyes
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Humans
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Luminescent Measurements
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Macrophages / chemistry
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Macrophages / immunology*
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Macrophages / metabolism*
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Monocytes / chemistry
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Monocytes / immunology
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Monocytes / metabolism
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Peptide Fragments / chemistry*
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Peptide Fragments / metabolism
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Peptide Fragments / pharmacology*
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Protein Binding / immunology
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Respiratory Burst / drug effects
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Respiratory Burst / immunology*
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Superoxides / metabolism
Substances
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Amyloid beta-Peptides
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Fluorescent Dyes
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Peptide Fragments
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amyloid beta-protein (1-11)
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amyloid beta-protein (1-42)
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amyloid beta-protein (25-35)
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Superoxides
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Fluorescein-5-isothiocyanate