The amino-terminus of the amyloid-β protein is critical for the cellular binding and consequent activation of the respiratory burst of human macrophages

• Published in: Journal of neuroimmunology 1999-04, Vol.96 (1), p.121-130
• Main Authors: Van Muiswinkel, Freek L, Raupp, Sigrid F.A, de Vos, N.Machiel, Smits, Hessel A, Verhoef, Jan, Eikelenboom, Piet, Nottet, Hans S.L.M
• Format: Article
• Language: English
• Subjects: Alzheimer Disease - immunology; Alzheimer Disease - metabolism; Alzheimer's disease; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - metabolism; Amyloid beta-Peptides - pharmacology; Amyloid-β peptide; Binding, Competitive - drug effects; Binding, Competitive - immunology; Brain Chemistry - immunology; Chemiluminescence; Flow Cytometry; Fluorescein-5-isothiocyanate; Fluorescent Dyes; Human macrophages; Humans; Luminescent Measurements; Macrophages - chemistry; Macrophages - immunology; Macrophages - metabolism; Monocytes - chemistry; Monocytes - immunology; Monocytes - metabolism; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Peptide Fragments - pharmacology; Protein Binding - immunology; Respiratory Burst - drug effects; Respiratory Burst - immunology; Respiratory burst activity; Superoxides - metabolism
• ISSN: 0165-5728; 1872-8421
• DOI: 10.1016/S0165-5728(99)00019-3

Here, we show that amyloid-β (Aβ) is capable to prime and activate the respiratory burst of human macrophages. Previously, the N-terminus of Aβ(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 Aβ(1–42)-induced respiratory burst activity, the effect of Aβ subfragments on the Aβ(1–42)-induced superoxide release were studied. On the basis of the antagonistic properties of Aβ(1–16), it is concluded that the N-terminal region of Aβ is critical for the cellular binding and consequent activation of the respiratory burst of human phagocytes.