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

Abstract

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.