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

Here, we show that amyloid-beta (A beta) is capable to prime and activate t he respiratory burst of human macrophages. Previously, the N-terminus of A beta(1-42) has been shown to contain a cell binding domain that is implicat ed in eliciting neuropathogenic microglia in vitro. To evaluate the role of this domain in the A beta(1-42)-induced respiratory burst activity, the ef fect of A beta subfragments on the A beta(1-42)-induced superoxide release were studied. On the basis of the antagonistic properties of A beta(1-16), it is concluded that the N-terminal region of A beta is critical for the ce llular binding and consequent activation of the respiratory burst of human phagocytes. (C) 1999 Elsevier Science B.V. All rights reserved.