Abstract

ROS, including .OH, is now recognized as the hallmark of inflammation and damage to the anti-proteinase barrier has been implicated in a number of pathophysiological conditions. We have previously shown that O2 .- and H2O2/HOCl are physiologically relevant inactivators of α2M, a key anti-proteinase. Here, we show that .OH disrupted caprine α2M structure and antiproteolytic potential in vitro, suggesting that its function could be compromised via oxidative modification.

Keywords: Caprine, alpha-2-macroglobulin, hydroxyl radical