Hydroxyl radical mediates oxidative modification of caprine alpha-2 macroglobulin.
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 alpha 2M, a key anti-proteinase. Here, we show that (.)OH disrupted caprine alpha2M structure and antiproteolytic potential in vitro, suggesting that its function could be compromised via oxidative modification.
Khan
Shakil A
SA
Department of Biochemistry, Aligarh Muslim University, Aligarh - 202002, India.
Khan
Fahim H
FH
D000818:Animals; D000975:Antioxidants / Q000494:pharmacology; D006041:Goats; D017665:Hydroxyl Radical / Q000737:chemistry*; D010084:Oxidation-Reduction; D011480:Protease Inhibitors / Q000737:chemistry; D014357:Trypsin / Q000378:metabolism; D000511:alpha-Macroglobulins / Q000737:chemistry* / Q000378:metabolism
D000975:Antioxidants; D011480:Protease Inhibitors; D000511:alpha-Macroglobulins; D017665:Hydroxyl Radical; D014357:Trypsin