Methionine sulfoxide and the oxidative regulation of plasma proteinase inhibitors.
The sensitivity of methionine residues to oxidation is a mechanism by which many proteins, including plasma proteinase inhibitors, may be oxidatively inactivated. Much evidence suggests that methionine oxidation and concurrent losses of protein activity not only occur widely in living systems but are physiologic, homeostatic processes. Neutrophils, macrophages and other leukocytes secrete large quantities of powerful oxidants at sites of inflammation and may readily bring about methionine oxidative inactivation of proteins. In particular, oxidation of proteinase inhibitors may favorably alter the proteinase-antiproteinase balance to facilitate tissue remodeling and protection from invading organisms. Leukocyte-mediated inhibitor oxidation also appears to regulate local immunosuppressive activity. Pathophysiologic processes such as emphysema and rheumatoidal disease involve derangements of these homeostatic mechanisms.
D000818:Animals; D001665:Binding Sites; D010450:Endopeptidases / Q000097:blood*; D006801:Humans; D007962:Leukocytes / Q000201:enzymology; D008715:Methionine / Q000031:analogs & derivatives* / Q000378:metabolism; D010084:Oxidation-Reduction; D011480:Protease Inhibitors / Q000097:blood*; D012906:Smoke; D014361:Trypsin Inhibitors / Q000097:blood / Q000378:metabolism; D000515:alpha 1-Antitrypsin / Q000097:blood; D000511:alpha-Macroglobulins / Q000378:metabolism
D011480:Protease Inhibitors; D012906:Smoke; D014361:Trypsin Inhibitors; D000515:alpha 1-Antitrypsin; D000511:alpha-Macroglobulins; D008715:Methionine; D010450:Endopeptidases; C013111:methionine sulfoxide