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REVIEW: Methionine Sulfoxide and the Oxidative Regulation of Plasma Proteinase Inhibitors
Author(s) -
Swaim Mark W.,
Pizzo Salvatore V.
Publication year - 1988
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.43.4.365
Subject(s) - methionine , oxidative phosphorylation , biology , homeostasis , inflammation , biochemistry , methionine sulfoxide , secretion , oxidative stress , methionine sulfoxide reductase , microbiology and biotechnology , immunology , amino acid
Abstract 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.