Methionine sulfoxide and the oxidative regulation of plasma proteinase inhibitors.

Published

Journal Article (Review)

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.

Full Text

Duke Authors

Cited Authors

  • Swaim, MW; Pizzo, SV

Published Date

  • April 1, 1988

Published In

Volume / Issue

  • 43 / 4

Start / End Page

  • 365 - 379

PubMed ID

  • 2450941

Pubmed Central ID

  • 2450941

International Standard Serial Number (ISSN)

  • 0741-5400

Digital Object Identifier (DOI)

  • 10.1002/jlb.43.4.365

Language

  • eng

Conference Location

  • United States