Singlet oxygen (1O2) Inactivates plasmatic free and complexed α2-macroglobulin

Thrombosis Research

Volumn 98, Issue 6, 2000, Pages 541-547

  Stief, Thomas W ^a   Kropf, Jürgen ^a   Kretschmer, Volker ^a   Doss, Manfred O ^a   Fareed, Jawed ^b  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b LOYOLA UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

2 macroglobulin; Fibrinolysis; Granulocytes; Inflammation; Neutrophils; Phagocytes; Singlet oxygen (1O2)

Indexed keywords

ALPHA 2 MACROGLOBULIN; HYDROGEN PEROXIDE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SINGLET OXYGEN; TOSYLCHLORAMIDE SODIUM;

ARTICLE; CONTROLLED STUDY; FIBRINOLYSIS; GRANULOCYTE; HUMAN; HUMAN CELL; INFLAMMATION; NEUTROPHIL; OXIDATION; PHAGOCYTE; PRIORITY JOURNAL;

ALPHA-MACROGLOBULINS; ANTIPLASMIN; CHLORAMINES; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; HUMANS; HYDROGEN PEROXIDE; OXYGEN; PROTEASE INHIBITORS; SINGLET OXYGEN;

EID: 0034659279     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0049-3848(00)00205-X     Document Type: Article

References (21)

1. Gils A., Declerck P.J. Structure-function relationships in serpins. Current concepts and controversies Thromb Haemost. 80:1998;531-541.
2. Roberts R.M., Mathialagan N., Duffy J.Y., Smith G.W. Regulation and regulatory role of proteinase inhibitors. Crit Rev Eukaryot Gene Expr. 5:1995;385-436.
3. Nathan C.F. Neutrophil activation on biological surfaces. Massive secretion of hydrogen peroxide in response to products of macrophages and lymphocytes. J Clin Invest. 80:1987;1550-1560.
4. Weiss S.J. Tissue destruction by neutrophils. N Engl J Med. 320:1989;365-376.
5. Rosen H., Klebanoff S.J. Formation of singlet oxygen by the myeloperoxidase-mediated antimicrobial system. J Biol Chem. 252:1977;4803-4810.
6. Kanofsky J.R. Singlet oxygen production in biological systems. Chem Biol Interact. 70:1989;1-28.
7. Hampton M.B., Kettle A.J., Winterbourn C.C. Inside the neutrophil phagosome. Oxidants, myeloperoxidase, and bacterial killing Blood. 92:1998;3007-3017.
8. Lawrence D.A., Loskutoff D.J. Inactivation of plasminogen activator inhibitor by oxidants. Biochemistry. 25:1986;6351-6355.
9. Stief T.W., Ab A., Heimburger N. Oxidative inactivation of purified human alpha-2-antiplasmin, antithrombin III, and C1-inhibitor. Thromb Res. 49:1988;581-589.
10. Stief T.W., Lenz P., Becker U., Heimburger N. Determination of plasminogen activator inhibitor (PAI) capacity of human plasma in presence of oxidants. a novel principle Thromb Res. 50:1988;559-573.
11. Stief T.W., Heimburger N. Inactivation of serine protease inhibitors (serpins) in human plasma by reactive oxidants. Biol Chem Hoppe-Seyler. 369:1988;1337-1342.
12. Reddy V.Y., Desorchers P.E., Pizzo S.V., Gonias S.L., Sahakian J.A., Levine R.L., Weiss S.J. Oxidative dissociation of human alpha2-macroglobulin tetramers into dysfunctional dimers. J Biol Chem. 269:1994;4683-4691.
13. Witko V., Nguyen A.T., Descamps-Latscha B. Microtiter plate assay for phagocyte derived taurine-chloramine. J Clin Lab Anal. 6:1992;47-53.
14. Friberger P. Chromogenic peptide substrates. Their use for the assay of factors in the fibrinolytic and plasma kallikrein-kinin systems. Scand J Clin Lab Invest. 42(Suppl 162):1982;84-85.
15. Davies K.J. Protein damage and degradation by oxygen radicals. I. General aspects. J Biol Chem. 262:1987;9895-9901.
16. Foote C.S., Clennan E.L. Properties and reactions of singlet oxygen. Foote C.S., Valentine J.S., Greenberg A., Liebman J.F. Active Oxygen in Chemistry. 1995;105-141 Blackie Academic and Professional, London.
17. Shechter Y., Burstein Y., Patchornik A. Selective oxidation of methionine residues in proteins. Biochem. 14:1975;4497-4503.
18. Gaussem P., Grailhe P., Angles-Cano E. Sodium dodecyl sulfate-induced dissociation of complexes between human tissue plasminogen activator and its specific inhibitor. J Biol Chem. 268:1993;12150-12155.
19. Lawrence D.A., Ginsburg D., Day D.E., Berkenpas M.B., Verhamme I.M., Kvassman J.O., Shore J.D. Serpin-protease complexes are trapped as stable acyl-enzyme intermediates. J Biol Chem. 270:1995;25309-25312.
20. Wilczynska M., Fa M., Ohlsson P.I., Ny T. The inhibition mechanism of serpins. Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex. J Biol Chem. 270:1995;29652-29655.
21. Stief T.W., Kurz J., Doss M.O., Fareed J. Singlet oxygen inactivates fibrinogen, factor V, factor VIII, factor X, and platelet aggregation of human blood. Thromb Res. 97:2000;473-480.