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2003 | 50 | 3 | 753-763

Article title

Properties of chemically oxidized kininogens.

Content

Title variants

Languages of publication

EN

Abstracts

EN
Kininogens are multifunctional proteins involved in a variety of regulatory processes including the kinin-formation cascade, blood coagulation, fibrynolysis, inhibition of cysteine proteinases etc. A working hypothesis of this work was that the properties of kininogens may be altered by oxidation of their methionine residues by reactive oxygen species that are released at the inflammatory foci during phagocytosis of pathogen particles by recruited neutrophil cells. Two methionine-specific oxidizing reagents, N-chlorosuccinimide (NCS) and chloramine-T (CT), were used to oxidize the high molecular mass (HK) and low molecular mass (LK) forms of human kininogen. A nearly complete conversion of methionine residues to methionine sulfoxide residues in the modified proteins was determined by amino acid analysis. Production of kinins from oxidized kininogens by plasma and tissue kallikreins was significantly lower (by at least 70%) than that from native kininogens. This quenching effect on kinin release could primarily be assigned to the modification of the critical Met-361 residue adjacent to the internal kinin sequence in kininogen. However, virtually no kinin could be formed by human plasma kallikrein from NCS-modified HK. This observation suggests involvement of other structural effects detrimental for kinin production. Indeed, NCS-oxidized HK was unable to bind (pre)kallikrein, probably due to the modification of methionine and/or tryptophan residues at the region on the kininogen molecule responsible for the (pro)enzyme binding. Tests on papain inhibition by native and oxidized kininogens indicated that the inhibitory activity of kininogens against cysteine proteinases is essentially insensitive to oxidation.

Year

Volume

50

Issue

3

Pages

753-763

Physical description

Dates

published
2003
received
2003-05-30
revised
2003-08-01
accepted
2003-08-11

Contributors

  • Faculty of Biotechnology, Jagiellonian University, Kraków, Poland
author
  • Faculty of Biotechnology, Jagiellonian University, Kraków, Poland
  • Faculty of Biotechnology, Jagiellonian University, Kraków, Poland
author
  • Faculty of Biotechnology, Jagiellonian University, Kraków, Poland
author
  • Faculty of Biotechnology, Jagiellonian University, Kraków, Poland

References

  • Babior BM. (1978) Oxygen-dependent microbial killing by phagocytes. N Engl J Med.; 298: 659-68.
  • Bhoola KD, Figueroa CD, Worthy K. (1992) Bioregulation of kinins: kallikreins, kininogens and kininases. Pharmacol Rev.; 44: 1-80.
  • Cohen SA, Meys M, Tarvin TL. (1989) The pico-Tag methods. Millipore Corporation, Bed- ford.
  • Colman RW. (1994) Structure-function correlates of human high molecular weight kininogen. Braz J Med Biol Res.; 27: 1839-53.
  • Colman RW, Schmaier AH. (1997) Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood.; 90: 3819-43.
  • Houghten RA, Li CH. (1976) Studies on pitu- itary prolactin. 39. Reaction of the ovine hormone with hydrogen peroxide. Biochim Biophys Acta.; 439: 240-9.
  • Hong B-S, Yang MCM, Liang JN, Pang PKT. (1986) Correlation of structural changes in parathyroid hormone with its vascular action. Peptides.; 7: 1131-5.
  • Imamura T, Tanase S, Hayashi I, Potempa J, Kozik A, Travis J. (2002) Release of a new vascular permeability enhancing peptide from kininogens by human neutrophil elastase. Biochem Biophys Res Commun.; 294: 423-8.
  • Johnson D, Travis J. (1979) The oxidative inactivation of human α1-proteinase inhibitor. Further evidence for methionine at the reactive center. J Biol Chem.; 254: 4022-6.
  • Joseph K, Gheberhiwet B, Kaplan A. (2001) Activation of the kinin- forming cascade on the surface of the endothelial cells. Biol Chem.; 382: 71-5.
  • Kozik A, Moore RB, Potempa J, Imamura T, Rapala-Kozik M, Travis J. (1998) A novel mechanism for bradykinin production at inflammatory sites. Diverse effects of a mixture of neutrophil elastase and mast cells tryptase versus tissue and plasma kallikreins on native and oxidized kininogens. J Biol Chem.; 273: 33224-9.
  • Li Y, Ferrante A, Poulos A, Harvey DP. (1996) Neutrophil oxygen radical generation. J Clin Invest.; 97: 1605-9.
  • Margolius HS (1998) Tissue kallikrein. Structure, regulation, and participation in mammalian physiology and disease. Clin Rev Allergy Immunol.; 16: 337-49.
  • Ossanna PJ, Test ST, Matheson NR, Regiani S, Weiss SJ. (1986) Oxidative regulation on neutrophil elastase-alpha-1-proteinase inhibitor interactions. J Clin Invest.; 77: 1939-51.
  • Reddy VY, Desrochers PE, Pizzo SV, Gonias SL, Sahakian JA, Levine RL, Weiss SJ. (1994) Oxidative dissociation of human α2-macroglobulin tetramers into dysfunctional dimers. J Biol Chem; 269: 4683-91.
  • Sato F, Nagasawa S. (1988) Mechanism of kinin release from human low-lecular-mass-kininogen by the synergistic action of human plasma kallikrein and leukocyte elastase. Biol Chem Hoppe Seyler.; 369: 1009-17.
  • Schechter Y, Burstein Y, Patchornik A. (1975) Selective oxidation of methionine residues in proteins. Biochemistry.; 14: 4497-503.
  • Swaim MW, Pizzo SV. (1988) Methionine sulfoxide and the oxidative regulation of plasma proteinase inhibitors. J Leukoc Biol.; 43: 365-79.
  • Teh L-C, Murphy LJ, Huq NL, Surus AS, Friesen HG, Lazarus L, Chapman GE. (1987) Methionine oxidation in human growth hormone and human chorionic somatomammotropin. J Biol Chem.; 262: 6472-7.
  • Vogt W. (1995) Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic Biol Med.; 18: 93-105.
  • Vogt W, Zimmermann B, Hesse D, Nolte R. (1992) Activation of the fifth component of human complement, without cleavage, by methionine oxidizing agents. Mol Immunol.; 29: 251-56.

Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv50i3p753kz
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