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Tytuł artykułu

Collagen type II modification by hypochlorite

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Oxidation of proteins is a common phenomenon in the inflammatory process medi­ated by highly reactive agents such as hypochlorite (HOCl/OCl-) produced by acti­vated neutrophils. For instance, in rheumatoid arthritis hypochlorite plays an impor­tant role in joint destruction. One of the major targets for HOCl/OCl- is collagen type II (CII) — the primary cartilage protein. In our study, HOCl/OCl- mediated collagen II modifications were tested using various methods: circular dichroism (CD), HPLC, ELISA, dynamic light scattering (DLS), fluorimetry and spectrophotometry. It was shown that hypochlorite action causes deamination with consecutive carbonyl group formation and transformation of tyrosine residues to dichlorotyrosine. Moreover, it was shown that ammonium chloramine (NH^Cl) formed in the reaction mixture reacts with CII. However, in this case the yield of carbonyl groups and dichlorotyrosine is lower than that observed for HOCl/OCl- by 50%. CD data revealed that collagen II ex­ists as a random coil in the samples and that chlorination is followed by CII fragmenta­tion. In the range of low HOCl/OCl- concentrations (up to 1 mM) 10-90 kDa peptides are predominant whereas massive production of shorter peptides was observed for high (5 mM) hypochlorite concentration. DLS measurements showed that chlorina- tion with HOCl/OCl- decreases the radius of collagen II aggregates from 30 to 6.8 nm. Taking into account the fact that chlorinated collagen is partially degraded, the DLS results suggest that smaller micelles are formed of the 10-90 kDa peptide fraction. Moreover, collagen chlorination results in epitope modification which affects CII rec­ognition by anti-CII antibodies. Finally, since in the synovial fluid the plausible hypochlorite concentration is smaller than that used in the model the change of size of molecular aggregates seems to be the best marker of hypochlorite-mediated collagen oxidation.

Wydawca

-

Rocznik

Tom

50

Numer

2

Opis fizyczny

p.471-479,fig.

Twórcy

autor
  • Collegium Medicum, Jagiellonian University, Czysta 18, 31-121 Krakow, Poland
autor
autor

Bibliografia

  • Davies KJA, Delsignore ME, Lin SW. (1987) Protein damage and degradation by oxygen radicals II. Primary structure. J Biol Chem.; 262: 9902-7.
  • Davies JMS, Horwittz DA, Davies KJL. (1993) Potential roles of hypochlorous acid and N-chloramines in collagen breakdown by phagocytic cells in synovitis. Free Radic Biol Med.; 15: 637-43.
  • Edwards SW, Hallett MB. (1997) Seeing the wood for the trees: the forgotten role of neutrophils in rheumatoid arthritis. Immunol Today.; 18: 320-4.
  • Hampton MB, Kettle AJ, Winterbourn CC. (1998) Inside the neutrophil phagosome: oxidants, myeloperoxidase and bacterial killing. Blood.; 92: 3007-17.
  • Kettle AJ. (1996) Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBSLett.; 379: 103-6.
  • Kwasny-Krochin B, Bobek M, Kontny E, Gluszko P, Biedron R, Chain BM, Maslinski W, Marcinkiewicz J. (2002) Effect of taurine chloramine. The product of activated neutrophils, on the development of collagen-induced arthritis in DBA 1/J mice. Amino Acids.; 23: 419-26.
  • Marcinkiewicz J, Chain BM, Olszowska E, Olszowski S, Zgliczynski JM. (1991) Enhancement of immunogenic properties of ovalbumin as a result of its chlorination. Int JBiochem.; 23: 1393-5.
  • Marcinkiewicz J, Olszowska E, Olszowski S, Zgliczynski JM. (1992) Enhancement of trinitrophenyl — specific humoral response to TNP proteins as a result of carrier chlorination. Immunology.; 76: 385-8.
  • Oliver CN. (1987) Inactivation of enzymes and oxidative modification of proteins by stimulated neutrophils. Arch Biochem Biophys.; 253: 62-72.
  • Olszowski S, Olszowska E, Stelmaszynska T, Kursa A. (1994) Influence of native and oxidized proteins on tumour necrosis factor preactivated PMN leukocytes. Anal Chim Acta.; 290: 186-9.
  • Olszowski S, Olszowska E, Stelmaszynska T, Krawczyk A, Marcinkiewicz J, Baczek N. (1996) Oxidative modification of albumin. Acta Biochim Polon.; 43: 661-72.
  • Rudie NG, Porter DJT, Bright HJ. (1980) Chlorination of an active site tyrosyl residue in D-amino-acid oxidase by N- chloro-D-leucine. J Biol Chem.; 255: 498-508.
  • Stelmaszynska T, Zgliczynski JM. (1978) N-(2Oxoacyl)-amino acids and nitryles as final products of dipeptyde chlorination mediated by the myeloperoxidase-H2O2Cl- system. Eur J Biochem.; 92: 301-8.
  • Vissers MCM, Winterbourn CC. (1991) Oxidative damage to fibronectin. I. The effects of the myeloperoxidase system and HOCl. Arch Biochem Biophys.; 285: 53-9.
  • Weiss SJ, Slivka A, Wei M. (1982) Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J Clin Invest.; 70: 598-607.
  • Weiss SJ, Lampert MB, Test ST. (1983) Long-lived oxidants generated by human neutrophils. Characterisation and bioactivity. Science.; 222: 625-8.

Typ dokumentu

Bibliografia

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