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Titolo:
A novel mechanism for bradykinin production at inflammatory sites - Diverse effects of a mixture of neutrophil elastase and mast cell tryptase versustissue and plasma kallikreins on native and oxidized kininogens
Autore:
Kozik, A; Moore, RB; Potempa, J; Imamura, T; Rapala-Kozik, M; Travis, J;
Indirizzi:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Biochem & Mol Biol, Athens, GA 30602 USA Jagiellonian Univ, Inst Mol Biol, PL-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 l Biol, PL-31120 Krakow, Poland Kumamoto Univ, Grad Sch Med Sci, Div Mol Pathol, Kumamoto 860, Japan Kumamoto Univ Kumamoto Japan 860 ci, Div Mol Pathol, Kumamoto 860, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 50, volume: 273, anno: 1998,
pagine: 33224 - 33229
SICI:
0021-9258(199812)273:50<33224:ANMFBP>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN ALPHA-1-PROTEINASE INHIBITOR; GINGIVAL CREVICULAR FLUID; RHEUMATOID-ARTHRITIS; SYNOVIAL-FLUID; PERIODONTITIS PATIENTS; GRANULOCYTE ELASTASE; BRONCHIAL LAVAGE; ACTIVATION; RELEASE; BRONCHOALVEOLAR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
73
Recensione:
Indirizzi per estratti:
Indirizzo: Travis, J Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA UnivGeorgia Athens GA USA 30602 Mol Biol, Athens, GA 30602 USA
Citazione:
A. Kozik et al., "A novel mechanism for bradykinin production at inflammatory sites - Diverse effects of a mixture of neutrophil elastase and mast cell tryptase versustissue and plasma kallikreins on native and oxidized kininogens", J BIOL CHEM, 273(50), 1998, pp. 33224-33229

Abstract

Coprocessing of kininogens by a mixture of human mast cell tryptase and neutrophil elastase was explored as a potential substitute for the kallikrein-dependent pathway for kinin generation during inflammation. Tryptase easily excised bradykinin from the synthetic heptadecapeptide, ISLMKRPPGFSPFRSSR, but was unable to produce significant amounts of kinin by proteolysis of kininogens. However, a mixture of tryptase and elastase released bradykininfrom each protein with a yield comparable to that of human plasma kallikrein, Significantly, neither plasma nor tissue kallikrein was able to effectively process N-chlorosuccinimide-oxidized high molecular weight kininogen, an effect attributed to the oxidation of a methionine residue upstream fromthe N terminus of the kinin domain. In support of these results the model heptadecapetide, ISL(MO)KRPPGFSPFRSSR, was also resistant to hydrolysis by either kallikrein. In contrast, the release of bradykinin from oxidized peptide or protein substrates by the tryptase/elastase mixture was not altered. Because kininogen modification may occur at inflammatory sites, as a result of the oxidative burst of recruited neutrophils and macrophages, these results suggest an alternative pathway for kinin production and the necessity for the novel utilization of two specific proteinases known to be released from these cells during inflammatory episodes.

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Documento generato il 22/09/20 alle ore 06:50:55