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Titolo:
Comparative cleavage sites within the reactive-site loop of native and oxidized alpha(1)-proteinase inhibitor by selected bacterial proteinases
Autore:
Rapala-Kozik, M; Potempa, J; Nelson, D; Kozik, A; 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
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 10, volume: 380, anno: 1999,
pagine: 1211 - 1216
SICI:
1431-6730(199910)380:10<1211:CCSWTR>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA ALPHA-1-PROTEINASE INHIBITOR; SERRATIA-MARCESCENS PNEUMONIA; PSEUDOMONAS-AERUGINOSA; PROTEOLYTIC INACTIVATION; MICROBIAL PROTEINASES; STAPHYLOCOCCUS-AUREUS; ENZYMATIC REDUCTION; PROTEASES; METHIONINE; ELASTASE;
Keywords:
aureolysin; human neutrophil elastase; metalloproteinase; methionine oxidation; serralysin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
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:
M. Rapala-Kozik et al., "Comparative cleavage sites within the reactive-site loop of native and oxidized alpha(1)-proteinase inhibitor by selected bacterial proteinases", BIOL CHEM, 380(10), 1999, pp. 1211-1216

Abstract

Human alpha(1)-proteinase inhibitor (alpha 1-PI) is responsible for the tight control of neutrophil elastase activity which, if down regulated, may cause local excessive tissue degradation, Many bacterial proteinases can inactivate alpha(1)-PI by hydrolytic cleavage within its reactive site, resulting in the down regulation of elastase, and this mechanism is likely to contribute to the connective tissue damage often associated with bacterial infections, Another pathway of the inactivation of alpha(1)-PI is reversible and involves oxidation of a critical active-site methionine residue that mayinfluence inhibitor susceptibility to proteolytic inactivation, Hence, theaim of this work was to determine whether this oxidation event might affect the rate and pattern of the cleavage of the alpha(1)-PI reactive-site loop by selected bacterial proteinases, including thermolysin, aureolysin, serralysin, pseudolysin, Staphylococcus aureus serine proteinase, streptopain,and periodontain, A shift of cleavage specificity was observed after alpha(1)-PI oxidation, with a preference for the Glu(354)-Ala(355) bond by most of the proteinases tested. Only aureolysin and serralysin cleave the oxidized form of alpha(1)-PI faster than the native inhibitor, suggesting that bacteria which secrete these metalloproteinases may specifically take advantage of the host defense oxidative mechanism to accelerate elimination of alpha(1)-PI and, consequently, tissue degradation by neutrophil elastase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 18:37:29