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Titolo:
Purification and characterization of a novel cysteine proteinase (periodontain) from Porphyromonas gingivalis - Evidence for a role in the inactivation of human alpha(1)-proteinase inhibitor
Autore:
Nelson, D; Potempa, J; Kordula, T; 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, Dept Microbiol & Immunol, PL-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 mmunol, PL-31120 Krakow, Poland Jagiellonian Univ, Dept Anim Biochem, PL-31120 Krakow, Poland JagiellonianUniv Krakow Poland PL-31120 iochem, PL-31120 Krakow, Poland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 18, volume: 274, anno: 1999,
pagine: 12245 - 12251
SICI:
0021-9258(19990430)274:18<12245:PACOAN>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
IV-LIKE ACTIVITIES; CREVICULAR FLUID; BACTEROIDES-GINGIVALIS; PATHOGENIC MECHANISM; PROTEOLYTIC-ENZYMES; DISEASE; ELASTASE; GENE; ALPHA(1)-ANTITRYPSIN; DEGRADATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Travis, J Univ Georgia, Dept Biochem & Mol Biol, Life Sci Bldg, Athens, GA30602 USA Univ Georgia Life Sci Bldg Athens GA USA 30602 ens, GA 30602 USA
Citazione:
D. Nelson et al., "Purification and characterization of a novel cysteine proteinase (periodontain) from Porphyromonas gingivalis - Evidence for a role in the inactivation of human alpha(1)-proteinase inhibitor", J BIOL CHEM, 274(18), 1999, pp. 12245-12251

Abstract

Periodontal disease is characterized by inflammation of the periodontium manifested by recruitment of neutrophils, which can degranulate, releasing powerful proteinases responsible for destruction of connective tissues, and eventual loss of tooth attachment. Although the presence of host proteinaseinhibitors (serpins) should minimize tissue damage by endogenous proteinases, this is not seen clinically, and it has been speculated that proteolytic inactivation of serpins may contribute to progression of the disease. A major pathogen associated with periodontal disease is the Gram-negative anaerobe Porphyromonas gingivalis, and in this report, we describe a novel proteinase that has been isolated from culture supernatants of this organism that is capable of inactivating the human serpin, alpha(1)-proteinase inhibitor, the primary endogenous regulator of human neutrophil elastase, This newenzyme, referred to as periodontain, belongs to the cysteine proteinase family based on inhibition studies and exists as a 75-kDa heterodimer, Furthermore, periodontain shares significant homology to streptopain, a proteinase from Streptococcus pyogenes, and prtT, a putative proteinase from P, gingivalis. Clearly, the presence of this enzyme, which rapidly inactivates alpha(1)-proteinase inhibitor, could result in elevated levels of human neutrophil elastase clinically detected in periodontal disease and should be considered as a potential virulence factor for P, gingivalis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 15:24:29