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Titolo:
COMPARATIVE PROPERTIES OF 2 CYSTEINE PROTEINASES (GINGIPAINS-R), THE PRODUCTS OF 2 RELATED BUT INDIVIDUAL GENES OF PORPHYROMONAS-GINGIVALIS
Autore:
POTEMPA J; MIKOLAJCZYKPAWLINSKA J; BRASSELL D; NELSON D; THOGERSEN IB; ENGHILD JJ; TRAVIS J;
Indirizzi:
JAGIELLONIAN UNIV,INST MOL BIOL,DEPT IMMUNOL & MICROBIOL PL-31120 KRAKOW POLAND DUKE UNIV,MED CTR,DEPT PATHOL DURHAM NC 27710 UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL ATHENS GA 30602
Titolo Testata:
The Journal of biological chemistry
fascicolo: 34, volume: 273, anno: 1998,
pagine: 21648 - 21657
SICI:
0021-9258(1998)273:34<21648:CPO2CP>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
SODIUM DODECYL-SULFATE; BACTEROIDES-GINGIVALIS; ARG-GINGIPAIN; STRUCTURAL CHARACTERIZATION; POSSIBLE INVOLVEMENT; PERIODONTAL-DISEASE; MOLECULAR-CLONING; ACTIVE-SITE; PROTEASE; W50;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
J. Potempa et al., "COMPARATIVE PROPERTIES OF 2 CYSTEINE PROTEINASES (GINGIPAINS-R), THE PRODUCTS OF 2 RELATED BUT INDIVIDUAL GENES OF PORPHYROMONAS-GINGIVALIS", The Journal of biological chemistry, 273(34), 1998, pp. 21648-21657

Abstract

Proteolytic enzymes produced by Porphyromonas gingivalis are important virulence factors of this periodontopathogen, Two of these enzymes, referred to as arginine-specific cysteine proteinases (gingipains R), are the product of two related genes, Here, we describe the purification of an enzyme translated hom the rgpB/rgp-2 gene (gingipain R2, RGP-S) and secreted as a single chain protein of 422 residues. The enzyme occurs in several isoforms differing in pI, molecular mass, mobility in gelatin zymography gels, and affinity to arginine-Sepharose. In comparison to the 95-kDa gingipain R1, a complex of catalytic and hemagglutinin/adhesin domains, RGP-2 showed five times lower proteolytic activity, although its activity on various P-1-arginine p-nitroanity, substrates was generally higher, Gingipains R amidolytic activity, but not general proteolytic activity, was stimulated by glycyl-glycine. However, in cases of limited proteolysis, such as the inactivation of alpha-1-anti-chymotrypsin, glycyl-glycine potentiated inhibitor cleavage, Incontrast, alpha-1-proteinase inhibitor was not inactivated by gingipains R and only underwent proteolytic degradation during boiling in reducing SDS-polyacrylamide gel electrophoresis treatment buffer. Similarly, native type I collagen was completely resistant to cleavage by gingipains but readily degraded after denaturation, Together, these data explain much of the controversy regarding gingipains structure and substrate specificity and indicate that these enzymes function as P. gingivalis virulence factors by proteolysis of selected target proteins rather than random degradation of host connective tissue components.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 15:49:44