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Titolo:
THE POTENTIAL ROLE OF ALPHA(2)-MACROGLOBULIN IN THE CONTROL OF CYSTEINE PROTEINASES (GINGIPAINS) FROM PORPHYROMONAS-GINGIVALIS
Autore:
GRON H; PIKE R; POTEMPA J; TRAVIS J; THOGERSEN IB; ENGHILD JJ; PIZZO SV;
Indirizzi:
DUKE UNIV,MED CTR,DEPT PATHOL,BOX 3712 DURHAM NC 27710 UNIV GEORGIA,DEPT BIOCHEM ATHENS GA 30602 JAGIELLONIAN UNIV,INST MOL BIOL,DEPT MICROBIOL & IMMUNOL PL-31120 KRAKOW POLAND
Titolo Testata:
Journal of Periodontal Research
fascicolo: 1, volume: 32, anno: 1997,
parte:, 1
pagine: 61 - 68
SICI:
0022-3484(1997)32:1<61:TPROAI>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLACK-PIGMENTED BACTEROIDES; MACROGLOBULIN RAT ALPHA-1-INHIBITOR-3; VASCULAR-PERMEABILITY ENHANCEMENT; MAMMALIAN ALPHA-MACROGLOBULINS; TRYPSIN-LIKE ACTIVITY; HUMAN ALPHA-2-MACROGLOBULIN; PERIODONTAL-DISEASE; CREVICULAR FLUID; CLEAVAGE SITES; ACTINOBACILLUS-ACTINOMYCETEMCOMITANS;
Keywords:
ALPHA(2)-MACROGLOBULIN; GINGIPAIN; PERIODONTITIS; PORPHYROMONAS GINGIVALIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
70
Recensione:
Indirizzi per estratti:
Citazione:
H. Gron et al., "THE POTENTIAL ROLE OF ALPHA(2)-MACROGLOBULIN IN THE CONTROL OF CYSTEINE PROTEINASES (GINGIPAINS) FROM PORPHYROMONAS-GINGIVALIS", Journal of Periodontal Research, 32(1), 1997, pp. 61-68

Abstract

Porphyromonas gingivalis is closely associated with the development of some forms of periodontitis. The major cysteine proteinases releasedby this bacterium hydrolyze peptide bonds only after arginyl (gingipain R) or lysyl residues (gingipain K). No target protein inhibitors have been identified for either enzyme, leading us to investigate their inhibition by human plasma alpha(2)-macroglobulin (alpha(2)M). Both 50- and 95 kDa gingipain R were efficiently inhibited by alpha(2)M, whereas the catalytic activity of gingipain K could not be eliminated. All3 enzymes were, however, inhibited by a homologous macroglobulin fromrat plasma, alpha(1)-inhibitor-3 (alpha(1)I(3)). alpha-Macroglobulinsmust be cleaved in the so-called ''bait region'' in order to inhibit proteinases by a mechanism involving physical entrapment of the enzyme. A comparison of the aminio acid sequences of the 2 macroglobulins indicates that the lack of lysyl residues within the bait region of alpha(2)M protects Lys-specific proteinases from being trapped. On this basis, other highly specific proteinases might also not be inhibited by alpha(2)M, possibly explaining the inability of the inhibitor to control proteolytic activity in some bacterially induced inflammatory states, despite its abundance (2-5 mg/ml) in vascular fluids.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 09:52:10