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Titolo:
Protease-active extracellular protein preparations from Porphyromonas gingivalis W83 induce N-cadherin proteolysis, loss of cell adhesion, and apoptosis in human epithelial cells
Autore:
Chen, Z; Casiano, CA; Fletcher, HM;
Indirizzi:
Loma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350USA Loma Linda Univ Loma Linda CA USA 92350 ol Genet, Loma Linda, CA 92350USA Loma Linda Univ, Ctr Mol Biol & Gene Therapy, Loma Linda, CA 92350 USA Loma Linda Univ Loma Linda CA USA 92350 Therapy, Loma Linda, CA 92350 USA
Titolo Testata:
JOURNAL OF PERIODONTOLOGY
fascicolo: 5, volume: 72, anno: 2001,
pagine: 641 - 650
SICI:
0022-3492(200105)72:5<641:PEPPFP>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEUKOCYTE C5A RECEPTOR; IN-VITRO; BETA-CATENIN; EXPRESSION; GENE; FIBRONECTIN; DEGRADATION; VIRULENCE; GINGIPAIN; CLEAVAGE;
Keywords:
Porphyromonas gingivalis; cadherins; extracellular matrix proteins; cell adhesion molecules;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Fletcher, HM Loma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350USA Loma Linda Univ Loma Linda CA USA 92350 a Linda, CA 92350USA
Citazione:
Z. Chen et al., "Protease-active extracellular protein preparations from Porphyromonas gingivalis W83 induce N-cadherin proteolysis, loss of cell adhesion, and apoptosis in human epithelial cells", J PERIODONT, 72(5), 2001, pp. 641-650

Abstract

Background: The protease-induced cytotoxicity of P. gingivalis may partly result from alteration of the extracellular matrix and/or surface receptorsthat mediate interaction between the host cells and their matrix. While P.gingivalis-induced degradation of E-cadherin has been documented, there isno information on the effects of P. gingivalis proteases on other members of this family of cell adhesion proteins. Methods: Human epithelial KB cells were exposed to protease-active extracellular protein preparations from isogenic mutants of P. gingivalis. Quantification of apoptosis was performed by visualization of nuclei stained with 4,6 ' -diamidino-2-phenylindole. Alteration of cell adhesion proteins was examined by immunoblotting of cell lysates using monoclonal antibodies to those proteins. Results: Treated cells exhibited loss of cell adhesion properties with apoptotic cell death subsequently observed. These effects correlated with the different levels of cysteine-dependent proteolytic activities of the isogenic mutants tested. Cleavage of N-cadherin was observed in immunoblots of lysates from detached cells. There was a direct correlation between the kinetics of N-cadherin cleavage and loss of cell adhesion properties. Loss of cell adhesion, as well as N-cadherin cleavage, could be inhibited by preincubation of P. gingivalis protease active extracellular protein preparations with the cysteine protease inhibitor TLCK. In control experiments, the cleavage of N-cadherin was detected after treatment of KB cells with trypsin butnot after cell dissociation by a non-enzymatic method. Conclusions: These results suggest that extracellular pro teases from P. gingivalis can induce degradation of N-cadherin, which could have implications for the pathogenicity of this bacterium.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 18:45:27