Document Detail


Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion.
MedLine Citation:
PMID:  11447194     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Periodontitis is a chronic inflammatory disease affecting oral tissues. Oral epithelial cells represent the primary barrier against bacteria causing the disease. We examined the responses of such cells to an arginine-specific cysteine proteinase (RgpB) produced by a causative agent of periodontal disease, Porphyromonas gingivalis. This protease caused an intracellular calcium transient in an oral epithelial cell line (KB), which was dependent on its enzymatic activity. Since protease-activated receptors (PARs) might mediate such signaling, reverse transcription-PCR was used to characterize the range of these receptors expressed in the KB cells. The cells were found to express PAR-1, PAR-2, and PAR-3, but not PAR-4. In immunohistochemical studies, human gingival epithelial cells were found to express PAR-1, PAR-2, and PAR-3 on their surface, but not PAR-4, indicating that the cell line was an effective model for the in vivo situation. PAR-1 and PAR-2 expression was confirmed in intracellular calcium mobilization assays by treatment of the cells with the relevant receptor agonist peptides. Desensitization experiments strongly indicated that signaling of the effects of RgpB was occurring through PAR-1 and PAR-2. Studies with cells individually transfected with each of these two receptors confirmed that they were both activated by RgpB. Finally, it was shown that, in the oral epithelial cell line, PAR activation by the bacterial protease-stimulated secretion of interleukin-6. This induction of a powerful proinflammatory cytokine suggests a mechanism whereby cysteine proteases from P. gingivalis might mediate inflammatory events associated with periodontal disease on first contact with a primary barrier of cells.
Authors:
A Lourbakos; J Potempa; J Travis; M R D'Andrea; P Andrade-Gordon; R Santulli; E J Mackie; R N Pike
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Infection and immunity     Volume:  69     ISSN:  0019-9567     ISO Abbreviation:  Infect. Immun.     Publication Date:  2001 Aug 
Date Detail:
Created Date:  2001-07-11     Completed Date:  2001-08-23     Revised Date:  2013-06-09    
Medline Journal Info:
Nlm Unique ID:  0246127     Medline TA:  Infect Immun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5121-30     Citation Subset:  IM    
Affiliation:
Department of Biochemistry & Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
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MeSH Terms
Descriptor/Qualifier:
Adhesins, Bacterial
Animals
CHO Cells
Calcium / metabolism
Cell Line
Cricetinae
Cysteine Endopeptidases / metabolism*
Endopeptidases / metabolism*
Epithelial Cells / cytology,  metabolism
Gene Expression
Gingiva / cytology,  metabolism
Hemagglutinins / metabolism*
Humans
Interleukin-6 / secretion*
Mouth Mucosa / cytology,  secretion
Porphyromonas gingivalis / enzymology*
Receptor, PAR-1
Receptor, PAR-2
Receptors, Thrombin / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
DE 09761/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Adhesins, Bacterial; 0/Hemagglutinins; 0/Interleukin-6; 0/Receptor, PAR-1; 0/Receptor, PAR-2; 0/Receptors, Thrombin; 0/protease-activated receptor 3; 7440-70-2/Calcium; EC 3.4.-/Endopeptidases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.37/argingipain, Porphyromonas gingivalis; EC 3.4.99.-/arginine protease
Comments/Corrections

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