Roles for Arg- and Lys-Gingipains in the Disruption of Cytokine Responses and Loss of Viability of Human Endothelial Cells by Porphyromonas gingivalis Infection

@inproceedings{Baba2002RolesFA,
  title={Roles for Arg- and Lys-Gingipains in the Disruption of Cytokine Responses and Loss of Viability of Human Endothelial Cells by Porphyromonas gingivalis Infection},
  author={A. Baba and T. Kadowaki and T. Asao and Kenji Yamamoto},
  booktitle={Biological chemistry},
  year={2002}
}
Abstract Accumulating evidence indicates that periodontal disease is associated with human cardiovascular diseases. The periodontal pathogen Porphyromonas gingivalis was shown to be present in atherosclerotic plaques in addition to periodontal pockets. This bacterium is known to produce two individual cysteine proteinases, Arggingipain (Rgp) and Lysgingipain (Kgp). Here we show that these two enzymes are responsible for either the disruption of cytokine responses in human umbilical vein… Expand
A role for gingipains in cellular responses and bacterial survival in Porphyromonas gingivalis-infected cells.
TLDR
Recent knowledge on the pathophysiological role of gingipains in the virulence of P. gingivalis is summarized including host cell responses to bacterial infection and its evasion from host defense mechanisms. Expand
Role for Gingipains in Porphyromonas gingivalis Traffic to Phagolysosomes and Survival in Human Aortic Endothelial Cells
TLDR
It is found that the number of intracellular viable WT cells decreased more slowly than that of KDP136 cells, thus suggesting that gingipains contribute to bacterial survival, but not to trafficking, within the infected cells. Expand
Cysteine proteases from Porphyromonas gingivalis and TLR ligands synergistically induce the synthesis of the cytokine IL-8 in human artery endothelial cells.
TLDR
The synergistic effects of TLR ligands and P. gingivalis cysteine protease gingipain towards the proinflammatory response of human aortic endothelial cells are demonstrated to highlight a mechanism by which bacteria may contribute to the development of atherosclerosis. Expand
Gingipains from Porphyromonas gingivalis W83 Induce Cell Adhesion Molecule Cleavage and Apoptosis in Endothelial Cells
TLDR
Results indicate that gingipains from P. gingivalis can alter cell adhesion molecules and induce endothelial cell death, which could have implications for the pathogenicity of this organism. Expand
Proteolytic activity of Porphyromonas gingivalis attenuates MCP-1 mRNA expression in LPS-stimulated THP-1 cells.
TLDR
Results suggest that the proteolytic activity of P. gingivalis attenuate MCP-1 mRNA expression by promoting the decay of MCP -1 mRNA in LPS-stimulated THP-1 cells. Expand
A Functional Virulence Complex Composed of Gingipains, Adhesins, and Lipopolysaccharide Shows High Affinity to Host Cells and Matrix Proteins and Escapes Recognition by Host Immune Systems
TLDR
Inhibition of the proteolytic activities of the gingipain complex did not up-regulate the cytokine production, indicating that the functional domains in LPS are structurally masked by the complex proteins. Expand
Suppression of Pathogenicity of Porphyromonas gingivalis by Newly Developed Gingipain Inhibitors
TLDR
Results indicate that the newly developed KYT-1 andKYT-36 both should provide a broader application in studies of this important class of enzymes and facilitate the development of new approaches to periodontal diseases. Expand
Selective proteolysis of apolipoprotein B-100 by Arg-gingipain mediates atherosclerosis progression accelerated by bacterial exposure.
TLDR
Results indicate that degradation of apoB-100 by Rgp plays a crucial role in the promotion of atherosclerosis by P. gingivalis infection. Expand
[Gingipains as the determinants of periodontopathogenicity].
TLDR
Novel proteinase inhibitors specific to Rgp and Kgp on the basis of cleavage sites suppressed the characteristic features of P. gingivalis associated with its pathogenicity such as degradation of host proteins, hemagglutination, enhancement of vascular permeability, disruption of leukocytes function, and induction of host cell death. Expand
Gingipains from Porphyromonas gingivalis synergistically induce the production of proinflammatory cytokines through protease‐activated receptors with Toll‐like receptor and NOD1/2 ligands in human monocytic cells
TLDR
Results indicate that gingipains stimulate the secretion of cytokines from monocytic cells through the activation of PARs with synergistic effects by PAMPs, the first report of synergism of signalling via PARs, and TLRs or NOD1/2. Expand
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It is suggested that Rgp disrupts the integrinfibronectin interactions in fibroblasts, thereby contributing to the damage of periodontal tissues inperiodontal diseases caused by P. gingivalis. Expand
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TLDR
Evidence that RGP acts as a major processing enzyme for various cell surface and secretory proteins in P. gingivalis is provided and Lys-gingipain was found to be abnormally processed in the RGP-null mutant, suggesting that KGP is not involved in the normal processing mechanisms of these proteins. Expand
The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain
TLDR
Western blot (immunoblot) analysis using antibodies produced against RGP and the N-terminal peptides of RGP or the catalytic subunit of KGP indicated that these enzymes are synthesized by the strains studied and exist as multiple molecular mass species. Expand
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TLDR
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TLDR
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TLDR
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TLDR
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