Ghrelin Protects against the Detrimental Consequences of Porphyromonas gingivalis-Induced Akt Inactivation through S-Nitrosylation on Salivary Mucin Synthesis
Disturbances in nitric oxide synthase isozyme system and the impairment in salivary mucin synthesis are well-recognized features associated with oral mucosal inflammatory responses to periodontopathic bacterium, P. gingivalis. In this study, using rat sublingual gland acinar cells, we report that P....
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Wiley
2011-01-01
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Series: | International Journal of Inflammation |
Online Access: | http://dx.doi.org/10.4061/2011/807279 |
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author | Bronislaw L. Slomiany Amalia Slomiany |
author_facet | Bronislaw L. Slomiany Amalia Slomiany |
author_sort | Bronislaw L. Slomiany |
collection | DOAJ |
description | Disturbances in nitric oxide synthase isozyme system and the impairment in salivary mucin synthesis are well-recognized features associated with oral mucosal inflammatory responses to periodontopathic bacterium, P. gingivalis. In this study, using rat sublingual gland acinar cells, we report that P. gingivalis LPS-induced impairment in mucin synthesis and associated suppression in Akt kinase activity were accompanied by a decrease in constitutive nitric oxide synthase (cNOS) activity and an induction in inducible nitric oxide synthase (iNOS) expression. The LPS effect on Akt inactivation was manifested in the kinase S-nitrosylation and a decrease in its phosphorylation at Ser473. Further, we demonstrate that a peptide hormone, ghrelin, countered the LPS-induced impairment in mucin synthesis. This effect of ghrelin was reflected in the suppression of iNOS and the increase in Akt activation, associated with the loss in S-nitrosylation and the increase in phosphorylation, as well as cNOS activation through phosphorylation. Our findings suggest that induction in iNOS expression by P. gingivalis-LPS leads to Akt kinase inactivation through S-nitrosylation that detrimentally impacts cNOS activation through phosphorylation as well as mucin synthesis. We also show that the countering effect of ghrelin on P. gingivalis-induced impairment in mucin synthesis is associated with Akt activation through phosphorylation. |
format | Article |
id | doaj-art-afd0b6ce8e974250823b21fd053472f5 |
institution | Kabale University |
issn | 2042-0099 |
language | English |
publishDate | 2011-01-01 |
publisher | Wiley |
record_format | Article |
series | International Journal of Inflammation |
spelling | doaj-art-afd0b6ce8e974250823b21fd053472f52025-02-03T06:42:01ZengWileyInternational Journal of Inflammation2042-00992011-01-01201110.4061/2011/807279807279Ghrelin Protects against the Detrimental Consequences of Porphyromonas gingivalis-Induced Akt Inactivation through S-Nitrosylation on Salivary Mucin SynthesisBronislaw L. Slomiany0Amalia Slomiany1Research Center, University of Medicine and Dentistry of New Jersey, P.O. Box 1709, Newark, NJ 07103-2400, USAResearch Center, University of Medicine and Dentistry of New Jersey, P.O. Box 1709, Newark, NJ 07103-2400, USADisturbances in nitric oxide synthase isozyme system and the impairment in salivary mucin synthesis are well-recognized features associated with oral mucosal inflammatory responses to periodontopathic bacterium, P. gingivalis. In this study, using rat sublingual gland acinar cells, we report that P. gingivalis LPS-induced impairment in mucin synthesis and associated suppression in Akt kinase activity were accompanied by a decrease in constitutive nitric oxide synthase (cNOS) activity and an induction in inducible nitric oxide synthase (iNOS) expression. The LPS effect on Akt inactivation was manifested in the kinase S-nitrosylation and a decrease in its phosphorylation at Ser473. Further, we demonstrate that a peptide hormone, ghrelin, countered the LPS-induced impairment in mucin synthesis. This effect of ghrelin was reflected in the suppression of iNOS and the increase in Akt activation, associated with the loss in S-nitrosylation and the increase in phosphorylation, as well as cNOS activation through phosphorylation. Our findings suggest that induction in iNOS expression by P. gingivalis-LPS leads to Akt kinase inactivation through S-nitrosylation that detrimentally impacts cNOS activation through phosphorylation as well as mucin synthesis. We also show that the countering effect of ghrelin on P. gingivalis-induced impairment in mucin synthesis is associated with Akt activation through phosphorylation.http://dx.doi.org/10.4061/2011/807279 |
spellingShingle | Bronislaw L. Slomiany Amalia Slomiany Ghrelin Protects against the Detrimental Consequences of Porphyromonas gingivalis-Induced Akt Inactivation through S-Nitrosylation on Salivary Mucin Synthesis International Journal of Inflammation |
title | Ghrelin Protects against the Detrimental Consequences of Porphyromonas gingivalis-Induced Akt Inactivation through S-Nitrosylation on Salivary Mucin Synthesis |
title_full | Ghrelin Protects against the Detrimental Consequences of Porphyromonas gingivalis-Induced Akt Inactivation through S-Nitrosylation on Salivary Mucin Synthesis |
title_fullStr | Ghrelin Protects against the Detrimental Consequences of Porphyromonas gingivalis-Induced Akt Inactivation through S-Nitrosylation on Salivary Mucin Synthesis |
title_full_unstemmed | Ghrelin Protects against the Detrimental Consequences of Porphyromonas gingivalis-Induced Akt Inactivation through S-Nitrosylation on Salivary Mucin Synthesis |
title_short | Ghrelin Protects against the Detrimental Consequences of Porphyromonas gingivalis-Induced Akt Inactivation through S-Nitrosylation on Salivary Mucin Synthesis |
title_sort | ghrelin protects against the detrimental consequences of porphyromonas gingivalis induced akt inactivation through s nitrosylation on salivary mucin synthesis |
url | http://dx.doi.org/10.4061/2011/807279 |
work_keys_str_mv | AT bronislawlslomiany ghrelinprotectsagainstthedetrimentalconsequencesofporphyromonasgingivalisinducedaktinactivationthroughsnitrosylationonsalivarymucinsynthesis AT amaliaslomiany ghrelinprotectsagainstthedetrimentalconsequencesofporphyromonasgingivalisinducedaktinactivationthroughsnitrosylationonsalivarymucinsynthesis |