cyclooxygenase-2 s-nitrosylation in salivary gland acinar cell inflammatory responses to porphyromonas gingivalis modulatory effect of ghrelincyclooxygenase-2 s-nitrosylation在唾腺腺泡的细胞炎症反应porphyromonas gingivalis激素调节的影响.pdfVIP

cyclooxygenase-2 s-nitrosylation in salivary gland acinar cell inflammatory responses to porphyromonas gingivalis modulatory effect of ghrelincyclooxygenase-2 s-nitrosylation在唾腺腺泡的细胞炎症反应porphyromonas gingivalis激素调节的影响.pdf

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cyclooxygenase-2 s-nitrosylation in salivary gland acinar cell inflammatory responses to porphyromonas gingivalis modulatory effect of ghrelincyclooxygenase-2 s-nitrosylation在唾腺腺泡的细胞炎症反应porphyromonas gingivalis激素调节的影响

Advances in Bioscience and Biotechnology, 2011, 2, 434-442 ABB doi:10.4236/abb.2011.26064 Published Online December 2011 (http://www.SciRP.org/journal/abb/). Cyclooxygenase-2 S-nitrosylation in salivary gland acinar cell inflammatory responses to Porphyromonas gingivalis : modulatory effect of ghrelin Bronislaw L. Slomiany, Amalia Slomiany University of Medicine and Dentistry of New Jersey, Newark, USA. Email: slomiabr@ Received 23 September 2011; revised 30 October 2011; accepted 18 November 2011. ABSTRACT responses to P. gingivalis and its key virulence factor, cell-wall lipopolysaccharide (LPS), are characterized by Disturbances in nitric oxide synthase (NOS) system a massive rise in epithelial cell apoptosis and proinflam- and the excessive prostaglandin (PGE2) generation matory cytokine expression, excessive nitric oxide (NO) are well-recognized features of oral mucosal inflam- generation, and a marked increase in prostaglandin matory responses to periodontopathic bacterium, P. (PGE2) production [3-6]. A growing volume of literature, gingivalis. Employing rat sublingual gland acinar cells, moreover, points towards the existence of a functional we show that P. gingivalis LPS-induced up-regulation and signaling relationship between NO, generated by ni- in PGE2 generation and the enhancement in inducible tric oxide synthase (NOS) isozyme system, and the for- (i) iNOS activity was associated with COX-2 activa- mation of PGE2 synthesized from arachidonic acid (AA) tion through S-nitrosylation, and accompanied by the

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