mangostin has been researched along with Pain* in 2 studies
2 other study(ies) available for mangostin and Pain
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Anti-inflammatory activity of mangostins from Garcinia mangostana.
The fruit hull of Garcinia mangostana Linn (Guttiferae) is used as an anti-inflammatory drug in Southeast Asia. Two xanthones, alpha- and gamma-mangostins, were isolated from the fruit hull of G. mangostana, and both significantly inhibited nitric oxide (NO) and PGE(2) production from lipopolysaccharide (LPS)-stimulated RAW 264.7 cells. The IC(50) values for the inhibition of NO production by alpha- and gamma-mangostins were 12.4 and 10.1 microM, respectively. After iNOS enzyme activity was stimulated by LPS for 12 h, treatment with either alpha- or gamma-mangostin at 5 microg/ml (12.2 and 12.6 microM, respectively) for 24 h did not significantly inhibit NO production. The data show that the inhibitory activities of alpha- and gamma-mangostins are not due to direct inhibition of iNOS enzyme activity. On the other hand, expression of iNOS was inhibited by alpha- and gamma-mangostins in LPS-stimulated RAW 264.7 cells, but not by COX-2. However, the level of PGE(2) production was reduced by the two xanthones. In an in vivo study, alpha-mangostin significantly inhibited mice carrageenan-induced paw edema. In conclusion, alpha- and gamma-mangostins from G. mangostana are bioactive substances with anti-inflammatory effects. Topics: Animals; Anti-Inflammatory Agents; Cells, Cultured; Dinoprostone; Fruit; Garcinia mangostana; Lipopolysaccharides; Macrophages; Mice; Nitric Oxide Synthase Type II; Pain; Xanthones | 2008 |
gamma-Mangostin inhibits inhibitor-kappaB kinase activity and decreases lipopolysaccharide-induced cyclooxygenase-2 gene expression in C6 rat glioma cells.
We investigated the effect of gamma-mangostin purified from the fruit hull of the medicinal plant Garcinia mangostana on spontaneous prostaglandin E(2) (PGE(2)) genase release and inducible cyclooxy-2 (COX-2) gene expression in C6 rat glioma cells. An 18-h treatment with gamma-mangostin potently inhibited spontaneous PGE(2) release in a concentration-dependent manner with the IC(50) value of approximately 2 microM, without affecting the cell viability even at 30 microM. By immunoblotting and reverse-transcription polymerase chain reaction, we showed that gamma-mangostin concentration-dependently inhibited lipopolysaccharide (LPS)-induced expression of COX-2 protein and its mRNA, but not those of constitutive COX-1 cyclooxygenase. Because LPS is known to stimulate inhibitor kappaB (IkappaB) kinase (IKK)-mediated phosphorylation of IkappaB followed by its degradation, which in turn induces nuclear factor (NF)-kappaB nuclear translocation leading to transcriptional activation of COX-2 gene, the effect of gamma-mangostin on the IKK/IkappaB cascade controlling the NF-kappaB activation was examined. An in vitro IKK assay using IKK protein immunoprecipitated from C6 cell extract showed that this compound inhibited IKK activity in a concentration-dependent manner, with the IC(50) value of approximately 10 microM. Consistently gamma-mangostin was also observed to decrease the LPS-induced IkappaB degradation and phosphorylation in a concentration-dependent manner, as assayed by immunoblotting. Furthermore, luciferase reporter assays showed that gamma-mangostin reduced the LPS-inducible activation of NF-kappaB-and human COX-2 gene promoter region-dependent transcription. gamma-Mangostin also inhibited rat carrageenan-induced paw edema. These results suggest that gamma-mangostin directly inhibits IKK activity and thereby prevents COX-2 gene transcription, an NF-kappaB target gene, probably to decrease the inflammatory agent-stimulated PGE(2) production in vivo, and is a new useful lead compound for anti-inflammatory drug development. Topics: Animals; Brain Neoplasms; Cyclooxygenase 1; Cyclooxygenase 2; Dinoprostone; Drug Interactions; Gene Expression; Glioma; I-kappa B Kinase; I-kappa B Proteins; Isoenzymes; Lipopolysaccharides; Male; Membrane Proteins; NF-kappa B; Pain; Prostaglandin-Endoperoxide Synthases; Protein Serine-Threonine Kinases; Rats; Rats, Wistar; RNA, Messenger; Transcriptional Activation; Tumor Cells, Cultured; Xanthones | 2004 |