Pseudoguaianolides isolated from inula britannica var. chinenis as inhibitory constituents against inducible nitric oxide synthase
- 83 Downloads
Three pseudoguaianolide type sesquiterpenes, bigelovin (1), 2,3-dihydroaromaticin (2), and ergolide (3) were isolated as inhibitory constituents against inducible nitric oxide synthase (iNOS) from the flowers ofInula britannica var. chinensis. Bigelovin (1) exhibited a highly potent inhibitory activity on lipopolysaccharide (LPS)-induced iNOS in murine macrophage RAW 264.7 cells with an IC50 value of 0.46 mM, which is about 8 times more potent than the known selective inhibitor of iNOS, L-N6-(1-iminoethyl)lysine (IC50 3.49 üM). 2,3-Dihydroaroma-ticin (2) and ergolide (3) also exhibited potent inhibitory activities on LPS-induced iNOS with IC50 values of 1.05 and 0.69 üM, respectively.
Key wordsInula britannica var. chinensis Bigelovin 2,3-Dihydroaromaticin Ergolide iNOS inhibitor
Unable to display preview. Download preview PDF.
- Bensky, D., Gamble, A., Kaptchuk, T. J., and Bensky, L. L.,Chinese Herbal Medicine: Materia Medica. Eastland Press, Seattle, pp. 193–194, (1993).Google Scholar
- Escott, K. J., Beech, J. S., Haga, K. K., Williams, S. C., Meldrum, B. S., and Bath, P. M., Cerebroprotective effect of the nitric oxide synthase inhibitors, 1-(2-trifluoromethylphenyl) imidazole and 7-nitro indazole, after transient focal cerebral ischemia in the rat.J. Cereb. Blood Flow Metab., 18, 281–287 (1998).PubMedCrossRefGoogle Scholar
- Han, J. W., Lee, B. G., Kim, Y. K., Yoon, J. W., Jin, H. K., Hong, S., Lee, H. Y., Lee, K. R., and Lee, H. W., Ergolide, sesquiterpene lactone fro.Inula britannica, inhibits inducible nitric oxide synthase and cyclo-oxygenase-2 expression in RAW 264.7 macrophages through the inactivation of NF-kB.Br. J. Pharmacol., 133, 503–512 (2001).CrossRefGoogle Scholar
- Hukkanen, M., Hughes, R J., Buttery, L. D., Gross, S. S., Evans, T. J., Seddon, S., Riveros-Moreno, V., Macintyre, I., and Polak, J. M., Cytokine-stimulated expression of inducible nitric oxide synthase by mouse, rat, and human osteoblast-like cells and its functional role of osteoblast metabolic activity.Endocrinology, 136, 5445–5453 (1995).PubMedCrossRefGoogle Scholar