Glycoprotein isolated from Cudrania tricuspidata Bureau inhibits iNO and COX-2 expression through modulation of NF-κB in LPS-stimulated RAW 264.7 cells

Environmental Toxicology and Pharmacology

Volumn 27, Issue 2, 2009, Pages 247-252

  Joo, Heon Yeong ^a   Lim, Kye Taek ^b  

^a Chonnam National University   (South Korea)

^b Chonnam National University   (South Korea)

Author keywords

Cudrania tricuspidata Bureau glycoprotein (CTB glycoprotein); Inducible NO (iNO); Intracellular ROS; NF k cyrillic B; RAW 264.7 cells

Indexed keywords

1,1 DIPHENYL 2 PICRYLHYDRAZYL; CTB GLYCOPROTEIN; CUDRANIA TRICUSPIDATA EXTRACT; CYCLOOXYGENASE 2; CYCLOOXYGENASE 2 INHIBITOR; GLYCOPROTEIN; HERBACEOUS AGENT; HYDROXYL RADICAL; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INDUCIBLE NITRIC OXIDE SYNTHASE; INDUCIBLE NITRIC OXIDE SYNTHASE INHIBITOR; LIPOPOLYSACCHARIDE; NITRIC OXIDE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIINFLAMMATORY ACTIVITY; ANTIOXIDANT ACTIVITY; ARTICLE; CONTROLLED STUDY; CUDRANIA TRICUSPIDATA BUREAU; FRUIT; IMMUNOMODULATION; KOREA; LUNG INJURY; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE;

MACLURA TRICUSPIDATA;

EID: 59649093474     PISSN: 13826689     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.etap.2008.10.014     Document Type: Article

References (28)

1. Agren M., Kogerman P., Kleman M.I., Wessling M., and Toftgard R. Gene 330 (2004) 101-114
2. Anderson D. Antioxidant defenses against reactive oxygen species causing genetic and other damage. Mutat. Res. 350 (1996) 103-108
3. Aruoma O.I. Deoxyribose assay for detecting hydroxyl radicals. Methods Enzymol. 233 (1994) 57-66
4. Barnes P.J., and Karin M. Nuclear factor-kappa B: a pivotal transcription factor in chronic inflammatory diseases. N. Engl. J. Med. 336 (1997) 1066-1071
5. Cesaratto L., Vascotto C., Calligaris S., and Tell G. The importance of redox state in liver damage. Ann. Hepatol. 3 (2004) 86-92
6. Dubois M., Gilles K.A., Hamilton J.K., Rebers P.A., and Smith F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 20 (1956) 875-882
7. Franzini E., Sellak H., Hakim J., and Pasquier C. Comparative sugar degradation by (OH) produced by the iron-driven Fenton reaction and gamma radiolysis. Arch. Biochem. Biophys. 309 (1994) 261-265
8. Gotoh N., and Niki E. Rates of interactions of superoxide with vitamin E, vitamin C and related compounds as measured by chemiluminescence. Biochim. Biophys. Acta 1115 (1992) 201-207
9. Green L.C., Wagner D.A., Glogowski J., Skipper P.L., Wishnok J.S., and Tannenbaum S.R. Analysis of nitrate, nitrite, and [15N] nitrate in biological fluids. Anal. Biochem. 126 (1982) 131-138
10. Halliwell B., Gutteridge J.M., and Aruoma O.I. The deoxyribose method: a simple "test-tube" assay for determination of rate constants for reactions of hydroxyl radicals. Anal. Biochem. 165 (1987) 215-219
11. Kabe Y., Ando K., Hirao S., Yoshida M., and Handa H. Redoxregulation of NF-κB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxidants Redox Signal. 7 (2005) 395-403
12. Kaplanski G., Marin V., Montero-Julian F., Mantovani A., and Farnarier C. IL-6 a regulator of the transition from neutrophil to monocyte recruitment during inflammation. Trends Immunol. 24 (2003) 25-29
13. Ko J.H., Lee S.J., and Lim K.T. Toxicol. In Vitro 19 (2005) 353-363
14. Kowaltowski A.J., and Vercesi A.E. Mitochondrial damage induced by conditions of oxidative stress. Free Radic. Biol. Med. 26 (1999) 463-471
15. Lappas M., Permezel M., Georgiou H.M., and Rice G.E. Nuclear factor kappa B regulation of proinflammatory cytokines in human gestational tissues in vitro. Biol. Reprod. 67 (2002) 668-673
16. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall R.J.J. Biol. Chem. 193 (1951) 265-275
17. Maffei Facino R., Carini M., Aldini G., Berti F., and Rossoni G. Panax ginseng administration in the rat prevents myocardial ischemiareperfusion damage induced by hyperbaric oxygen: evidence for an antioxidant intervention. Plant. Med. 65 (1999) 614-619
18. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65 (1983) 55-63
19. Mckellar G., Madhok R., and Singh G. The problem with NSAIDs: what data to believe?. Curr. Pain Headache Rep. 11 (2007) 423-427
20. Murakami M., Yoshihara K., Shimbara S., Lambeau G., Gelb M.H., Singer A.G., Sawada M., Inagaki N., Nagai H., Ishihara M., Ishikawa Y., Ishii T., and Kudo I. Cellular arachidonate-releasing function and inflammation-associated expression of group IIF secretory phospholipase A2. J. Biol. Chem. 277 21 (2002) 19145-19155
21. Neville D.M., and Glossmann H. Molecular weight determination of membrane protein and glycoprotein subunits by discontinuous gel electrophoresis in dodecyl sulfate. Methods Enzymol. 32 (1974) 92-102
22. Ooi V.E., and Liu F. Immunomodulation and anti-cancer activity of polysaccharide-protein complexes. Curr. Med. Chem. 7 (2000) 715-729
23. Romanovsky A.A., Ivanov A.I., and Petresen S.R. Microsomal prostaglandin E synthase-1, ephrins, and ephrin kinases as suspected therapeutic targets in arthritis. Ann. N.Y. Acad. Sci. 1069 (2006) 183-194
24. Roth E. Oxygen free radicals and their clinical implications. Acta Chir. Hung. 36 (1997) 302-305
25. 2 in cultured endothelial cells. Arch. Biochem. Biophys. 302 (1993) 348-355
26. Swierkosz T.A., Mitchell J.A., Warner T.D., Botting R.M., and Vane J.R. Co-induction of nitric oxide synthase and cyclooxygenase: interactions between nitric oxide and prostanoids. Br. J. Pharm. 114 7 (1995) 1335-1342
27. Vane J.R., Mitchell J.A., and Appleton I. Inducible isoforms of cyclooxygenase and nitric-oxide synthase in inflammation. Proceedings of the National Academy of Sciences of the United States of America, vol. 91 (1994) 2046-2050
28. Wallace J.L. Nitric oxide as a regulator of inflammatory processes. Mem. Inst. Oswaldo Cruz 100 (2005) 5-9