Anti-inflammatory effects and molecular mechanisms of 8-prenyl quercetin

Molecular Nutrition and Food Research

Volumn 60, Issue 5, 2016, Pages 1020-1032

  Hisanaga, Ayami ^a   Mukai, Rie ^b   Sakao, Kozue ^a   Terao, Junji ^b   Hou, De Xing ^a  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKUSHIMA   (Japan)

Author keywords

Cellular signaling; Direct binding; Inflammatory mediators; Molecular targets; Prenyl quercetin

Indexed keywords

8-PRENYL QUERCETIN; ANTIINFLAMMATORY AGENT; CYCLOOXYGENASE 2; CYTOKINE; INDUCIBLE NITRIC OXIDE SYNTHASE; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE; NITRIC OXIDE; NOS2 PROTEIN, MOUSE; PROSTAGLANDIN E2; PTGS2 PROTEIN, MOUSE; QUERCETIN; TLR4 PROTEIN, MOUSE; TOLL LIKE RECEPTOR 4;

ANALOGS AND DERIVATIVES; ANIMAL; CHEMISTRY; DISEASE MODEL; EDEMA; GENETICS; INSTITUTE FOR CANCER RESEARCH MOUSE; MALE; METABOLISM; MOLECULAR MODEL; MOUSE; PROTEIN CONFORMATION; RAW 264.7 CELL LINE;

ANIMALS; ANTI-INFLAMMATORY AGENTS; CYCLOOXYGENASE 2; CYTOKINES; DINOPROSTONE; DISEASE MODELS, ANIMAL; EDEMA; EXTRACELLULAR SIGNAL-REGULATED MAP KINASES; LIPOPOLYSACCHARIDES; MALE; MICE; MICE, INBRED ICR; MODELS, MOLECULAR; NITRIC OXIDE; NITRIC OXIDE SYNTHASE TYPE II; PROTEIN CONFORMATION; QUERCETIN; RAW 264.7 CELLS; TOLL-LIKE RECEPTOR 4;

EID: 84960932769     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201500871     Document Type: Article

References (33)

1. Yazaki, K., Sasaki, K., Tsurumaru, Y., Prenylation of aromatic compounds, a key diversification of plant secondary metabolites. Phytochemistry 2009, 70, 1739-1745.
2. Barron, D., Ibrahim, R. K., Isoprenylated flavonoids-A survey. Phytochemistry 1996, 43, 921-982.
3. Chen, X., Mukwaya, E., Wong, M. S., Zhang, Y., A systematic review on biological activities of prenylated flavonoids. Pharm. Biol. 2014, 52, 655-660.
4. Kretzschmar, G., Zierau, O., Wober, J., Tischer, S. et al., Prenylation has a compound specific effect on the estrogenicity of naringenin and genistein. J. Steroid Biochem. Mol. Biol. 2010, 118, 1-6.
5. Mukai, R., Horikawa, H., Fujikura, Y., Kawamura, T. et al., Prevention of disuse muscle atrophy by dietary ingestion of 8-prenylnaringenin in denervated mice. PLoS One 2012, 7, e45048.
6. Peterson, J., Dwyer, J., Flavonoids: dietary occurrence and biochemical activity. Nutr. Res. 1998, 18, 1995-2018.
7. Moskaug, J. O., Carlsen, H., Myhrstad, M., Blomhoff, R., Molecular imaging of the biological effects of quercetin and quercetin-rich foods. Mech. Ageing Dev. 2004, 125, 315-324.
8. Tanigawa, S., Fujii, M., Hou, D. X., Stabilization of p53 is involved in quercetin-induced cell cycle arrest and apoptosis in HepG2 cells. Biocsci. Biotechnol. Biochem. 2008, 72, 797-804.
9. Formica, J. V., Regelson, W., Review of biology of querctin and related bioflavonoids. Food Chem. Toxicol. 1995, 33, 1061-1080.
10. Cho, S. Y., Park, S. J., Kwon, M. J., Jeong, T. S. et al., Quercetin suppresses proinflammatory cytokines production through MAP kinases and NF-κB pathway in lipopolysaccharide-stimulated macrophage. Mol. Cell. Biochem. 2003, 243, 153-160.
11. Comalada, M., Camesco, D., Sierra, S., Ballester, I. et al., In vivo quercetin anti-inflammatory effect involves release of quercetin, which inhibits inflammation through down-regulation of the NF-κB pathway. Eur. J. Immunol. 2005, 35, 584-592.
12. Wu, Y., Luo, Q., Sun, C., Wang, G. et al. Chemical constituents contained in Desmodium caudatum. Zhongguo Zhong Yao Za Zhi 2012, 37, 1788-1792.
13. Sasaki, H., Kashiwada, Y., Shibatav, H., Takaishi, Y., Prenylated flavonoids from the roots of Desmodium caudatum and evaluation of their antifungal activity. Planta Med. 2012, 78, 1851-1856.
14. Laskin, D. L., Laskin, J. D., Role of macrophages and inflammatory mediators in chemically induced toxicity. Toxicology 2001, 160, 111-118.
15. Hadad, J. J., Cytokines and related receptor-mediated signaling pathways, Biochem. Biophys. Res. Commun. 2002, 297, 700-713.
16. Lu, Y. C., Yeh, W. C., Ohashi, P. S., LPS/TLR4 signal transduction pathway. Cytokine 2008, 42, 145-151.
17. Chang, L., Karin, M., Mammalian MAP kinase signalling cascades. Nature 2001, 410, 37-40.
18. Rossol, M., Heine, H., Meusch, U., Quandt, D. et al., LPS-induced cytokine production in human monocytes and macrophages. Crit. Rev. Immunol. 2011, 31, 379-446.
19. Lee, K. W., Kang, N. J., Rogozin, E. A., Kim, H. G. et al., Myricetin is a novel natural inhibitor of neoplastic cell transformation and MEK1. Carcinogenesis 2007, 28, 1918-1927.
20. Kang, N. J., Lee, K. W., Lee, D. E., Rogozin, E. A. et al., Cocoa procyanidins suppress transformation by inhibiting mitogen-activated protein kinase kinase. J. Biol. Chem. 2008, 283, 20664-20673.
21. Kawamura, T., Hayashi, M., Mukai, R., Terao, J. et al., An efficient method for c8-prenylation of flavonols and flavanones. Synthesis 2012, 44, 1308-1314.
22. Uto, T., Fujii, M., Hou, D.-X., 6-(Methylsulfinyl)hexyl isothiocyanate suppresses inducible nitric oxide synthase expression through the inhibition of Janus kinase 2-mediated JNK pathway in lipopolysaccharide-activated murine macrophages. Biochem. Pharmacol. 2005, 70, 1211-1221.
23. Uto, T., Fujii, M., Hou, D.-X., Inhibition of lipopolysaccharideinduced cyclooxygenase-2 transcription by 6-(methylsulfinyl) hexyl isothiocyanate, a chemopreventive compound from Wasabia japonica (Miq.) Matsumura, in mouse macrophages. Biochem. Pharmacol. 2005, 70, 1772-1784.
24. You, S., Nakanishi, E., Kuwata, H., Chen, J. et al., Inhibitory effects and molecular mechanisms of garlic organosulfur compounds on the production of inflammatory mediators. Mol. Nutr. Food Res. 2013, 57, 2049-2060.
25. Kim, J. K., Jun, J. G. Ailanthoidol suppresses lipopolysaccharide-stimulated inflammatory reactions in RAW264.7 cells and endotoxin shock in mice. J. Cell. Biochem. 2011, 112, 3816-3823.
26. Kumamoto, T., Fujii, M., Hou, D. -X., Akt is a direct target for myricetin to inhibit cell transformation. Mol. Cell Biochem. 2009, 332, 33-41.
27. Xing, J., Li, R., Li, N., Zhang, J. et al., Anti-inflammatory effect of procyanidin B1 on LPS-treated THP1 cells via interaction with the TLR4-MD-2 heterodimer and p38 MAPK and NF-κB signaling. Mol. Cell Biochem. 2015, 407, 89-95.
28. Park, B. S., Song, D. H., Kim, H. M., Choi, B. S. et al., The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature, 2009, 458, 1191-1196.
29. Kim, J. E., Kwon, J. Y., Seo, S. K., Son, J. E. et al, Cyanidin suppresses ultraviolet B-induced COX-2 expression in epidermal cells by targeting MKK4, MEK1, and Raf-1. Biochem. Pharmacol. 2010, 79, 1473-1482.
30. Goto, J., Kataoka, R., Muta, H., Hirayama, N., ASEDock docking based on alpha spheres and excluded volumes. J. Chem. Inf. Model. 2008, 48, 583-590.
31. Mukai, R., Fujikura, Y., Murota, K., Uehara, M. et al., Prenylation enhances quercetin uptake and reduces efflux in Caco-2 cells and enhances tissue accumulation in mice fed long-term. J. Nutr. 2013, 143, 1558-1564.
32. Tammela, P., Laitinen, L., Galkin, A., Wennberg, T. et al., Permeability characteristics and membrane affinity of flavonoids and alkyl gallates in Caco-2 cells and in phospholipid vesicles. Arch. Biochem. Biophys. 2004, 425, 193-199.
33. Akira, S., Takeda, K., Kaisho, T., Toll-like receptors: critical proteins linking innate and acquired immunity. Nat. Immunol. 2001, 2, 675-680.