Luteolin exhibits anti-inflammatory effects by blocking the activity of heat shock protein 90 in macrophages

Biochemical and Biophysical Research Communications

Volumn 443, Issue 1, 2014, Pages 326-332

  Chen, Dan ^a   Bi, Aijing ^a   Dong, Xiaoliang ^a   Jiang, Yi ^b   Rui, Bing ^a   Liu, Jinjiao ^a   Yin, Zhimin ^b   Luo, Lan ^a  

^a NANJING UNIVERSITY   (China)

^b NANJING NORMAL UNIVERSITY   (China)

Author keywords

C Jun; Heat shock protein 90; High mobility group B 1; HMGB1; Lipopolysaccharide; Luteolin; Macrophage; RAGE

Indexed keywords

ENDOTOXIN; ESCHERICHIA COLI LIPOPOLYSACCHARIDE; HEAT SHOCK PROTEIN 90; HIGH MOBILITY GROUP B1 PROTEIN; I KAPPA B; LIPOPOLYSACCHARIDE; LUTEOLIN; MITOGEN ACTIVATED PROTEIN KINASE; NITRIC OXIDE; PROTEIN C JUN; PROTEIN KINASE B; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; TUMOR NECROSIS FACTOR ALPHA;

ANIMAL CELL; ANIMAL CELL CULTURE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIINFLAMMATORY ACTIVITY; ARTICLE; CELL VIABILITY; CONFOCAL LASER MICROSCOPY; CONTROLLED STUDY; CYTOKINE PRODUCTION; CYTOTOXICITY; ENZYME ACTIVATION; ENZYME INHIBITION; IN VITRO STUDY; IN VIVO STUDY; INFLAMMATION; LETHALITY; MORTALITY; MOUSE; NONHUMAN; PERITONEUM MACROPHAGE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN SECRETION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION; WESTERN BLOTTING;

MUS;

C-JUN; HEAT SHOCK PROTEIN 90; HIGH MOBILITY GROUP B-1; HMGB1; LIPOPOLYSACCHARIDE; LUTEOLIN; MACROPHAGE; RAGE; RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS;

ANIMALS; ANTI-INFLAMMATORY AGENTS, NON-STEROIDAL; CELL LINE; DISEASE MODELS, ANIMAL; HEK293 CELLS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; JNK MITOGEN-ACTIVATED PROTEIN KINASES; LIPOPOLYSACCHARIDES; LUTEOLIN; MACROPHAGES; MICE; MICE, INBRED BALB C; PROTO-ONCOGENE PROTEINS C-AKT; SEPSIS; SIGNAL TRANSDUCTION;

EID: 84890859996     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.11.122     Document Type: Article

References (23)

1. Ulevitch R.J., Tobias P.S. Recognition of gram-negative bacteria and endotoxin by the innate immune system. Curr. Opin. Immunol. 1999, 11:19-22.
2. Guha M., Mackman N. LPS induction of gene expression in human monocytes. Cell. Signal. 2001, 13:85-94.
3. Yokochi T. A new experimental murine model for lipopolysaccharide-mediated lethal shock with lung injury. Innate Immun. 2011, 18:364-370.
4. Desai S.B., Furst D.E. Problems encountered during anti-tumour necrosis factor therapy. Best Pract. Res. Clin. Rheumatol. 2006, 20:757-790.
5. Wu C.X., Sun H., Liu Q., Guo H., Gong J.P. LPS induces HMGB1 relocation and release by activating the NF-kappaB-CBP signal transduction pathway in the murine macrophage-like cell line RAW 264.7. J. Surg. Res. 2011, 175:88-100.
6. Tsao P.N., Wei S.C., Huang M.T., Lee M.C., Chou H.C., Chen C.Y., Hsieh W.S. Lipopolysaccharide-induced notch signaling activation through JNK-dependent pathway regulates inflammatory response. J. Biomed. Sci. 2011, 18:56.
7. Jiang W., Pisetsky D.S. The role of IFN-alpha and nitric oxide in the release of HMGB1 by RAW 264.7 cells stimulated with polyinosinic-polycytidylic acid or lipopolysaccharide. J. Immunol. 2006, 177:3337-3343.
8. Wang H., Bloom O., Zhang M., Vishnubhakat J.M., Ombrellino M., Che J., Frazier A., Yang H., Ivanova S., Borovikova L., Manogue K.R., Faist E., Abraham E., Andersson J., Andersson U., Molina P.E., Abumrad N.N., Sama A., Tracey K.J. HMG-1 as a late mediator of endotoxin lethality in mice. Science 1999, 285:248-251.
9. Naglova H., Bucova M. HMGB1 and its physiological and pathological roles. Bratisl. Lek. Listy 2012, 113:163-171.
10. van Zoelen M.A., Yang H., Florquin S., Meijers J.C., Akira S., Arnold B., Nawroth P.P., Bierhaus A., Tracey K.J., van der Poll T. Role of toll-like receptors 2 and 4, and the receptor for advanced glycation end products in high-mobility group box 1-induced inflammation in vivo. Shock 2009, 31:280-284.
11. Kim D.E., Min K.J., Kim J.S., Kwon T.K. High-mobility group box-1 protein induces mucin 8 expression through the activation of the JNK and PI3K/Akt signal pathways in human airway epithelial cells. Biochem. Biophys. Res. Commun. 2012, 421:436-441.
12. Yang H., Ochani M., Li J., Qiang X., Tanovic M., Harris H.E., Susarla S.M., Ulloa L., Wang H., DiRaimo R., Czura C.J., Wang H., Roth J., Warren H.S., Fink M.P., Fenton M.J., Andersson U., Tracey K.J. Reversing established sepsis with antagonists of endogenous high-mobility group box 1. Proc. Natl. Acad. Sci. USA 2004, 101:296-301.
13. Fu J., Chen D., Zhao B., Zhao Z., Zhou J., Xu Y., Xin Y., Liu C., Luo L., Yin Z. Luteolin induces carcinoma cell apoptosis through binding Hsp90 to suppress constitutive activation of STAT3. PLoS ONE 2012, 7:e49194.
14. Wolfle U., Esser P.R., Simon-Haarhaus B., Martin S.F., Lademann J., Schempp C.M. UVB-induced DNA damage, generation of reactive oxygen species, and inflammation are effectively attenuated by the flavonoid luteolin in vitro and in vivo. Free Radical Biol. Med. 2011, 50:1081-1093.
15. Kotanidou A., Xagorari A., Bagli E., Kitsanta P., Fotsis T., Papapetropoulos A., Roussos C. Luteolin reduces lipopolysaccharide-induced lethal toxicity and expression of proinflammatory molecules in mice. Am. J. Respir. Crit. Care Med. 2002, 165:818-823.
16. Choi E.Y., Jin J.Y., Choi J.I., Choi I.S., Kim S.J. Effects of luteolin on the release of nitric oxide and interleukin-6 by macrophages stimulated with lipopolysaccharide from prevotella intermedia. J. Periodontol. 2011, 82:1509-1517.
17. Andersson U., Wang H., Palmblad K., Aveberger A.C., Bloom O., Erlandsson-Harris H., Janson A., Kokkola R., Zhang M., Yang H., Tracey K.J. High mobility group 1 protein (HMG-1) stimulates proinflammatory cytokine synthesis in human monocytes. J. Exp. Med. 2000, 192:565-570.
18. Wegele H., Muller L., Buchner J. HSP70 and HSP90 a relay team for protein folding. Rev. Physiol. Biochem. Pharmacol. 2004, 151:1-44.
19. Gong H., Zuliani P., Komuravelli A., Faeder J.R., Clarke E.M. Analysis and verification of the HMGB1 signaling pathway. BMC Bioinformatics 2010, 11(Suppl. 7):S10.
20. Basso A.D., Solit D.B., Chiosis G., Giri B., Tsichlis P., Rosen N. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem. 2002, 277:39858-39866.
21. Andersson U., Tracey K.J. HMGB1 is a therapeutic target for sterile inflammation and infection. Annu. Rev. Immunol. 2011, 29:139-162.
22. Chen C.Y.-C., Chen G.-W., Chen W.Y.-C. Molecular simulation of HER2/neu degradation by inhibiting HSP90. J. Chin. Chem. Soc. 2008, 55:297-302.
23. Kim H.G., Shrestha B., Lim S.Y., Yoon D.H., Chang W.C., Shin D.J., Han S.K., Park S.M., Park J.H., Park H.I., Sung J.M., Jang Y., Chung N., Hwang K.C., Kim T.W. Cordycepin inhibits lipopolysaccharide-induced inflammation by the suppression of NF-kappaB through Akt and p38 inhibition in RAW 264.7 macrophage cells. Eur. J. Pharmacol. 2006, 545:192-199.