Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase

Antonio Rossi; Pankaj Kapahi; Gioacchino Natoli; Takayuki Takahashi; Yi Chen; Michael Karin; M. Gabriella Santoro

doi:10.1038/47520

journal article Jan 01, 2000

Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase

Antonio Rossi Pankaj Kapahi Gioacchino Natoli Takayuki Takahashi Yi Chen

Michael Karin

M. Gabriella Santoro

Nature Vol. 403 No. 6765 pp. 103-108 · Springer Science and Business Media LLC

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References

30

[1]

Baldwin,A. S. The NF-κB and IκB proteins: new discoveries and insights. Annu. Rev. Immunol. 14, 649–683 (1996). 10.1146/annurev.immunol.14.1.649

[2]

Barnes,P. J. & Karin,M. Nuclear factor-κB—a pivotal transcription factor in chronic inflammatory diseases. New Engl. J. Med. 336, 1066–1071 (1997). 10.1056/nejm199704103361506

[3]

DiDonato,J. A., Hayakawa,M., Rothwarf,D. M., Zandi,E. & Karin,M. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature 388, 548–554 (1997). 10.1038/41493

[4]

Zandi,E., Chen,Y. & Karin,M. Direct phosphorylation of IκB by IKKα and IKKβ: discrimination between free and NF-κB-bound substrate. Science 281, 1360–1363 (1998). 10.1126/science.281.5381.1360

[5]

Herschman,H. R. et al. Function and regulation of prostaglandin synthase-2. Adv. Exp. Med. Biol. 407, 61–66 (1997). 10.1007/978-1-4899-1813-0_9

[6]

Newton,R., Kintert,L. M. E., Bergmann,M., Adcock,I. M. & Barnes,P. I. Evidence for involvement of NF-κB in the transcriptional control of COX-2 gene expression by IL-1β. Biochem. Biophys. Res. Comm. 237, 28–32 (1997). 10.1006/bbrc.1997.7064

[7]

Gilroy,D. W. et al. Inducible cyclooxygenase may have anti-inflammatory properties. Nature Med. 5, 698–701 (1999). 10.1038/9550

[8]

Ricote,M., Li,A. C., Willson,T. M., Kelly,C. J. & Glass,C. K. The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation. Nature 391, 79–82 (1998). 10.1038/34178

[9]

Jiang,C., Ting,A. T. & Seed,B. PPAR-γ agonists inhibit production of monocyte inflammatory cytokines. Nature 391, 82–86 (1998). 10.1038/34184

[10]

Delhase,M., Hayakawa,M., Chen,Y. & Karin,M. Positive and negative regulation of IκB kinase activity through IKKβ subunit phosphorylation. Science 284, 309–313 (1999). 10.1126/science.284.5412.309

[11]

Tanaka,M. et al. Embryonic lethality, liver degeneration and impaired NF-κB activation in IKK-β-deficient mice. Immunity 10, 421–429 (1999). 10.1016/s1074-7613(00)80042-4

[12]

Santoro,M. G. Antiviral activity of cyclopentenone prostanoids. Trends Microbiol. 5, 276–281 (1997). 10.1016/s0966-842x(97)01066-4

[13]

Rozera,C. et al. Inhibition of HIV-1 replication by cyclopentenone prostaglandins in acutely infected human cells. J. Clin. Invest. 97, 1795–1803 (1996). 10.1172/jci118609

[14]

Rossi,A., Elia,G. & Santoro,M. G. Inhibition of nuclear factor κB by prostaglandin A1: an effect associated with heat shock transcription factor activation. Proc. Natl Acad. Sci. USA 94, 746–750 (1997). 10.1073/pnas.94.2.746

[15]

Rothwarf,D. M., Zandi,E., Natoli,G. & Karin,M. IKK-γ is an essential regulatory subunit of the IκB kinase complex. Nature 395, 297–300 (1998). 10.1038/26261

[16]

Yamaoka,S. et al. Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation. Cell 93, 1231–1240 (1998). 10.1016/s0092-8674(00)81466-x

[17]

Karin,M. & Delhase,M. JNK or IKK, AP-1 or NF-κB, which are the targets for MEK kinase 1 action? Proc. Natl Acad. Sci. USA 95, 9067–9069 (1998). 10.1073/pnas.95.16.9067

[18]

Yin,M., Yamamoto,Y. & Gaynor,R. B. The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β. Nature 398, 77–80 (1998). 10.1038/23948

[19]

Fukushima,M. Prostaglandin J2-anti-tumor and anti-viral activities and the mechanisms involved. Eicosanoids 3, 189–199 (1990).

[20]

Rossi,A., Elia,G. & Santoro,M. G. 2-Cyclopenten-1-one, a new inducer of heat shock protein 70 with antiviral activity. J. Biol. Chem. 271, 32192–32196 (1996). 10.1074/jbc.271.50.32192

[21]

Gray,N. S. et al. Exploiting chemical libraries, structure and genomics in the search for kinase inhibitors. Science 281, 533–537 (1998). 10.1126/science.281.5376.533

[22]

Santoro,M. G., Garaci,E. & Amici,C. Prostaglandins with antiproliferative activity induce the synthesis of a heat shock protein in human cells. Proc. Natl Acad. Sci. USA 86, 8407–8411 (1989). 10.1073/pnas.86.21.8407

[23]

Santoro,M. G., Benedetto,A., Carruba,G., Garaci,E. & Jaffe,B. M. Prostaglandin A compounds as antiviral agents. Science 209, 1032–1034 (1980). 10.1126/science.6157190

[24]

Staels,B. et al. Activation of human aorta smooth-muscle cells is inhibited by PPARα but not by PPARγ activators. Nature 393, 790–793 (1998). 10.1038/31701

[25]

Serhan,C. N., Haeggström,J. Z. & Leslie,C. C. Lipid mediator networks in cell signaling: update and impact of cytokines. FASEB J. 10, 1147–1158 (1996). 10.1096/fasebj.10.10.8751717

[26]

Calderwood,S. K., Bornstein,B., Farnum,E. K. & Stevenson,M. A. Heat shock stimulates the release of arachidonic acid and the synthesis of prostaglandins and leukotriene B4 in mammalian cells. J. Cell Physiol. 141, 325–333 (1989). 10.1002/jcp.1041410214

[27]

Leung,D. Y. et al. Increased in vitro bone resorption by monocytes in the hyper-immunoglobulin E syndrome. J. Immunol. 140, 84–88 (1988). 10.4049/jimmunol.140.1.84

[28]

Offenbacher,S., Odle,B. M. & Van Dyke,T. E. The use of crevicular fluid prostaglandin E2 levels as a predictor of periodontal attachment loss. J. Periodontal Res. 21, 101–112 (1986). 10.1111/j.1600-0765.1986.tb01443.x

[29]

Wang,C. Y., Mayo,M. W. & Baldwin,A. S. TNF and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB. Science 274, 786–787 (1998).

[30]

Hirose,S. et al. Expression and localization of cyclooxygenase isoforms and cytosolic phospholipase A2 in anti-Thy-1 glomerulonephritis. J. Am. Soc. Nephrol. 9, 408–416 (1998). 10.1681/asn.v93408

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Published: Jan 01, 2000
Vol/Issue: 403(6765)
Pages: 103-108
License: View

Authors

Shenzhen University

Cite This Article

Antonio Rossi, Pankaj Kapahi, Gioacchino Natoli, et al. (2000). Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase. Nature, 403(6765), 103-108. https://doi.org/10.1038/47520

Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase

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