메뉴 건너뛰기




Volumn 184, Issue 4, 2010, Pages 2140-2147

NCX 4040, a nitric oxide-donating aspirin, exerts anti-inflammatory effects through inhibition of IκB-α degradation in human monocytes

Author keywords

[No Author keywords available]

Indexed keywords

1H 1,2,4 OXADIAZOLO[4,3 A]QUINOXALIN 1 ONE; ACETYLSALICYLIC ACID; ACETYLSALICYLIC ACID 3 (NITROXYMETHYL)PHENYL ESTER; ACETYLSALICYLIC ACID DERIVATIVE; ANTIINFLAMMATORY AGENT; CYCLIC GMP; CYCLOOXYGENASE 2; I KAPPA B; INTERLEUKIN 10; INTERLEUKIN 18; INTERLEUKIN 1BETA; LIPOPOLYSACCHARIDE; NCX 4040; NITRIC OXIDE; PROSTAGLANDIN E2; PROTEASOME; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; CYCLOOXYGENASE 1; DRUG DERIVATIVE; NF KAPPAB INHIBITOR ALPHA; NF-KAPPAB INHIBITOR ALPHA; NITRIC OXIDE DONOR; NITRO DERIVATIVE; NONSTEROID ANTIINFLAMMATORY AGENT; PTGS1 PROTEIN, HUMAN; PTGS2 PROTEIN, HUMAN;

EID: 77949911051     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0903107     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0015237292 scopus 로고
    • Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs
    • Vane, J. R. 1971. Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs. Nat. New Biol. 231: 232-235.
    • (1971) Nat. New Biol. , vol.231 , pp. 232-235
    • Vane, J.R.1
  • 2
    • 0028339780 scopus 로고
    • Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin
    • Lecomte, M., O. Laneuville, C. Ji, D. L. DeWitt, and W. L. Smith. 1994. Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin. J. Biol. Chem. 269: 13207-13215.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13207-13215
    • Lecomte, M.1    Laneuville, O.2    Ji, C.3    DeWitt, D.L.4    Smith, W.L.5
  • 5
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: Structural, cellular, and molecular biology
    • Smith, W. L., D. L. DeWitt, and R. M. Garavito. 2000. Cyclooxygenases: structural, cellular, and molecular biology. Annu. Rev. Biochem. 69: 145-182.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 145-182
    • Smith, W.L.1    DeWitt, D.L.2    Garavito, R.M.3
  • 6
    • 34247505895 scopus 로고    scopus 로고
    • Regulation of intracellular cyclooxygenase levels by gene transcription and protein degradation
    • Kang, Y. J., U. R. Mbonye, C. J. DeLong, M. Wada, and W. L. Smith. 2007. Regulation of intracellular cyclooxygenase levels by gene transcription and protein degradation. Prog. Lipid Res. 46: 108-125.
    • (2007) Prog. Lipid Res. , vol.46 , pp. 108-125
    • Kang, Y.J.1    Mbonye, U.R.2    DeLong, C.J.3    Wada, M.4    Smith, W.L.5
  • 8
    • 0034946873 scopus 로고    scopus 로고
    • Cyclooxygenase-selective inhibition of prostanoid formation: Transducing biochemical selectivity into clinical read-outs
    • Patrono, C., P. Patrignani, and L. A. García Rodríguez. 2001. Cyclooxygenase-selective inhibition of prostanoid formation: transducing biochemical selectivity into clinical read-outs. J. Clin. Invest. 108: 7-13.
    • (2001) J. Clin. Invest. , vol.108 , pp. 7-13
    • Patrono, C.1    Patrignani, P.2    García Rodríguez, L.A.3
  • 9
    • 0012191369 scopus 로고    scopus 로고
    • Formation and actions of prostaglandins and inhibition of their synthesis
    • J. R. Vane, and R. M. Botting, eds. Wiliam Harvey Press, London
    • Vane, J. R., and R. M. Botting. 2001. Formation and actions of prostaglandins and inhibition of their synthesis. In Therapeutic roles of selective COX-2 inhibitors. J. R. Vane, and R. M. Botting, eds. Wiliam Harvey Press, London, p. 1-47.
    • (2001) Therapeutic Roles of Selective COX-2 Inhibitors , pp. 1-47
    • Vane, J.R.1    Botting, R.M.2
  • 10
    • 0030871687 scopus 로고    scopus 로고
    • COX-1 and COX-2 tissue expression: Implications and predictions
    • Crofford, L. J. 1997. COX-1 and COX-2 tissue expression: implications and predictions. J. Rheumatol. Suppl. 49: 15-19.
    • (1997) J. Rheumatol. Suppl. , vol.49 , pp. 15-19
    • Crofford, L.J.1
  • 11
    • 0036157485 scopus 로고    scopus 로고
    • Many actions of cyclooxygenase-2 in cellular dynamics and in cancer
    • Cao, Y., and S. M. Prescott. 2002. Many actions of cyclooxygenase-2 in cellular dynamics and in cancer. J. Cell. Physiol. 190: 279-286.
    • (2002) J. Cell. Physiol. , vol.190 , pp. 279-286
    • Cao, Y.1    Prescott, S.M.2
  • 12
    • 0032802682 scopus 로고    scopus 로고
    • NO-aspirins: A class of new antiinflammatory and antithrombotic agents
    • del Soldato, P., R. Sorrentino, and A. Pinto. 1999. NO-aspirins: a class of new antiinflammatory and antithrombotic agents. Trends Pharmacol. Sci. 20: 319-323.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 319-323
    • Del Soldato, P.1    Sorrentino, R.2    Pinto, A.3
  • 13
    • 0035352883 scopus 로고    scopus 로고
    • Nitric oxide-releasing nonsteroidal anti-inflammatory drugs: Novel gastrointestinal-sparing drugs
    • Bandarage, U. K., and D. R. Janero. 2001. Nitric oxide-releasing nonsteroidal anti-inflammatory drugs: novel gastrointestinal-sparing drugs. Mini Rev. Med. Chem. 1: 57-70.
    • (2001) Mini Rev. Med. Chem. , vol.1 , pp. 57-70
    • Bandarage, U.K.1    Janero, D.R.2
  • 14
    • 20444373321 scopus 로고    scopus 로고
    • Novel nonsteroidal antiinflammatory drugs possessing a nitric oxide donor diazen-1-ium-1,2-diolate moiety: Design, synthesis, biological evaluation, and nitric oxide release studies
    • Velázquez, C., P. N. Praveen Rao, and E. E. Knaus. 2005. Novel nonsteroidal antiinflammatory drugs possessing a nitric oxide donor diazen-1-ium-1,2-diolate moiety: design, synthesis, biological evaluation, and nitric oxide release studies. J. Med. Chem. 48: 4061-4067.
    • (2005) J. Med. Chem. , vol.48 , pp. 4061-4067
    • Velázquez, C.1    Praveen Rao, P.N.2    Knaus, E.E.3
  • 15
    • 14344255689 scopus 로고    scopus 로고
    • Positional isomerism markedly affects the growth inhibition of colon cancer cells by nitric oxide-donating aspirin in vitro and in vivo
    • Kashfi, K., S. Borgo, J. L. Williams, J. Chen, J. Gao, A. Glekas, F. Benedini, P. Del Soldato, and B. Rigas. 2005. Positional isomerism markedly affects the growth inhibition of colon cancer cells by nitric oxide-donating aspirin in vitro and in vivo. J. Pharmacol. Exp. Ther. 312: 978-988.
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 978-988
    • Kashfi, K.1    Borgo, S.2    Williams, J.L.3    Chen, J.4    Gao, J.5    Glekas, A.6    Benedini, F.7    Del Soldato, P.8    Rigas, B.9
  • 16
    • 0343628040 scopus 로고    scopus 로고
    • A common pathway for nitric oxide release from NO-aspirin and glyceryl trinitrate
    • Grosser, N., and H. Schröder. 2000. A common pathway for nitric oxide release from NO-aspirin and glyceryl trinitrate. Biochem. Biophys. Res. Commun. 274: 255-258.
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 255-258
    • Grosser, N.1    Schröder, H.2
  • 17
    • 0036681476 scopus 로고    scopus 로고
    • In vitro metabolism of a nitroderivative of acetylsalicylic acid (NCX4016) by rat liver: LC and LC-MS studies
    • Carini, M., G. Aldini, M. Orioli, and R. Maffei Facino. 2002. In vitro metabolism of a nitroderivative of acetylsalicylic acid (NCX4016) by rat liver: LC and LC-MS studies. J. Pharm. Biomed. Anal. 29: 1061-1071.
    • (2002) J. Pharm. Biomed. Anal. , vol.29 , pp. 1061-1071
    • Carini, M.1    Aldini, G.2    Orioli, M.3    Maffei Facino, R.4
  • 18
    • 14344262182 scopus 로고    scopus 로고
    • In vitro metabolism of nitric oxide-donating aspirin: The effect of positional isomerism
    • Gao, J., K. Kashfi, and B. Rigas. 2005. In vitro metabolism of nitric oxide-donating aspirin: the effect of positional isomerism. J. Pharmacol. Exp. Ther. 312: 989-997.
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 989-997
    • Gao, J.1    Kashfi, K.2    Rigas, B.3
  • 19
    • 47049119551 scopus 로고    scopus 로고
    • NCX 4040, an NO-donating acetylsalicylic acid derivative: Efficacy and mechanisms of action in cancer cells
    • Tesei, A., W. Zoli, F. Fabbri, C. Leonetti, M. Rosetti, M. Bolla, D. Amadori, and R. Silvestrini. 2008. NCX 4040, an NO-donating acetylsalicylic acid derivative: efficacy and mechanisms of action in cancer cells. Nitric Oxide 19: 225-236.
    • (2008) Nitric Oxide , vol.19 , pp. 225-236
    • Tesei, A.1    Zoli, W.2    Fabbri, F.3    Leonetti, C.4    Rosetti, M.5    Bolla, M.6    Amadori, D.7    Silvestrini, R.8
  • 20
    • 47049098556 scopus 로고    scopus 로고
    • Nitrates and NO-NSAIDs in cancer chemoprevention and therapy: In vitro evidence querying the NO donor functionality
    • Dunlap, T., S. O. Abdul-Hay, R. E. Chandrasena, G. K. Hagos, V. Sinha, Z. Wang, H. Wang, and G. R. Thatcher. 2008. Nitrates and NO-NSAIDs in cancer chemoprevention and therapy: in vitro evidence querying the NO donor functionality. Nitric Oxide 19: 115-124.
    • (2008) Nitric Oxide , vol.19 , pp. 115-124
    • Dunlap, T.1    Abdul-Hay, S.O.2    Chandrasena, R.E.3    Hagos, G.K.4    Sinha, V.5    Wang, Z.6    Wang, H.7    Thatcher, G.R.8
  • 21
    • 34249008406 scopus 로고    scopus 로고
    • Chemical insights in the concept of hybrid drugs: The antitumor effect of nitric oxide-donating aspirin involves a quinone methide but not nitric oxide nor aspirin
    • Hulsman, N., J. P. Medema, C. Bos, A. Jongejan, R. Leurs, M. J. Smit, I. J. de Esch, D. Richel, and M. Wijtmans. 2007. Chemical insights in the concept of hybrid drugs: the antitumor effect of nitric oxide-donating aspirin involves a quinone methide but not nitric oxide nor aspirin. J. Med. Chem. 50: 2424-2431.
    • (2007) J. Med. Chem. , vol.50 , pp. 2424-2431
    • Hulsman, N.1    Medema, J.P.2    Bos, C.3    Jongejan, A.4    Leurs, R.5    Smit, M.J.6    De Esch, I.J.7    Richel, D.8    Wijtmans, M.9
  • 22
    • 34249657760 scopus 로고    scopus 로고
    • The mechanism of action of nitric oxide-donating aspirin
    • Kashfi, K., and B. Rigas. 2007. The mechanism of action of nitric oxide-donating aspirin. Biochem. Biophys. Res. Commun. 358: 1096-1101.
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 1096-1101
    • Kashfi, K.1    Rigas, B.2
  • 23
    • 0034450123 scopus 로고    scopus 로고
    • Molecular mechanisms of NF-κB activation induced by bacterial lipopolysaccharide through Toll-like receptors
    • Zhang, G., and S. Ghosh. 2000. Molecular mechanisms of NF-κB activation induced by bacterial lipopolysaccharide through Toll-like receptors. J. Endotoxin Res. 6: 453-457.
    • (2000) J. Endotoxin Res. , vol.6 , pp. 453-457
    • Zhang, G.1    Ghosh, S.2
  • 24
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-kB activity
    • Karin, M., and Y. Ben-Neriah. 2000. Phosphorylation meets ubiquitination: the control of NF-kB activity. Annu. Rev. Immunol. 18: 621-663.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 28
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D. H., and A. L. Goldberg. 1998. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8: 397-403.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 29
    • 0029122910 scopus 로고
    • Potent and selective inhibition of nitric oxide-sensitive guanylyl cyclase by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one
    • Garthwaite, J., E. Southam, C. L. Boulton, E. B. Nielsen, K. Schmidt, and B. Mayer. 1995. Potent and selective inhibition of nitric oxide-sensitive guanylyl cyclase by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one. Mol. Pharmacol. 48: 184-188.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 184-188
    • Garthwaite, J.1    Southam, E.2    Boulton, C.L.3    Nielsen, E.B.4    Schmidt, K.5    Mayer, B.6
  • 32
    • 0034327850 scopus 로고    scopus 로고
    • IL-1b converting enzyme is a target for nitric oxide-releasing aspirin: New insights in the antiinflammatory mechanism of nitric oxide-releasing nonsteroidal antiinflammatory drugs
    • Fiorucci, S., L. Santucci, G. Cirino, A. Mencarelli, L. Familiari, P. D. Soldato, and A. Morelli. 2000. IL-1b converting enzyme is a target for nitric oxide-releasing aspirin: new insights in the antiinflammatory mechanism of nitric oxide-releasing nonsteroidal antiinflammatory drugs. J. Immunol. 165: 5245-5254.
    • (2000) J. Immunol. , vol.165 , pp. 5245-5254
    • Fiorucci, S.1    Santucci, L.2    Cirino, G.3    Mencarelli, A.4    Familiari, L.5    Soldato, P.D.6    Morelli, A.7
  • 34
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev, A. F., and A. L. Goldberg. 2001. Proteasome inhibitors: from research tools to drug candidates. Chem. Biol. 8: 739-758.
    • (2001) Chem. Biol. , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 35
    • 0036104603 scopus 로고    scopus 로고
    • Not just research tools - Proteasome inhibitors offer therapeutic promise
    • Goldberg, A. L., and K. Rock. 2002. Not just research tools - proteasome inhibitors offer therapeutic promise. Nat. Med. 8: 338-340.
    • (2002) Nat. Med. , vol.8 , pp. 338-340
    • Goldberg, A.L.1    Rock, K.2
  • 36
    • 3042837373 scopus 로고    scopus 로고
    • Nitric-oxide-donating NSAIDs as agents for cancer prevention
    • Rigas, B., and K. Kashfi. 2004. Nitric-oxide-donating NSAIDs as agents for cancer prevention. Trends Mol. Med. 10: 324-330.
    • (2004) Trends Mol. Med. , vol.10 , pp. 324-330
    • Rigas, B.1    Kashfi, K.2
  • 38
    • 0142195896 scopus 로고    scopus 로고
    • Aspirin insensitive eicosanoid biosynthesis in cardiovascular disease
    • Patrignani, P. 2003. Aspirin insensitive eicosanoid biosynthesis in cardiovascular disease. Thromb. Res. 110: 281-286.
    • (2003) Thromb. Res. , vol.110 , pp. 281-286
    • Patrignani, P.1
  • 40
    • 0034816925 scopus 로고    scopus 로고
    • Cyclooxygenase-independent actions of cyclooxygenase inhibitors
    • Tegeder, I., J. Pfeilschifter, and G. Geisslinger. 2001. Cyclooxygenase-independent actions of cyclooxygenase inhibitors. FASEB J. 15: 2057-2072.
    • (2001) FASEB J. , vol.15 , pp. 2057-2072
    • Tegeder, I.1    Pfeilschifter, J.2    Geisslinger, G.3
  • 41
    • 0028167846 scopus 로고
    • Inhibition of NF-kappaB by sodium salicylate and aspirin
    • Kopp, E., and S. Ghosh. 1994. Inhibition of NF-κB by sodium salicylate and aspirin. Science 265: 956-959. (Pubitemid 2115182)
    • (1994) Science , vol.265 , Issue.5174 , pp. 956-959
    • Kopp, E.1    Ghosh, S.2
  • 42
    • 0032487857 scopus 로고    scopus 로고
    • The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β
    • Yin, M. J., Y. Yamamoto, and R. B. Gaynor. 1998. The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β. Nature 396: 77-80.
    • (1998) Nature , vol.396 , pp. 77-80
    • Yin, M.J.1    Yamamoto, Y.2    Gaynor, R.B.3
  • 44
    • 33749404802 scopus 로고    scopus 로고
    • Aspirin induces apoptosis through the inhibition of proteasome function
    • Dikshit, P., M. Chatterjee, A. Goswami, A. Mishra, and N. R. Jana. 2006. Aspirin induces apoptosis through the inhibition of proteasome function. J. Biol. Chem. 281: 29228-29235.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29228-29235
    • Dikshit, P.1    Chatterjee, M.2    Goswami, A.3    Mishra, A.4    Jana, N.R.5
  • 45
    • 0027530664 scopus 로고
    • The gastrointestinal toxicity of aspirin: An overview of randomised controlled trials
    • Roderick, P. J., H. C. Wilkes, and T. W. Meade. 1993. The gastrointestinal toxicity of aspirin: an overview of randomised controlled trials. Br. J. Clin. Pharmacol. 35: 219-226.
    • (1993) Br. J. Clin. Pharmacol. , vol.35 , pp. 219-226
    • Roderick, P.J.1    Wilkes, H.C.2    Meade, T.W.3
  • 48
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding machines
    • Elsasser, S., and D. Finley. 2005. Delivery of ubiquitinated substrates to protein-unfolding machines. Nat. Cell Biol. 7: 742-749.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 742-749
    • Elsasser, S.1    Finley, D.2
  • 49
    • 32644481227 scopus 로고    scopus 로고
    • Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction
    • Goswami, A., P. Dikshit, A. Mishra, S. Mulherkar, N. Nukina, and N. R. Jana. 2006. Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction. Biochem. Biophys. Res. Commun. 342: 184-190.
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 184-190
    • Goswami, A.1    Dikshit, P.2    Mishra, A.3    Mulherkar, S.4    Nukina, N.5    Jana, N.R.6
  • 50
    • 0035869450 scopus 로고    scopus 로고
    • Biphasic regulation of NF-κB activity underlies the pro- And anti-inflammatory actions of nitric oxide
    • Connelly, L., M. Palacios-Callender, C. Ameixa, S. Moncada, and A. J. Hobbs. 2001. Biphasic regulation of NF-κB activity underlies the pro- and antiinflammatory actions of nitric oxide. J. Immunol. 166: 3873-3881. (Pubitemid 32224913)
    • (2001) Journal of Immunology , vol.166 , Issue.6 , pp. 3873-3881
    • Connelly, L.1    Palacios-Callender, M.2    Ameixa, C.3    Moncada, S.4    Hobbs, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.