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Volumn 107, Issue 1, 2010, Pages 28-33

Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1

Author keywords

Adrenic acid; Arachidonic acid; Nonsteroidal antiinflammatory drugs; Platelet; Prostaglandin

Indexed keywords

5 BROMO 2 (4 FLUOROPHENYL) 3 (4 METHYLSULFONYLPHENYL)THIOPHENE; ACETYLSALICYLIC ACID; ARACHIDONIC ACID; CELECOXIB; CYCLOOXYGENASE 1; DIMER; IBUPROFEN; INDOMETACIN; MONOMER; N (2 CYCLOHEXYLOXY 4 NITROPHENYL)METHANESULFONAMIDE; NIMESULIDE;

EID: 76249130338     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0909765106     Document Type: Article
Times cited : (165)

References (48)
  • 1
    • 0037207124 scopus 로고    scopus 로고
    • The cyclooxygenase reaction mechanism
    • van der Donk W, Tsai A, Kulmacz R (2002) The cyclooxygenase reaction mechanism. Biochemistry, 41(52):15451-15458.
    • (2002) Biochemistry , vol.41 , Issue.52 , pp. 15451-15458
    • van der Donk, W.1    Tsai, A.2    Kulmacz, R.3
  • 2
    • 0037898985 scopus 로고    scopus 로고
    • Mechanism of free radical oxygenation of polyunsaturated fatty acids by cyclooxygenases
    • Rouzer C, Marnett L (2003) Mechanism of free radical oxygenation of polyunsaturated fatty acids by cyclooxygenases. Chem Rev, 103(6):2239-2304.
    • (2003) Chem Rev , vol.103 , Issue.6 , pp. 2239-2304
    • Rouzer, C.1    Marnett, L.2
  • 3
    • 37749018414 scopus 로고    scopus 로고
    • Nutritionally essential fatty acids and biologically indispensable cyclooxygenases
    • Smith WL (2008) Nutritionally essential fatty acids and biologically indispensable cyclooxygenases. Trends Biochem Sci, 33(1):27-37.
    • (2008) Trends Biochem Sci , vol.33 , Issue.1 , pp. 27-37
    • Smith, W.L.1
  • 4
    • 34248596797 scopus 로고    scopus 로고
    • Control of oxygenation in lipoxygenase and cyclooxygenase catalysis
    • Schneider C, Pratt DA, Porter NA, Brash AR (2007) Control of oxygenation in lipoxygenase and cyclooxygenase catalysis. Chem Biol, 14(5):473-488.
    • (2007) Chem Biol , vol.14 , Issue.5 , pp. 473-488
    • Schneider, C.1    Pratt, D.A.2    Porter, N.A.3    Brash, A.R.4
  • 5
    • 43749115768 scopus 로고    scopus 로고
    • Non-redundant Functions of Cyclooxygenases: Oxygenation of Endocannabinoids
    • Rouzer CA, Marnett LJ (2008) Non-redundant Functions of Cyclooxygenases: Oxygenation of Endocannabinoids. J Biol Chem, 283(13):8065-8069.
    • (2008) J Biol Chem , vol.283 , Issue.13 , pp. 8065-8069
    • Rouzer, C.A.1    Marnett, L.J.2
  • 6
    • 31044441042 scopus 로고    scopus 로고
    • Biological basis for the cardiovascular consequences of COX-2 inhibition: Therapeutic challenges and opportunities
    • Grosser T, Fries S, FitzGerald GA (2006) Biological basis for the cardiovascular consequences of COX-2 inhibition: Therapeutic challenges and opportunities. J Clin Invest, 116(1):4-15.
    • (2006) J Clin Invest , vol.116 , Issue.1 , pp. 4-15
    • Grosser, T.1    Fries, S.2    FitzGerald, G.A.3
  • 8
    • 65649108576 scopus 로고    scopus 로고
    • Cyclooxygenase allosterism, fatty acid-mediated cross-talk between monomers of cyclooxygenase homodimers
    • Yuan C, et al. (2009) Cyclooxygenase allosterism, fatty acid-mediated cross-talk between monomers of cyclooxygenase homodimers. J Biol Chem, 284(15):10046-10055.
    • (2009) J Biol Chem , vol.284 , Issue.15 , pp. 10046-10055
    • Yuan, C.1
  • 9
    • 0022382640 scopus 로고
    • Stoichiometry and kinetics of the interaction of prostaglandin H synthase with anti-inflammatory agents
    • Kulmacz RJ, Lands WEM (1985) Stoichiometry and kinetics of the interaction of prostaglandin H synthase with anti-inflammatory agents. J Biol Chem, 260(23):12572-12578.
    • (1985) J Biol Chem , vol.260 , Issue.23 , pp. 12572-12578
    • Kulmacz, R.J.1    Lands, W.E.M.2
  • 10
    • 68249100483 scopus 로고    scopus 로고
    • Differential sensitivity and mechanism of inhibition of COX-2 oxygenation of arachidonic acid and 2-arachidonoylglycerol by ibuprofen and mefenamic acid
    • Prusakiewicz J, Duggan K, Rouzer C, Marnett L (2009) Differential sensitivity and mechanism of inhibition of COX-2 oxygenation of arachidonic acid and 2-arachidonoylglycerol by ibuprofen and mefenamic acid. Biochemistry, 49:7353-7355.
    • (2009) Biochemistry , vol.49 , pp. 7353-7355
    • Prusakiewicz, J.1    Duggan, K.2    Rouzer, C.3    Marnett, L.4
  • 11
    • 0032816884 scopus 로고    scopus 로고
    • PGHS-2 inhibitors, NS-398 and DuP-697, attenuate the inhibition of PGHS-1 by aspirin and indomethacin without altering its activity
    • Rosenstock M, Danon A, Rimon G (1999) PGHS-2 inhibitors, NS-398 and DuP-697, attenuate the inhibition of PGHS-1 by aspirin and indomethacin without altering its activity. Biochim Biophys Acta, 1440(1):127-137.
    • (1999) Biochim Biophys Acta , vol.1440 , Issue.1 , pp. 127-137
    • Rosenstock, M.1    Danon, A.2    Rimon, G.3
  • 12
    • 0035910355 scopus 로고    scopus 로고
    • Prostaglandin H synthase-2 inhibitors interfere with prostaglandin H synthase-1 inhibition by nonsteroidal antiinflammatory drugs
    • Rosenstock M, Danon A, Rubin M, Rimon G (2001) Prostaglandin H synthase-2 inhibitors interfere with prostaglandin H synthase-1 inhibition by nonsteroidal antiinflammatory drugs. Eur J Pharmacol, 412(1):101-108.
    • (2001) Eur J Pharmacol , vol.412 , Issue.1 , pp. 101-108
    • Rosenstock, M.1    Danon, A.2    Rubin, M.3    Rimon, G.4
  • 13
    • 0037174840 scopus 로고    scopus 로고
    • On the interaction of specific prostaglandin H synthase-2 inhibitors with prostaglandin H synthase-1
    • Burde T, Rimon G (2002) On the interaction of specific prostaglandin H synthase-2 inhibitors with prostaglandin H synthase-1. Eur J Pharmacol, 453:167-173.
    • (2002) Eur J Pharmacol , vol.453 , pp. 167-173
    • Burde, T.1    Rimon, G.2
  • 14
    • 0035807799 scopus 로고    scopus 로고
    • A high level of cyclooxygenase-2 inhibitor selectivity is associated with a reduced interference of platelet cyclooxygenase-1 inactivation by aspirin
    • Ouellet M, Riendeau D, Percival MD (2001) A high level of cyclooxygenase-2 inhibitor selectivity is associated with a reduced interference of platelet cyclooxygenase-1 inactivation by aspirin. Proc Natl Acad Sci USA, 98(25):14583-14588.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.25 , pp. 14583-14588
    • Ouellet, M.1    Riendeau, D.2    Percival, M.D.3
  • 15
    • 0036708029 scopus 로고    scopus 로고
    • Celecoxib does not affect the antiplatelet activity of aspirin in healthy volunteers
    • K Wilner, et al. (2002) Celecoxib does not affect the antiplatelet activity of aspirin in healthy volunteers. J Clin Pharmacol, 42(9):1027-1030.
    • (2002) J Clin Pharmacol , vol.42 , Issue.9 , pp. 1027-1030
    • Wilner, K.1
  • 16
    • 41249103710 scopus 로고    scopus 로고
    • The antiplatelet effect of six non-steroidal anti-inflammatory drugs and their pharmacodynamic interaction with aspirin in healthy volunteers
    • Gladding P, et al. (2008) The antiplatelet effect of six non-steroidal anti-inflammatory drugs and their pharmacodynamic interaction with aspirin in healthy volunteers. Am J Cardiol, 101(7):1060-1063.
    • (2008) Am J Cardiol , vol.101 , Issue.7 , pp. 1060-1063
    • Gladding, P.1
  • 17
    • 0033730933 scopus 로고    scopus 로고
    • A new cyclooxygenase-2 inhibitor, rofecoxib (VIOXX), did not alter the antiplatelet effects of low-dose aspirin in healthy volunteers
    • Greenberg HE, et al. (2000) A new cyclooxygenase-2 inhibitor, rofecoxib (VIOXX), did not alter the antiplatelet effects of low-dose aspirin in healthy volunteers. J Clin Pharmacol, 40(12):1509-1515.
    • (2000) J Clin Pharmacol , vol.40 , Issue.12 , pp. 1509-1515
    • Greenberg, H.E.1
  • 18
    • 0035924765 scopus 로고    scopus 로고
    • Cyclooxygenase inhibitors and the antiplatelet effects of aspirin
    • Catella-Lawson F, et al. (2001) Cyclooxygenase inhibitors and the antiplatelet effects of aspirin. N Engl J Med, 345(25):1809-1817.
    • (2001) N Engl J Med , vol.345 , Issue.25 , pp. 1809-1817
    • Catella-Lawson, F.1
  • 19
    • 42449093389 scopus 로고    scopus 로고
    • Cardiovascular risk of celecoxib in 6 randomized placebocontrolled trials: The cross trial safety analysis
    • Solomon SD, et al. (2008) Cardiovascular risk of celecoxib in 6 randomized placebocontrolled trials: The cross trial safety analysis. Circulation, 117(16):2104-2113.
    • (2008) Circulation , vol.117 , Issue.16 , pp. 2104-2113
    • Solomon, S.D.1
  • 20
    • 0035859802 scopus 로고    scopus 로고
    • Effects of selective cyclooxygenase-2 inhibition on vascular responses and thrombosis in canine coronary arteries
    • Hennan JK, et al. (2001) Effects of selective cyclooxygenase-2 inhibition on vascular responses and thrombosis in canine coronary arteries. Circulation, 104(7):820-825.
    • (2001) Circulation , vol.104 , Issue.7 , pp. 820-825
    • Hennan, J.K.1
  • 21
    • 0028139275 scopus 로고
    • Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase
    • Copeland RA, et al. (1994) Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase. Proc Natl Acad Sci USA, 91(23):11202-11206.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.23 , pp. 11202-11206
    • Copeland, R.A.1
  • 22
    • 0027986841 scopus 로고
    • Differential inhibition of human prostaglandin endoperoxide H synthases-1 and -2 by nonsteroidal anti-inflammatory drugs
    • Laneuville O, et al. (1994) Differential inhibition of human prostaglandin endoperoxide H synthases-1 and -2 by nonsteroidal anti-inflammatory drugs. J Pharmacol Exp Ther, 271(2):927-934.
    • (1994) J Pharmacol Exp Ther , vol.271 , Issue.2 , pp. 927-934
    • Laneuville, O.1
  • 23
    • 0033546297 scopus 로고    scopus 로고
    • The role of arginine 120 of human prostaglandin endoperoxide H synthase-2 in the interaction with fatty acid substrates and inhibitors
    • Rieke CJ, Mulichak AM, Garavito RM, Smith WL (1999) The role of arginine 120 of human prostaglandin endoperoxide H synthase-2 in the interaction with fatty acid substrates and inhibitors. J Biol Chem, 274(24):17109-17114.
    • (1999) J Biol Chem , vol.274 , Issue.24 , pp. 17109-17114
    • Rieke, C.J.1    Mulichak, A.M.2    Garavito, R.M.3    Smith, W.L.4
  • 24
    • 0035425205 scopus 로고    scopus 로고
    • A three-step kinetic mechanism for selective inhibition of cyclo-oxygenase-2 by diarylheterocyclic inhibitors
    • Walker M, et al. (2001) A three-step kinetic mechanism for selective inhibition of cyclo-oxygenase-2 by diarylheterocyclic inhibitors. Biochem J, 357(Pt 3):709-718.
    • (2001) Biochem J , vol.357 , Issue.PART 3 , pp. 709-718
    • Walker, M.1
  • 25
    • 33745981772 scopus 로고    scopus 로고
    • Divergent cyclooxygenase responses to fatty acid structure and peroxide level in fish and mammalian prostaglandin H synthases
    • LiuW, Cao D, Oh SF, Serhan CN, Kulmacz RJ (2006) Divergent cyclooxygenase responses to fatty acid structure and peroxide level in fish and mammalian prostaglandin H synthases. FASEB J, 20(8):1097-1108.
    • (2006) FASEB J , vol.20 , Issue.8 , pp. 1097-1108
    • Liu, W.1    Cao, D.2    Oh, S.F.3    Serhan, C.N.4    Kulmacz, R.J.5
  • 26
    • 33845436304 scopus 로고    scopus 로고
    • The cyclooxygenase 2 genetic variant -765G>C does not modulate the effects of celecoxib on prostaglandin E2 production
    • Skarke C, et al. (2006) The cyclooxygenase 2 genetic variant -765G>C does not modulate the effects of celecoxib on prostaglandin E2 production. Clin Pharmacol Ther, 80 (6):621-632.
    • (2006) Clin Pharmacol Ther , vol.80 , Issue.6 , pp. 621-632
    • Skarke, C.1
  • 27
    • 46949094133 scopus 로고    scopus 로고
    • Determination of acetylsalicylic acid and its major metabolite, salicylic acid, in human plasma using liquid chromatography-tandem mass spectrometry: Application to pharmacokinetic study of Astrix in Korean healthy volunteers
    • Bae SK, et al. (2008) Determination of acetylsalicylic acid and its major metabolite, salicylic acid, in human plasma using liquid chromatography-tandem mass spectrometry: Application to pharmacokinetic study of Astrix in Korean healthy volunteers. Biomed Chromatogr, 22(6):590-595.
    • (2008) Biomed Chromatogr , vol.22 , Issue.6 , pp. 590-595
    • Bae, S.K.1
  • 28
    • 39149103679 scopus 로고    scopus 로고
    • Prevalence of platelet nonresponsiveness to aspirin in patients treated for secondary stroke prophylaxis and in patients with recurrent ischemic events
    • Gengo FM, et al. (2008) Prevalence of platelet nonresponsiveness to aspirin in patients treated for secondary stroke prophylaxis and in patients with recurrent ischemic events. J Clin Pharmacol, 48(3):335-343.
    • (2008) J Clin Pharmacol , vol.48 , Issue.3 , pp. 335-343
    • Gengo, F.M.1
  • 29
    • 0032916736 scopus 로고    scopus 로고
    • Cox-2-selective inhibitors: The new super aspirins
    • DeWitt DL (1999) Cox-2-selective inhibitors: The new super aspirins. Mol Pharmacol, 55 (4):625-631.
    • (1999) Mol Pharmacol , vol.55 , Issue.4 , pp. 625-631
    • DeWitt, D.L.1
  • 30
    • 39349118197 scopus 로고    scopus 로고
    • Nimesulide is a selective COX-2 inhibitory, atypical nonsteroidal anti-inflammatory drug
    • Suleyman H, Cadirci E (2008) Nimesulide is a selective COX-2 inhibitory, atypical nonsteroidal anti-inflammatory drug. Curr Med Chem, 15:278-283.
    • (2008) Curr Med Chem , vol.15 , pp. 278-283
    • Suleyman, H.1    Cadirci, E.2
  • 31
    • 0029911267 scopus 로고    scopus 로고
    • Flexibility of the NSAID binding site in the structure of human cylcooxygenase-2
    • Luong C, et al. (1996) Flexibility of the NSAID binding site in the structure of human cylcooxygenase-2. Nat Struct Biol, 3:927-933.
    • (1996) Nat Struct Biol , vol.3 , pp. 927-933
    • Luong, C.1
  • 32
    • 0030461132 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents
    • Kurumbail RG, et al. (1996) Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents. Nature, 384(6610):644-648.
    • (1996) Nature , vol.384 , Issue.6610 , pp. 644-648
    • Kurumbail, R.G.1
  • 33
    • 0034665857 scopus 로고    scopus 로고
    • The x-ray crystal structure of prostaglandin endoperoxide H synthase-1 complexed with arachidonic acid
    • Malkowski MG, Ginell S, Smith WL, Garavito RM (2000) The x-ray crystal structure of prostaglandin endoperoxide H synthase-1 complexed with arachidonic acid. Science, 289:1933-1937.
    • (2000) Science , vol.289 , pp. 1933-1937
    • Malkowski, M.G.1    Ginell, S.2    Smith, W.L.3    Garavito, R.M.4
  • 34
    • 34547137409 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide H synthases: Peroxidase hydroperoxide specificity and cyclooxygenase activation
    • Liu J, et al. (2007) Prostaglandin endoperoxide H synthases: Peroxidase hydroperoxide specificity and cyclooxygenase activation. J Biol Chem, 282:18233-18244.
    • (2007) J Biol Chem , vol.282 , pp. 18233-18244
    • Liu, J.1
  • 35
    • 34547958615 scopus 로고    scopus 로고
    • Specificities of enzymes and receptors of prostaglandin pathways with arachidonic acid and eicosapentaenoic acid derived substrates and products
    • Wada M, et al. (2007) Specificities of enzymes and receptors of prostaglandin pathways with arachidonic acid and eicosapentaenoic acid derived substrates and products. J Biol Chem, 282:22254-22266.
    • (2007) J Biol Chem , vol.282 , pp. 22254-22266
    • Wada, M.1
  • 36
    • 40649109492 scopus 로고    scopus 로고
    • Acetylation of prostaglandin H2 synthases by aspirin is inhibited by redox cycling of the peroxidase
    • Bala M, et al. (2008) Acetylation of prostaglandin H2 synthases by aspirin is inhibited by redox cycling of the peroxidase. Biochem Pharmacol, 75(7):1472-1481.
    • (2008) Biochem Pharmacol , vol.75 , Issue.7 , pp. 1472-1481
    • Bala, M.1
  • 37
    • 5644259546 scopus 로고    scopus 로고
    • Crystal structure of arachidonic acid bound to a mutant of prostaglandin endoperoxide H synthase-1 that forms predominantly 11-hydroperoxyeicosatetraenoic acid
    • Harman CA, Rieke CJ, Garavito RM, Smith WL (2004) Crystal structure of arachidonic acid bound to a mutant of prostaglandin endoperoxide H synthase-1 that forms predominantly 11-hydroperoxyeicosatetraenoic acid. J Biol Chem, 279(41):42929-42935.
    • (2004) J Biol Chem , vol.279 , Issue.41 , pp. 42929-42935
    • Harman, C.A.1    Rieke, C.J.2    Garavito, R.M.3    Smith, W.L.4
  • 38
    • 34948902032 scopus 로고    scopus 로고
    • Structural basis of enantioselective inhibition of cyclooxygenase-1 by S-{alpha}-substituted indomethacin ethanolamides
    • Harman CA, et al. (2007) Structural basis of enantioselective inhibition of cyclooxygenase-1 by S-{alpha}-substituted indomethacin ethanolamides. J Biol Chem, 282(38): 28096-28105.
    • (2007) J Biol Chem , vol.282 , Issue.38 , pp. 28096-28105
    • Harman, C.A.1
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of x-ray diffraction data collected in oscillation mode. Method Enzymol, 276:307-326.
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D, 58(Pt 11):1948-1954.
    • (2002) Acta Crystallogr D , vol.58 , Issue.PART 11 , pp. 1948-1954
    • Adams, P.D.1
  • 42
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf AW, van Aalten DM (2004) PRODRG: A tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr D, 60(Pt 8):1355-1363.
    • (2004) Acta Crystallogr D , vol.60 , Issue.PART 8 , pp. 1355-1363
    • Schuttelkopf, A.W.1    van Aalten, D.M.2
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Pt 1
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr, 60(Pt 12, Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 44
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthurMW, Moss DS, Thornton JM (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst, 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 45
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res, 35(Suppl 2):W375-383.
    • (2007) Nucleic Acids Res , vol.35 , Issue.SUPPL. 2
    • Davis, I.W.1
  • 47
    • 0030659457 scopus 로고    scopus 로고
    • PDBsum: A web-based database of summaries and analyses of all PDB structures
    • Laskowski R, et al. (1997) PDBsum: A web-based database of summaries and analyses of all PDB structures. Trends Biochem Sci, 22(12):488-490.
    • (1997) Trends Biochem Sci , vol.22 , Issue.12 , pp. 488-490
    • Laskowski, R.1


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