메뉴 건너뛰기




Volumn 36, Issue 1, 2009, Pages 122-136

Kinetic modelling of NSAID action on COX-1: Focus on in vitro/in vivo aspects and drug combinations

Author keywords

Aspirin; Celecoxib; Cyclooxygenase; Drug combination; Kinetic model; NSAID

Indexed keywords

ACETYLSALICYLIC ACID; ARACHIDONIC ACID; CELECOXIB; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; ETORICOXIB; INDOMETACIN; NAPROXEN; NONSTEROID ANTIINFLAMMATORY AGENT; PEROXIDASE; PROSTAGLANDIN SYNTHASE; THROMBOXANE; VALDECOXIB;

EID: 58149136055     PISSN: 09280987     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejps.2008.10.015     Document Type: Article
Times cited : (19)

References (29)
  • 1
    • 1042289786 scopus 로고    scopus 로고
    • Role of Asn-382 and Thr-383 in activation and inactivation of human prostaglandin H synthase cyclooxygenase catalysis
    • Bambai B., Rogge C.E., Stec B., and Kulmacz R.J. Role of Asn-382 and Thr-383 in activation and inactivation of human prostaglandin H synthase cyclooxygenase catalysis. J. Biol. Chem. 279 (2004) 4084-4092
    • (2004) J. Biol. Chem. , vol.279 , pp. 4084-4092
    • Bambai, B.1    Rogge, C.E.2    Stec, B.3    Kulmacz, R.J.4
  • 2
    • 0034983085 scopus 로고    scopus 로고
    • Arachidonic acid as a bioactive molecule
    • Brash A.R. Arachidonic acid as a bioactive molecule. J. Clin. Invest. 107 (2001) 1339-1345
    • (2001) J. Clin. Invest. , vol.107 , pp. 1339-1345
    • Brash, A.R.1
  • 4
    • 0018088932 scopus 로고
    • Sensitivity of fatty acid cyclooxygenase from human aorta to acetylation by aspirin
    • Burch J.W., Baenziger N.L., Stanford N., and Majerus P.W. Sensitivity of fatty acid cyclooxygenase from human aorta to acetylation by aspirin. Proc. Natl. Acad. Sci. U.S.A. 75 (1978) 5181-5184
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 5181-5184
    • Burch, J.W.1    Baenziger, N.L.2    Stanford, N.3    Majerus, P.W.4
  • 5
    • 0030063502 scopus 로고    scopus 로고
    • The kinetic factors that determine the affinity and selectivity for slow binding inhibition of human prostaglandin H synthase 1 and 2 by indomethacin and flurbiprofen
    • Callan O.H., So O.-Y., and Swinney D.C. The kinetic factors that determine the affinity and selectivity for slow binding inhibition of human prostaglandin H synthase 1 and 2 by indomethacin and flurbiprofen. J. Biol. Chem. 271 (1996) 3548-3554
    • (1996) J. Biol. Chem. , vol.271 , pp. 3548-3554
    • Callan, O.H.1    So, O.-Y.2    Swinney, D.C.3
  • 8
    • 0033575249 scopus 로고    scopus 로고
    • Hydroperoxide dependence and cooperative cyclooxygenase kinetics in prostaglandin H synthase-1 and -2
    • Chen W., Pawelek T.R., and Kulmacz R.J. Hydroperoxide dependence and cooperative cyclooxygenase kinetics in prostaglandin H synthase-1 and -2. J. Biol. Chem. 274 (1999) 20301-20306
    • (1999) J. Biol. Chem. , vol.274 , pp. 20301-20306
    • Chen, W.1    Pawelek, T.R.2    Kulmacz, R.J.3
  • 9
    • 1542499456 scopus 로고    scopus 로고
    • The case for an adverse interaction between aspirin and non-steroidal anti-inflammatory drugs: is it time to believe the hype?
    • Curtis J.P., and Krumholz H.M. The case for an adverse interaction between aspirin and non-steroidal anti-inflammatory drugs: is it time to believe the hype?. J. Am. Coll. Cardiol. 43 (2004) 991-993
    • (2004) J. Am. Coll. Cardiol. , vol.43 , pp. 991-993
    • Curtis, J.P.1    Krumholz, H.M.2
  • 11
    • 0032825010 scopus 로고    scopus 로고
    • DBsolve: mathematical simulation and analysis of cellular metabolism and regulation
    • Goryanin I., Hodgman T.C., and Selkov E. DBsolve: mathematical simulation and analysis of cellular metabolism and regulation. Bioinformatics 15 (1999) 749-758
    • (1999) Bioinformatics , vol.15 , pp. 749-758
    • Goryanin, I.1    Hodgman, T.C.2    Selkov, E.3
  • 12
    • 31044441042 scopus 로고    scopus 로고
    • Biological basis for the cardiovascular consequences of COX-2 inhibition: therapeutic challenges and opportunities
    • Grosser T., Fries A., and FitzGerald G.A. Biological basis for the cardiovascular consequences of COX-2 inhibition: therapeutic challenges and opportunities. J. Clin. Invest. 116 (2006) 4-15
    • (2006) J. Clin. Invest. , vol.116 , pp. 4-15
    • Grosser, T.1    Fries, A.2    FitzGerald, G.A.3
  • 13
    • 1242340306 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs and cardiovascular risk
    • Howard P.A., and Delafontaine P. Nonsteroidal anti-inflammatory drugs and cardiovascular risk. J. Am. Coll. Cardiol. 43 (2004) 519-525
    • (2004) J. Am. Coll. Cardiol. , vol.43 , pp. 519-525
    • Howard, P.A.1    Delafontaine, P.2
  • 15
    • 0023839665 scopus 로고
    • Higher oxidation states of prostaglandin H synthase. EPR study of a transient tyrosyl radical in the enzyme during the peroxidase reaction
    • Karthein R., Dietz R., Nastainczyk W., and Ruf H.H. Higher oxidation states of prostaglandin H synthase. EPR study of a transient tyrosyl radical in the enzyme during the peroxidase reaction. Eur. J. Biochem. 171 (1988) 313-320
    • (1988) Eur. J. Biochem. , vol.171 , pp. 313-320
    • Karthein, R.1    Dietz, R.2    Nastainczyk, W.3    Ruf, H.H.4
  • 16
    • 0024363551 scopus 로고
    • Topography of prostaglandin H synthase. antiinflammatory agents and the protease-sensitive arginine 253 region
    • Kulmacz R.J. Topography of prostaglandin H synthase. antiinflammatory agents and the protease-sensitive arginine 253 region. J. Biol. Chem. 264 (1989) 14136-14144
    • (1989) J. Biol. Chem. , vol.264 , pp. 14136-14144
    • Kulmacz, R.J.1
  • 17
    • 0028059103 scopus 로고
    • Interaction between peroxidase and cyclooxygenase activities in prostaglandin-endoperoxide synthase. Interpretation of reaction kinetics
    • Kulmacz R.J., Pendleton R.B., and Lands W.E. Interaction between peroxidase and cyclooxygenase activities in prostaglandin-endoperoxide synthase. Interpretation of reaction kinetics. J. Biol. Chem. 269 (1994) 5527-5536
    • (1994) J. Biol. Chem. , vol.269 , pp. 5527-5536
    • Kulmacz, R.J.1    Pendleton, R.B.2    Lands, W.E.3
  • 18
    • 0037567429 scopus 로고    scopus 로고
    • Comparison of the properties of prostaglandin H synthase-1 and -2
    • Kulmacz R.J., van der Donk W.A., and Tsai A.-L. Comparison of the properties of prostaglandin H synthase-1 and -2. Prog. Lipid Res. 42 (2003) 377-404
    • (2003) Prog. Lipid Res. , vol.42 , pp. 377-404
    • Kulmacz, R.J.1    van der Donk, W.A.2    Tsai, A.-L.3
  • 19
    • 0033523008 scopus 로고    scopus 로고
    • Comparison of the peroxidase reaction kinetics of prostaglandin H synthase-1 and -2
    • Lu G., Tsai A.L., Van Wart H.E., and Kulmacz R.J. Comparison of the peroxidase reaction kinetics of prostaglandin H synthase-1 and -2. J. Biol. Chem. 74 (1999) 16162-16177
    • (1999) J. Biol. Chem. , vol.74 , pp. 16162-16177
    • Lu, G.1    Tsai, A.L.2    Van Wart, H.E.3    Kulmacz, R.J.4
  • 20
    • 33845991203 scopus 로고    scopus 로고
    • The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system
    • Mbonye U.R., Wada M., Rieke C.J., Tang H.Y., Dewitt D.L., and Smith W.L. The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system. J. Biol. Chem. 281 (2006) 35770-35778
    • (2006) J. Biol. Chem. , vol.281 , pp. 35770-35778
    • Mbonye, U.R.1    Wada, M.2    Rieke, C.J.3    Tang, H.Y.4    Dewitt, D.L.5    Smith, W.L.6
  • 21
    • 0027146692 scopus 로고
    • Selectivity of nonsteroidal antiinflammatory drugs as inhibitors of constitutive and inducible cyclooxygenase
    • Mitchell J.A., Akarasereenont P., Thiemermann C., Flower R.J., and Vane J.R. Selectivity of nonsteroidal antiinflammatory drugs as inhibitors of constitutive and inducible cyclooxygenase. Proc. Natl. Acad. Sci. U.S.A. 90 (1994) 11693-11697
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 11693-11697
    • Mitchell, J.A.1    Akarasereenont, P.2    Thiemermann, C.3    Flower, R.J.4    Vane, J.R.5
  • 22
    • 33845631867 scopus 로고    scopus 로고
    • Stronger inhibition by nonsteroid anti-inflammatory drugs of cyclooxygenase-1 in endothelial cells than platelets offers an explanation for increased risk of thrombotic events
    • Mitchell J.A., Lucas R., Vojnovic I., Hasan K., Pepper J.R., and Warner T.D. Stronger inhibition by nonsteroid anti-inflammatory drugs of cyclooxygenase-1 in endothelial cells than platelets offers an explanation for increased risk of thrombotic events. FASEB J. 20 (2006) 2468-2475
    • (2006) FASEB J. , vol.20 , pp. 2468-2475
    • Mitchell, J.A.1    Lucas, R.2    Vojnovic, I.3    Hasan, K.4    Pepper, J.R.5    Warner, T.D.6
  • 23
    • 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., and Percival M.D. 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. U.S.A. 98 (2001) 14583-14588
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14583-14588
    • Ouellet, M.1    Riendeau, D.2    Percival, M.D.3
  • 25
    • 0000151210 scopus 로고
    • Structural requirements for time-dependent inhibition of prostaglandin biosynthesis by anti-inflammatory drugs
    • Rome L.H., and Lands W.E.M. Structural requirements for time-dependent inhibition of prostaglandin biosynthesis by anti-inflammatory drugs. Proc. Natl. Acad. Sci. U.S.A. 72 (1975) 4863-4865
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 4863-4865
    • Rome, L.H.1    Lands, W.E.M.2
  • 27
    • 0033594911 scopus 로고    scopus 로고
    • Nonsteroid drug selectivities for cyclo-oxygenase-1 rather than cyclo-oxygenase-2 are associated with human gastrointestinal toxicity: a full in vitro analysis
    • Warner T.D., Giuliano F., Vojnovic I., Bukasa A., Mitchell J.A., and Vane J.R. Nonsteroid drug selectivities for cyclo-oxygenase-1 rather than cyclo-oxygenase-2 are associated with human gastrointestinal toxicity: a full in vitro analysis. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 7563-7568
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7563-7568
    • Warner, T.D.1    Giuliano, F.2    Vojnovic, I.3    Bukasa, A.4    Mitchell, J.A.5    Vane, J.R.6
  • 28
    • 0029005442 scopus 로고
    • Comparison of branched-chain and tightly coupled reaction mechanisms for prostaglandin H synthase
    • Wei C., Kulmacz R.J., and Tsai A.L. Comparison of branched-chain and tightly coupled reaction mechanisms for prostaglandin H synthase. Biochemistry 34 (1995) 8499-8512
    • (1995) Biochemistry , vol.34 , pp. 8499-8512
    • Wei, C.1    Kulmacz, R.J.2    Tsai, A.L.3
  • 29
    • 0344413861 scopus 로고    scopus 로고
    • Cyclooxygenase inactivation kinetics during reaction of prostaglandin H synthase-1 with peroxide
    • Wu G., Kulmacz R.J., and Tsai A.L. Cyclooxygenase inactivation kinetics during reaction of prostaglandin H synthase-1 with peroxide. Biochemistry 42 (2003) 13772-13777
    • (2003) Biochemistry , vol.42 , pp. 13772-13777
    • Wu, G.1    Kulmacz, R.J.2    Tsai, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.