메뉴 건너뛰기




Volumn 48, Issue 51, 2009, Pages 12233-12241

Characterization of an AM404 analogue, N-(3-hydroxyphenyl) arachidonoylamide, as a substrate and inactivator of prostaglandin endoperoxide synthase

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL STUDIES; ARACHIDONATE; ARACHIDONIC ACIDS; COVALENT MODIFICATIONS; ENDOCANNABINOID; ENDOPEROXIDES; HEME MOIETY; META ISOMERS; NO OXIDATION; STRUCTURAL REQUIREMENTS; SYNTHASES;

EID: 73149117125     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901181z     Document Type: Article
Times cited : (4)

References (36)
  • 3
    • 0026735231 scopus 로고
    • cDNA cloning and functional activity of a glucocorticoid-regulated inflammatory cyclooxygenase
    • O'Banion, M. K., Winn, V. D., and Young, D. A. (1992) cDNA cloning and functional activity of a glucocorticoid-regulated inflammatory cyclooxygenase. Proc. Natl. Acad. Sci. U.S.A. 89, 4888-4892.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 4888-4892
    • O'Banion, M.K.1    Winn, V.D.2    Young, D.A.3
  • 4
    • 0025754779 scopus 로고
    • Expression of a mitogen-responsive gene encoding prostaglandin synthase is regulated by mRNA splicing
    • Xie, W. L., Chipman, J. G., Robertson, D. L., Erikson, R. L., and Simmons, D. L. (1991) Expression of a mitogen-responsive gene encoding prostaglandin synthase is regulated by mRNA splicing. Proc. Natl. Acad. Sci. U.S.A. 88, 2692-2696.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 2692-2696
    • Xie, W.L.1    Chipman, J.G.2    Robertson, D.L.3    Erikson, R.L.4    Simmons, D.L.5
  • 8
    • 0033551732 scopus 로고    scopus 로고
    • The binding of arachidonic acid in the cyclooxygenase active site of mouse prostaglandin endoperoxide synthase-2 (COX-2). A putative L-shaped binding conformation utilizing the top channel region
    • Rowlinson, S. W., Crews, B. C., Lanzo, C. A., and Marnett, L. J. (1999) The binding of arachidonic acid in the cyclooxygenase active site of mouse prostaglandin endoperoxide synthase-2 (COX-2). A putative L-shaped binding conformation utilizing the top channel region. J. Biol. Chem. 274, 23305-23310.
    • (1999) J. Biol. Chem , vol.274 , pp. 23305-23310
    • Rowlinson, S.W.1    Crews, B.C.2    Lanzo, C.A.3    Marnett, L.J.4
  • 9
    • 0034665857 scopus 로고    scopus 로고
    • The productive conformation of arachidonic acid bound to prostaglandin synthase
    • Malkowski, M. G., Ginell, S. L., Smith, W. L., and Garavito, R. M. (2000) The productive conformation of arachidonic acid bound to prostaglandin synthase. Science 289, 1933-1937.
    • (2000) Science , vol.289 , pp. 1933-1937
    • Malkowski, M.G.1    Ginell, S.L.2    Smith, W.L.3    Garavito, R.M.4
  • 10
    • 0041664897 scopus 로고    scopus 로고
    • Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid anandamide
    • Kozak, K. R., Prusakiewicz, J. J., Rowlinson, S. W., Prudhomme, D. R., and Marnett, L. J. (2003) Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid anandamide. Biochemistry 42, 9041-9049.
    • (2003) Biochemistry , vol.42 , pp. 9041-9049
    • Kozak, K.R.1    Prusakiewicz, J.J.2    Rowlinson, S.W.3    Prudhomme, D.R.4    Marnett, L.J.5
  • 11
    • 0035839520 scopus 로고    scopus 로고
    • Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid 2-arachidonylglycerol
    • Kozak, K. R., Prusakiewicz, J. J., Rowlinson, S. W., Schneider, C., and Marnett, L. J. (2001) Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid 2-arachidonylglycerol. J. Biol. Chem. 276, 30072-30077.
    • (2001) J. Biol. Chem , vol.276 , pp. 30072-30077
    • Kozak, K.R.1    Prusakiewicz, J.J.2    Rowlinson, S.W.3    Schneider, C.4    Marnett, L.J.5
  • 13
    • 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, C. J., Mulichak, A. M., Garavito, R. M., and Smith, W. L. (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, 17109-17114.
    • (1999) J. Biol. Chem , vol.274 , pp. 17109-17114
    • Rieke, C.J.1    Mulichak, A.M.2    Garavito, R.M.3    Smith, W.L.4
  • 14
    • 0029911267 scopus 로고    scopus 로고
    • Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2
    • Luong, C., Miller, A., Barnett, J., Chow, J., Ramesha, C., and Browner, M. F. (1996) Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2. Nat. Struct. Biol. 3, 927-933.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 927-933
    • Luong, C.1    Miller, A.2    Barnett, J.3    Chow, J.4    Ramesha, C.5    Browner, M.F.6
  • 15
    • 0034721794 scopus 로고    scopus 로고
    • Oxygenation of the endocannabinoid, 2-arachidonylglycerol, to glyceryl prostaglandins by cyclooxygenase-2
    • Kozak, K. R., Rowlinson, S. W., and Marnett, L. J. (2000) Oxygenation of the endocannabinoid, 2-arachidonylglycerol, to glyceryl prostaglandins by cyclooxygenase-2. J. Biol. Chem. 275, 33744-33749.
    • (2000) J. Biol. Chem , vol.275 , pp. 33744-33749
    • Kozak, K.R.1    Rowlinson, S.W.2    Marnett, L.J.3
  • 17
    • 0030611859 scopus 로고    scopus 로고
    • Synthesis of prostaglandin E2 ethanolamide from anandamide by cyclooxygenase-2
    • Yu, M., Ives, D., and Ramesha, C. S. (1997) Synthesis of prostaglandin E2 ethanolamide from anandamide by cyclooxygenase-2. J. Biol. Chem. 272, 21181-21186.
    • (1997) J. Biol. Chem , vol.272 , pp. 21181-21186
    • Yu, M.1    Ives, D.2    Ramesha, C.S.3
  • 18
    • 24744469860 scopus 로고    scopus 로고
    • Conversion of acetaminophen to the bioactive N-acylphenolamine AM404 via fatty acid amide hydrolase-dependent arachidonic acid conjugation in the nervous system
    • Hogestatt, E. D., Jonsson, B. A., Ermund, A., Andersson, D. A., Bjork, H., Alexander, J. P., Cravatt, B. F., Basbaum, A. I., and Zygmunt, P. M. (2005) Conversion of acetaminophen to the bioactive N-acylphenolamine AM404 via fatty acid amide hydrolase-dependent arachidonic acid conjugation in the nervous system. J. Biol. Chem. 280, 31405-31412.
    • (2005) J. Biol. Chem , vol.280 , pp. 31405-31412
    • Hogestatt, E.D.1    Jonsson, B.A.2    Ermund, A.3    Andersson, D.A.4    Bjork, H.5    Alexander, J.P.6    Cravatt, B.F.7    Basbaum, A.I.8    Zygmunt, P.M.9
  • 20
    • 0037341020 scopus 로고    scopus 로고
    • Compounds acting at the endocannabinoid and/or endovanilloid systems reduce hyperkinesia in a rat model of Huntington's disease
    • Lastres-Becker, I., de Miguel, R., De Petrocellis, L., Makriyannis, A., Di Marzo, V., and Fernandez-Ruiz, J. (2003) Compounds acting at the endocannabinoid and/or endovanilloid systems reduce hyperkinesia in a rat model of Huntington's disease. J. Neurochem. 84, 1097-1109.
    • (2003) J. Neurochem , vol.84 , pp. 1097-1109
    • Lastres-Becker, I.1    de Miguel, R.2    De Petrocellis, L.3    Makriyannis, A.4    Di Marzo, V.5    Fernandez-Ruiz, J.6
  • 21
    • 33749341230 scopus 로고    scopus 로고
    • AM404, an inhibitor of anandamide uptake, prevents pain behaviour and modulates cytokine and apoptotic pathways in a rat model of neuropathic pain
    • Costa, B., Siniscalco, D., Trovato, A. E., Comelli, F., Sotgiu, M. L., Colleoni, M., Maione, S., Rossi, F., and Giagnoni, G. (2006) AM404, an inhibitor of anandamide uptake, prevents pain behaviour and modulates cytokine and apoptotic pathways in a rat model of neuropathic pain. Br. J. Pharmacol. 148, 1022-1032.
    • (2006) Br. J. Pharmacol , vol.148 , pp. 1022-1032
    • Costa, B.1    Siniscalco, D.2    Trovato, A.E.3    Comelli, F.4    Sotgiu, M.L.5    Colleoni, M.6    Maione, S.7    Rossi, F.8    Giagnoni, G.9
  • 22
    • 38649118521 scopus 로고    scopus 로고
    • AM404, an anandamide transport inhibitor, reduces plasma extravasation in a model of neuropathic pain in rat: Role for cannabinoid receptors
    • La Rana, G., Russo, R., D'Agostino, G., Sasso, O., Raso, G. M., Iacono, A., Meli, R., Piomelli, D., and Calignano, A. (2008) AM404, an anandamide transport inhibitor, reduces plasma extravasation in a model of neuropathic pain in rat: Role for cannabinoid receptors. Neuropharmacology 54, 521-529.
    • (2008) Neuropharmacology , vol.54 , pp. 521-529
    • La Rana, G.1    Russo, R.2    D'Agostino, G.3    Sasso, O.4    Raso, G.M.5    Iacono, A.6    Meli, R.7    Piomelli, D.8    Calignano, A.9
  • 24
    • 3343005418 scopus 로고    scopus 로고
    • AM404 enhances the spontaneous release of R-glutamate in a manner sensitive to capsazepine in adult rat substantia gelatinosa neurones
    • Yue, H.-Y., Fujita, T., Kawasaki, Y., and Kumamoto, E. (2004) AM404 enhances the spontaneous release of R-glutamate in a manner sensitive to capsazepine in adult rat substantia gelatinosa neurones. Brain Res. 1018, 283-287.
    • (2004) Brain Res , vol.1018 , pp. 283-287
    • Yue, H.-Y.1    Fujita, T.2    Kawasaki, Y.3    Kumamoto, E.4
  • 25
    • 0021738403 scopus 로고
    • Mechanism of the stimulation of prostaglandin H synthase and prostacyclin synthase by the antithrombotic and antimetastatic agent, nafazatrom
    • Marnett, L. J., Siedlik, P. H., Ochs, R. C., Pagels, W. R., Das, M., Honn, K. V., Warnock, R. H., Tainer, B. E., and Eling, T. E. (1984) Mechanism of the stimulation of prostaglandin H synthase and prostacyclin synthase by the antithrombotic and antimetastatic agent, nafazatrom. Mol. Pharmacol. 26, 328-335.
    • (1984) Mol. Pharmacol , vol.26 , pp. 328-335
    • Marnett, L.J.1    Siedlik, P.H.2    Ochs, R.C.3    Pagels, W.R.4    Das, M.5    Honn, K.V.6    Warnock, R.H.7    Tainer, B.E.8    Eling, T.E.9
  • 26
    • 41149171201 scopus 로고    scopus 로고
    • Oxidative metabolism of a fatty acid amide hydrolase-regulated lipid, arachidonoyltaurine
    • Turman, M. V., Kingsley, P. J., Rouzer, C. A., Cravatt, B. F., and Marnett, L. J. (2008) Oxidative metabolism of a fatty acid amide hydrolase-regulated lipid, arachidonoyltaurine. Biochemistry 47, 3917-3925.
    • (2008) Biochemistry , vol.47 , pp. 3917-3925
    • Turman, M.V.1    Kingsley, P.J.2    Rouzer, C.A.3    Cravatt, B.F.4    Marnett, L.J.5
  • 27
    • 0017231143 scopus 로고
    • A convenient calibration of the Clark oxygen electrode
    • Misra, H. P., and Fridovich, I. (1976) A convenient calibration of the Clark oxygen electrode. Anal. Biochem. 70, 632-634.
    • (1976) Anal. Biochem , vol.70 , pp. 632-634
    • Misra, H.P.1    Fridovich, I.2
  • 29
    • 0023657172 scopus 로고
    • Controlled tryptic digestion of prostaglandin H synthase. Characterization of protein fragments and enhanced rate of proteolysis of oxidatively inactivated enzyme
    • Chen, Y. N., Bienkowski, M. J., and Marnett, L. J. (1987) Controlled tryptic digestion of prostaglandin H synthase. Characterization of protein fragments and enhanced rate of proteolysis of oxidatively inactivated enzyme. J. Biol. Chem. 262, 16892-16899.
    • (1987) J. Biol. Chem , vol.262 , pp. 16892-16899
    • Chen, Y.N.1    Bienkowski, M.J.2    Marnett, L.J.3
  • 31
    • 0018240486 scopus 로고
    • Accelerative autoactivation of prostaglandin biosynthesis by PGG2
    • Hemler, M. E., Graff, G., and Lands, W. E. (1978) Accelerative autoactivation of prostaglandin biosynthesis by PGG2. Biochem. Biophys. Res. Commun. 85, 1325-1331.
    • (1978) Biochem. Biophys. Res. Commun , vol.85 , pp. 1325-1331
    • Hemler, M.E.1    Graff, G.2    Lands, W.E.3
  • 32
    • 0018976320 scopus 로고
    • Evidence for a peroxideinitiated free radical mechanism of prostaglandin biosynthesis
    • Hemler, M. E., and Lands, W. E. (1980) Evidence for a peroxideinitiated free radical mechanism of prostaglandin biosynthesis. J. Biol. Chem. 255, 6253-6261.
    • (1980) J. Biol. Chem , vol.255 , pp. 6253-6261
    • Hemler, M.E.1    Lands, W.E.2
  • 34
    • 0023667648 scopus 로고
    • Attachment of substrate metabolite to prostaglandin H synthase upon reaction with arachidonic acid
    • Kulmacz, R. J. (1987) Attachment of substrate metabolite to prostaglandin H synthase upon reaction with arachidonic acid. Biochem. Biophys. Res. Commun. 148, 539-545.
    • (1987) Biochem. Biophys. Res. Commun , vol.148 , pp. 539-545
    • Kulmacz, R.J.1
  • 35
    • 0017686820 scopus 로고
    • Covalent binding of an intermediate(s) in prostaglandin biosynthesis to guinea pig lung microsomal protein
    • Eling, T. E., Wilson, A. G., Chaudhari, A., and Anderson, M. W. (1977) Covalent binding of an intermediate(s) in prostaglandin biosynthesis to guinea pig lung microsomal protein. Life Sci. 21, 245-251.
    • (1977) Life Sci , vol.21 , pp. 245-251
    • Eling, T.E.1    Wilson, A.G.2    Chaudhari, A.3    Anderson, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.