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Volumn 39, Issue 12, 2009, Pages 851-860

Direct evidence of the cyclooxygenase pathway of prostaglandin synthesis in arthropods: Genetic and biochemical characterization of two crustacean cyclooxygenases

Author keywords

Arthropod; Crustacean; Cyclooxygenase; Gene; Insect; Non mammalian oxylipins; Prostaglandin; Prostaglandin H synthase

Indexed keywords

PROSTAGLANDIN; PROSTAGLANDIN SYNTHASE;

EID: 73449096708     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2009.10.002     Document Type: Article
Times cited : (49)

References (47)
  • 2
    • 0035933736 scopus 로고    scopus 로고
    • The 3′-untranslated region of murine cyclooxygenase-2 contains multiple regulatory elements that alter message stability and translational efficiency
    • Cok S.J., and Morrison A.R. The 3′-untranslated region of murine cyclooxygenase-2 contains multiple regulatory elements that alter message stability and translational efficiency. J. Biol. Chem. 276 (2001) 23179-23185
    • (2001) J. Biol. Chem. , vol.276 , pp. 23179-23185
    • Cok, S.J.1    Morrison, A.R.2
  • 3
    • 0034697027 scopus 로고    scopus 로고
    • Post-transcriptional control of cyclooxygenase-2 gene expression. The role of the 3′-untranslated region
    • Dixon D.A., Kaplan C.D., McIntyre T.M., Zimmerman G.A., and Prescott S.M. Post-transcriptional control of cyclooxygenase-2 gene expression. The role of the 3′-untranslated region. J. Biol. Chem. 275 (2000) 11750-11757
    • (2000) J. Biol. Chem. , vol.275 , pp. 11750-11757
    • Dixon, D.A.1    Kaplan, C.D.2    McIntyre, T.M.3    Zimmerman, G.A.4    Prescott, S.M.5
  • 5
    • 12344319508 scopus 로고    scopus 로고
    • The role of the AU-rich elements of mRNAs in controlling translation
    • Espel E. The role of the AU-rich elements of mRNAs in controlling translation. Semin. Cell Dev. Biol. 16 (2005) 59-67
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 59-67
    • Espel, E.1
  • 6
    • 0001382636 scopus 로고    scopus 로고
    • Eicosanoids in nonmammals
    • Sankawa V. (Ed), Elsevier Science Publishers Ltd., Oxford
    • Gerwick W.H. Eicosanoids in nonmammals. In: Sankawa V. (Ed). Comprehensive Natural Products Chemistry Vol. 1 (1999), Elsevier Science Publishers Ltd., Oxford 207-254
    • (1999) Comprehensive Natural Products Chemistry , vol.1 , pp. 207-254
    • Gerwick, W.H.1
  • 9
    • 0034671987 scopus 로고    scopus 로고
    • Distinct influences of carboxyl terminal segment structure on function in the two isoforms of prostaglandin H synthase
    • Guo Q., and Kulmacz R.J. Distinct influences of carboxyl terminal segment structure on function in the two isoforms of prostaglandin H synthase. Arch. Biochem. Biophys. 384 (2000) 269-279
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 269-279
    • Guo, Q.1    Kulmacz, R.J.2
  • 10
    • 0026553243 scopus 로고
    • Biosynthesis of eicosanoids by blood cells of the crab Carcinus maenas
    • Hampson A.J., Rowley A.F., Barrow S.E., and Steadman R. Biosynthesis of eicosanoids by blood cells of the crab Carcinus maenas. Biochim. Biophys. Acta 1124 (1992) 143-150
    • (1992) Biochim. Biophys. Acta , vol.1124 , pp. 143-150
    • Hampson, A.J.1    Rowley, A.F.2    Barrow, S.E.3    Steadman, R.4
  • 11
    • 54149112779 scopus 로고    scopus 로고
    • Gene duplications and losses within the cyclooxygenase family of teleosts and other chordates
    • Havird J.C., Miyamoto M.M., Choe K.P., and Evans D.H. Gene duplications and losses within the cyclooxygenase family of teleosts and other chordates. Mol. Biol. Evol. 25 (2008) 2349-2359
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 2349-2359
    • Havird, J.C.1    Miyamoto, M.M.2    Choe, K.P.3    Evans, D.H.4
  • 14
    • 36849023824 scopus 로고    scopus 로고
    • Two inducible, functional cyclooxygenase-2 genes are present in the rainbow trout genome
    • Ishikawa T.O., and Herschman H.R. Two inducible, functional cyclooxygenase-2 genes are present in the rainbow trout genome. J. Cell Biochem. 102 (2007) 1486-1492
    • (2007) J. Cell Biochem. , vol.102 , pp. 1486-1492
    • Ishikawa, T.O.1    Herschman, H.R.2
  • 15
    • 1842690846 scopus 로고    scopus 로고
    • On the evolutionary origin of cyclooxygenase (COX) isozymes: characterization of marine invertebrate COX genes points to independent duplication events in vertebrate and invertebrate lineages
    • Järving R., Järving I., Kurg R., Brash A.R., and Samel N. On the evolutionary origin of cyclooxygenase (COX) isozymes: characterization of marine invertebrate COX genes points to independent duplication events in vertebrate and invertebrate lineages. J. Biol. Chem. 279 (2004) 13624-13633
    • (2004) J. Biol. Chem. , vol.279 , pp. 13624-13633
    • Järving, R.1    Järving, I.2    Kurg, R.3    Brash, A.R.4    Samel, N.5
  • 16
    • 0034054950 scopus 로고    scopus 로고
    • Monitoring and purification of proteins using bovine papillomavirus E2 epitope tags
    • Kaldalu N., Lepik D., Kristjuhan A., and Ustav M. Monitoring and purification of proteins using bovine papillomavirus E2 epitope tags. BioTechniques 28 (2000) 456-462
    • (2000) BioTechniques , vol.28 , pp. 456-462
    • Kaldalu, N.1    Lepik, D.2    Kristjuhan, A.3    Ustav, M.4
  • 17
    • 0035831484 scopus 로고    scopus 로고
    • The basis of prostaglandin synthesis in coral: molecular cloning and expression of a cyclooxygenase from the Arctic soft coral Gersemia fruticosa
    • Koljak R., Järving I., Kurg R., Boeglin W.E., Varvas K., Valmsen K., Ustav M., Brash A.R., and Samel N. The basis of prostaglandin synthesis in coral: molecular cloning and expression of a cyclooxygenase from the Arctic soft coral Gersemia fruticosa. J. Biol. Chem. 276 (2001) 7033-7040
    • (2001) J. Biol. Chem. , vol.276 , pp. 7033-7040
    • Koljak, R.1    Järving, I.2    Kurg, R.3    Boeglin, W.E.4    Varvas, K.5    Valmsen, K.6    Ustav, M.7    Brash, A.R.8    Samel, N.9
  • 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
    • 0032491396 scopus 로고    scopus 로고
    • The membrane association sequences of the prostaglandin endoperoxide synthases-1 and -2 isozymes
    • Li Y., Smith T., Grabski S., and DeWitt D.L. The membrane association sequences of the prostaglandin endoperoxide synthases-1 and -2 isozymes. J. Biol. Chem. 273 (1998) 29830-29837
    • (1998) J. Biol. Chem. , vol.273 , pp. 29830-29837
    • Li, Y.1    Smith, T.2    Grabski, S.3    DeWitt, D.L.4
  • 22
    • 0035852985 scopus 로고    scopus 로고
    • Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry
    • Nemeth J.F., Hochensang G.P., Marnett L.J., and Caprioli R.M. Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry. Biochemistry 40 (2001) 3109-3116
    • (2001) Biochemistry , vol.40 , pp. 3109-3116
    • Nemeth, J.F.1    Hochensang, G.P.2    Marnett, L.J.3    Caprioli, R.M.4
  • 23
    • 0027327231 scopus 로고
    • N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum
    • Otto J.C., DeWitt D.L., and Smith W.L. N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum. J. Biol. Chem. 268 (1993) 18234-18242
    • (1993) J. Biol. Chem. , vol.268 , pp. 18234-18242
    • Otto, J.C.1    DeWitt, D.L.2    Smith, W.L.3
  • 24
    • 27644459878 scopus 로고    scopus 로고
    • Changes in membrane lipid composition following rapid cold hardening in Drosophila melanogaster
    • Overgaard J., Sorensen J.G., Petersen S.O., Loeschcke V., and Holmstrup M. Changes in membrane lipid composition following rapid cold hardening in Drosophila melanogaster. J. Insect Physiol. 51 (2005) 1173-1182
    • (2005) J. Insect Physiol. , vol.51 , pp. 1173-1182
    • Overgaard, J.1    Sorensen, J.G.2    Petersen, S.O.3    Loeschcke, V.4    Holmstrup, M.5
  • 25
    • 0022827572 scopus 로고
    • Cyclooxygenase and lipoxygenase-like activity in Drosophila melanogaster
    • Pages M., Rosello J., Casas J., Gelpi E., Gualde N., and Rigaud M. Cyclooxygenase and lipoxygenase-like activity in Drosophila melanogaster. Prostaglandins 32 (1986) 729-740
    • (1986) Prostaglandins , vol.32 , pp. 729-740
    • Pages, M.1    Rosello, J.2    Casas, J.3    Gelpi, E.4    Gualde, N.5    Rigaud, M.6
  • 26
    • 0345687864 scopus 로고    scopus 로고
    • The synthesis and effects of prostaglandins on the ovary of the crab Oziotelphusa senex senex
    • Reddy P.S., Reddy P.R., and Nagaraju G.P. The synthesis and effects of prostaglandins on the ovary of the crab Oziotelphusa senex senex. Gen. Comp. Endocrinol. 135 (2004) 35-41
    • (2004) Gen. Comp. Endocrinol. , vol.135 , pp. 35-41
    • Reddy, P.S.1    Reddy, P.R.2    Nagaraju, G.P.3
  • 27
    • 0028961611 scopus 로고
    • Prostaglandin H synthase-1: evaluation of C-terminus function
    • Ren Y., Loose-Mitchell D.S., and Kulmacz R.J. Prostaglandin H synthase-1: evaluation of C-terminus function. Arch. Biochem. Biophys. 316 (1995) 751-757
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 751-757
    • Ren, Y.1    Loose-Mitchell, D.S.2    Kulmacz, R.J.3
  • 28
    • 0037898985 scopus 로고    scopus 로고
    • Mechanism of free radical oxygenation of polyunsaturated fatty acids by cyclooxygenases
    • Rouzer C.A., and Marnett L.J. Mechanism of free radical oxygenation of polyunsaturated fatty acids by cyclooxygenases. Chem. Rev. 103 (2003) 2239-2304
    • (2003) Chem. Rev. , vol.103 , pp. 2239-2304
    • Rouzer, C.A.1    Marnett, L.J.2
  • 29
    • 13644264121 scopus 로고    scopus 로고
    • Prostaglandins in non-insectan invertebrates: recent insights and unsolved problems
    • Rowley A.F., Vogan C.L., Taylor G.W., and Clare A.S. Prostaglandins in non-insectan invertebrates: recent insights and unsolved problems. J. Exp. Biol. 208 (2005) 3-14
    • (2005) J. Exp. Biol. , vol.208 , pp. 3-14
    • Rowley, A.F.1    Vogan, C.L.2    Taylor, G.W.3    Clare, A.S.4
  • 30
    • 0029415139 scopus 로고
    • Prostaglandin E2 in previtellogenic ovaries of the prawn Macrobrachium rosenbergii: synthesis and effect on the level of cAMP
    • Sagi A., Silkovsky J., Fleisher-Berkovich S., Danon A., and Chayoth R. Prostaglandin E2 in previtellogenic ovaries of the prawn Macrobrachium rosenbergii: synthesis and effect on the level of cAMP. Gen. Comp. Endocrinol. 100 (1995) 308-313
    • (1995) Gen. Comp. Endocrinol. , vol.100 , pp. 308-313
    • Sagi, A.1    Silkovsky, J.2    Fleisher-Berkovich, S.3    Danon, A.4    Chayoth, R.5
  • 31
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw G., and Kamen R. A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46 (1986) 659-667
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 32
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: structural, cellular, and molecular biology
    • Smith L., DeWitt D.L., and Garavito R.M. Cyclooxygenases: structural, cellular, and molecular biology. Annu. Rev. Biochem. 69 (2000) 145-182
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 145-182
    • Smith, L.1    DeWitt, D.L.2    Garavito, R.M.3
  • 33
    • 0027323306 scopus 로고
    • Molecular cloning of an allene oxide synthase: a cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides
    • Song W.-C., Funk C.D., and Brash A.R. Molecular cloning of an allene oxide synthase: a cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides. Proc. Natl. Acad. Sci. USA 90 (1993) 8519-8523
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8519-8523
    • Song, W.-C.1    Funk, C.D.2    Brash, A.R.3
  • 34
    • 0032540344 scopus 로고    scopus 로고
    • Subcellular localization of prostaglandin endoperoxide H synthases-1 and -2 by immunoelectron microscopy
    • Spencer A., Woods J.W., Arakawa T., Singer I.I., and Smith W.L. Subcellular localization of prostaglandin endoperoxide H synthases-1 and -2 by immunoelectron microscopy. J. Biol. Chem. 273 (1998) 9886-9893
    • (1998) J. Biol. Chem. , vol.273 , pp. 9886-9893
    • Spencer, A.1    Woods, J.W.2    Arakawa, T.3    Singer, I.I.4    Smith, W.L.5
  • 36
    • 30844448127 scopus 로고    scopus 로고
    • Prostaglandins and other eicosanoids in insects: biological significance
    • Stanley D.W. Prostaglandins and other eicosanoids in insects: biological significance. Annu. Rev. Entomol. 51 (2006) 25-44
    • (2006) Annu. Rev. Entomol. , vol.51 , pp. 25-44
    • Stanley, D.W.1
  • 37
    • 33645098178 scopus 로고    scopus 로고
    • Eicosanoid actions in insect cellular immune functions
    • Stanley D.W., and Miller J.S. Eicosanoid actions in insect cellular immune functions. Entomol. Exp. Appl. 119 (2006) 1-13
    • (2006) Entomol. Exp. Appl. , vol.119 , pp. 1-13
    • Stanley, D.W.1    Miller, J.S.2
  • 38
    • 0037228856 scopus 로고    scopus 로고
    • Comparison of fatty acid composition in major lipid classes of the dominant benthic invertebrates of the Yenisei river
    • Sushchik N.N., Gladyshev M.I., Moskvichova A.V., Makhutova O.N., and Kalachova G.S. Comparison of fatty acid composition in major lipid classes of the dominant benthic invertebrates of the Yenisei river. Comp. Biochem. Physiol. B 134 (2003) 111-122
    • (2003) Comp. Biochem. Physiol. B , vol.134 , pp. 111-122
    • Sushchik, N.N.1    Gladyshev, M.I.2    Moskvichova, A.V.3    Makhutova, O.N.4    Kalachova, G.S.5
  • 39
    • 16544389000 scopus 로고    scopus 로고
    • Maturation-related variations in prostaglandin and fatty acid content of ovary in the kuruma prawn (Marsupenaeus japonicus)
    • Tahara D., and Yano I. Maturation-related variations in prostaglandin and fatty acid content of ovary in the kuruma prawn (Marsupenaeus japonicus). Comp. Biochem. Physiol. A 137 (2004) 631-637
    • (2004) Comp. Biochem. Physiol. A , vol.137 , pp. 631-637
    • Tahara, D.1    Yano, I.2
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 42149157795 scopus 로고    scopus 로고
    • Drosophila Pxt: a cyclooxygenase-like facilitator of follicle maturation
    • Tootle T.L., and Spradling A.C. Drosophila Pxt: a cyclooxygenase-like facilitator of follicle maturation. Development 135 (2008) 839-847
    • (2008) Development , vol.135 , pp. 839-847
    • Tootle, T.L.1    Spradling, A.C.2
  • 42
    • 0034940463 scopus 로고    scopus 로고
    • The origin of 15R-prostaglandins in the Caribbean coral Plexaura homomalla: molecular cloning and expression of a novel cyclooxygenase
    • Valmsen K., Järving I., Boeglin W.E., Varvas K., Koljak R., Pehk T., Brash A.R., and Samel N. The origin of 15R-prostaglandins in the Caribbean coral Plexaura homomalla: molecular cloning and expression of a novel cyclooxygenase. Proc. Natl. Acad. Sci. USA 98 (2001) 7700-7705
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7700-7705
    • Valmsen, K.1    Järving, I.2    Boeglin, W.E.3    Varvas, K.4    Koljak, R.5    Pehk, T.6    Brash, A.R.7    Samel, N.8
  • 43
    • 4544365241 scopus 로고    scopus 로고
    • Structural and functional comparison of 15 S- and 15 R-specific cyclooxygenases from the coral Plexaura homomalla
    • Valmsen K., Boeglin W.E., Järving I., Schneider C., Varvas K., Brash A.R., and Samel N. Structural and functional comparison of 15 S- and 15 R-specific cyclooxygenases from the coral Plexaura homomalla. Eur. J. Biochem. 271 (2004) 3533-3538
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3533-3538
    • Valmsen, K.1    Boeglin, W.E.2    Järving, I.3    Schneider, C.4    Varvas, K.5    Brash, A.R.6    Samel, N.7
  • 44
    • 34948840083 scopus 로고    scopus 로고
    • A critical role of non-active site residues on cyclooxygenase helices 5 and 6 in the control of prostaglandin stereochemistry at carbon 15
    • Valmsen K., Boeglin W.E., Järving R., Järving I., Varvas K., Brash A.R., and Samel N. A critical role of non-active site residues on cyclooxygenase helices 5 and 6 in the control of prostaglandin stereochemistry at carbon 15. J. Biol. Chem. 282 (2007) 28157-28163
    • (2007) J. Biol. Chem. , vol.282 , pp. 28157-28163
    • Valmsen, K.1    Boeglin, W.E.2    Järving, R.3    Järving, I.4    Varvas, K.5    Brash, A.R.6    Samel, N.7
  • 45
    • 0027939491 scopus 로고
    • Endoperoxide pathway in prostaglandin biosynthesis in the soft coral Gersemia fruticosa
    • Varvas K., Koljak R., Järving I., Pehk T., and Samel N. Endoperoxide pathway in prostaglandin biosynthesis in the soft coral Gersemia fruticosa. Tetrahedron Lett. 35 (1994) 8267-8270
    • (1994) Tetrahedron Lett. , vol.35 , pp. 8267-8270
    • Varvas, K.1    Koljak, R.2    Järving, I.3    Pehk, T.4    Samel, N.5
  • 46
    • 0039180005 scopus 로고    scopus 로고
    • Evidence of a cyclooxygenase-related prostaglandin synthesis in coral. The allene oxide pathway is not involved in prostaglandin biosynthesis
    • Varvas K., Järving I., Koljak R., Valmsen K., Brash A.R., and Samel N. Evidence of a cyclooxygenase-related prostaglandin synthesis in coral. The allene oxide pathway is not involved in prostaglandin biosynthesis. J. Biol. Chem. 274 (1999) 9923-9929
    • (1999) J. Biol. Chem. , vol.274 , pp. 9923-9929
    • Varvas, K.1    Järving, I.2    Koljak, R.3    Valmsen, K.4    Brash, A.R.5    Samel, N.6
  • 47
    • 46449130668 scopus 로고    scopus 로고
    • The peroxidase-cyclooxygenase superfamily: reconstructed evolution of critical enzymes of the innate immune system
    • Zamocky M., Jakopitsch C., Furtmüller P.G., Dunand C., and Obinger C. The peroxidase-cyclooxygenase superfamily: reconstructed evolution of critical enzymes of the innate immune system. Proteins 72 (2008) 589-605
    • (2008) Proteins , vol.72 , pp. 589-605
    • Zamocky, M.1    Jakopitsch, C.2    Furtmüller, P.G.3    Dunand, C.4    Obinger, C.5


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