메뉴 건너뛰기




Volumn 130, Issue 6, 2000, Pages 1353-1361

The MAP kinase inhibitors, PD098059, UO126 and SB203580, inhibit IL-1β-dependent PGE2 release via mechanistically distinct processes

Author keywords

Epithelial cell; MAP kinase; Prostaglandin GH synthase

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; INTERLEUKIN 1BETA; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; PROSTAGLANDIN E2; PROSTAGLANDIN SYNTHASE;

EID: 0033914594     PISSN: 00071188     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.bjp.0703431     Document Type: Article
Times cited : (80)

References (49)
  • 1
    • 0032478741 scopus 로고    scopus 로고
    • Purification and characterization of 1-O-acylceramide synthase, a novel phospholipase A2 with transacylase activity
    • ABE, A. & SHAYMAN, J.A. (1998). Purification and characterization of 1-O-acylceramide synthase, a novel phospholipase A2 with transacylase activity. J. Biol. Chem., 273, 8467-8474.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8467-8474
    • Abe, A.1    Shayman, J.A.2
  • 2
    • 0028884033 scopus 로고
    • PD 098059 is a specific inhibitor of the activation of mitogen-activatcd protein kinase kinase in vitro and in vivo
    • ALESSI, D.R., CUENDA, A., COHEN, P., DUDLEY, D.T. & SALTIEL, A.R. (1995). PD 098059 is a specific inhibitor of the activation of mitogen-activatcd protein kinase kinase in vitro and in vivo. J. Biol. Chem., 270, 27489-27494.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 3
    • 0029862974 scopus 로고    scopus 로고
    • Distinct roles in signal transduction for each of the phospholipase A2 enzymes present in P388D1 macrophages
    • BALSINDE, J. & DENNIS, E.A. (1996). Distinct roles in signal transduction for each of the phospholipase A2 enzymes present in P388D1 macrophages. J. Biol. Chem., 271, 6758-6765.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6758-6765
    • Balsinde, J.1    Dennis, E.A.2
  • 4
    • 0031010112 scopus 로고    scopus 로고
    • Function and inhibition of intracellular calcium-independent phospholipase A2
    • BALSINDE, J. & DENNIS, E.A. (1997). Function and inhibition of intracellular calcium-independent phospholipase A2. J. Biol. Chem., 272, 16069-16072.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16069-16072
    • Balsinde, J.1    Dennis, E.A.2
  • 5
    • 0033604599 scopus 로고    scopus 로고
    • Therapeutic strategies for allergic diseases
    • BARNES, P.J. (1999). Therapeutic strategies for allergic diseases. Nature, 402 (Suppl.): B31-B38.
    • (1999) Nature , vol.402 , Issue.SUPPL.
    • Barnes, P.J.1
  • 6
    • 0032582678 scopus 로고    scopus 로고
    • Direct inhibition of cyclooxygenase-1 and -2 by the kinase inhibitors SB 203580 and PD 98059. SB 203580 also inhibits thromboxane synthase
    • BORSCH-HAUBOLD, A.G., PASQUET, S. & WATSON, S.P. (1998). Direct inhibition of cyclooxygenase-1 and -2 by the kinase inhibitors SB 203580 and PD 98059. SB 203580 also inhibits thromboxane synthase. J. Biol. Chem., 273, 28766-28772.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28766-28772
    • Borsch-Haubold, A.G.1    Pasquet, S.2    Watson, S.P.3
  • 8
    • 0025810578 scopus 로고
    • A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP
    • CLARK, J.D., LIN, L.L., KRIZ, R.W., RAMESHA, C.S., SULTZMAN, L.A., LIN, A.Y., MILONA, N. & KNOPF, J.L. (1991). A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell, 65, 1043-1051.
    • (1991) Cell , vol.65 , pp. 1043-1051
    • Clark, J.D.1    Lin, L.L.2    Kriz, R.W.3    Ramesha, C.S.4    Sultzman, L.A.5    Lin, A.Y.6    Milona, N.7    Knopf, J.L.8
  • 9
    • 0030602877 scopus 로고    scopus 로고
    • Lipocortin 1 and the control of cPLA2 activity in A549 cells. Glucocorticoids block EGF stimulation of cPLA2 phosphorylation
    • CROXTALL, J.D., CHOUDHURY, Q., NEWMAN, S. & FLOWER, R.J. (1996). Lipocortin 1 and the control of cPLA2 activity in A549 cells. Glucocorticoids block EOF stimulation of cPLA2 phosphorylation. Biochem. Pharmacol., 52, 351-356.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 351-356
    • Croxtall, J.D.1    Choudhury, Q.2    Newman, S.3    Flower, R.J.4
  • 10
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • CUENDA, A., ROUSE, J., DOZA, Y.N., MEIER, R., COHEN, P., GALLAGHER, T.F., YOUNG, P.R. & LEE, J.C. (1995). SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett., 364, 229-233.
    • (1995) FEBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 11
    • 0032951716 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase regulates cyclooxygenase-2 mRNA stability and transcription in lipopolysaccharide-treated human monocytes
    • DEAN, J.L., BROOK, M., CLARK, A.R. & SAKLATVALA, J. (1999). p38 mitogen-activated protein kinase regulates cyclooxygenase-2 mRNA stability and transcription in lipopolysaccharide-treated human monocytes. J. Biol. Chem., 274, 264-269.
    • (1999) J. Biol. Chem. , vol.274 , pp. 264-269
    • Dean, J.L.1    Brook, M.2    Clark, A.R.3    Saklatvala, J.4
  • 12
    • 0030614354 scopus 로고    scopus 로고
    • The growing phospholipase A2 superfamily of signal transduction enzymes
    • DENNIS, E.A. (1997). The growing phospholipase A2 superfamily of signal transduction enzymes. Trends. Biochem. Sci., 22, 1-2.
    • (1997) Trends. Biochem. Sci. , vol.22 , pp. 1-2
    • Dennis, E.A.1
  • 13
    • 0032916736 scopus 로고    scopus 로고
    • Cox-2-selectivc inhibitors: The new super aspirins
    • DEWITT, D.L. (1999). Cox-2-selectivc inhibitors: the new super aspirins. Mol. Pharmacol., 55, 625-631.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 625-631
    • DeWitt, D.L.1
  • 17
    • 0029665854 scopus 로고    scopus 로고
    • Cloning and expression of cystolic phospholipase A2 (cPLA2) and a naturally occurring variant. Phosphorylation of Ser505 of recombinant cPLA2 by p42 mitogen-activated protein kinase results in an increase in specific activity
    • GORDON, R.D., LEIGHTON, I.A., CAMPBELL, D.G., COHEN, P., CREANEY, A., WILTON, D.C., MASTERS, D.J., RITCHIE, G.A., MOTT, R., TAYLOR, I.W., BUNDELL, K.R., DOUGLAS, L., MORTEN, J. & NEEDHAM, M. (1996). Cloning and expression of cystolic phospholipase A2 (cPLA2) and a naturally occurring variant. Phosphorylation of Ser505 of recombinant cPLA2 by p42 mitogen-activated protein kinase results in an increase in specific activity. Eur. J. Biochem., 238, 690-697.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 690-697
    • Gordon, R.D.1    Leighton, I.A.2    Campbell, D.G.3    Cohen, P.4    Creaney, A.5    Wilton, D.C.6    Masters, D.J.7    Ritchie, G.A.8    Mott, R.9    Taylor, I.W.10    Bundell, K.R.11    Douglas, L.12    Morten, J.13    Needham, M.14
  • 18
    • 0030951146 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase down-regulates nitric oxide and upregulates prostaglandin E2 biosynthesis stimulated by interleukin-1beta
    • GUAN, Z., BAIER, L.D. & MORRISON, A.R. (1997). p38 mitogen-activated protein kinase down-regulates nitric oxide and upregulates prostaglandin E2 biosynthesis stimulated by interleukin-1beta. J. Biol. Chem., 272, 8083-8089.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8083-8089
    • Guan, Z.1    Baier, L.D.2    Morrison, A.R.3
  • 20
    • 0028824312 scopus 로고
    • Trunscriptional regulation of human prostaglandin-endoperoxide synthasc-2 gene by lipopolysaccharide and phorbol ester in vascular endothelial cells. Involvement of both nuclear factor for interleukin-6 expression site and cAMP response element
    • INOUE, H., YOKOYAMA, C., HARA, S., TONE, Y. & TANABE, T. (1995). Trunscriptional regulation of human prostaglandin-endoperoxide synthasc-2 gene by lipopolysaccharide and phorbol ester in vascular endothelial cells. Involvement of both nuclear factor for interleukin-6 expression site and cAMP response element. J. Biol. Chem., 270, 24965-24971.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24965-24971
    • Inoue, H.1    Yokoyama, C.2    Hara, S.3    Tone, Y.4    Tanabe, T.5
  • 22
    • 0029911368 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase phosphorylates cytosolic phospholipase A2 (cPLA2) in thrombin-stimulated platelets. Evidence that proline-directed phosphorylation is not required for mobilization of arachidonic acid by cPLA2
    • KRAMER, R.M., ROBERTS, E.F., UM, S.L., BORSCH, HAUBOLD, A.G., WATSON, S.P., FISHER, M.J. & JAKUBOWSKI, J.A. (1996). p38 mitogen-activated protein kinase phosphorylates cytosolic phospholipase A2 (cPLA2) in thrombin-stimulated platelets. Evidence that proline-directed phosphorylation is not required for mobilization of arachidonic acid by cPLA2. J. Biol. Chem., 271, 27723-27729.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27723-27729
    • Kramer, R.M.1    Roberts, E.F.2    Um, S.L.3    Borsch4    Haubold, A.G.5    Watson, S.P.6    Fisher, M.J.7    Jakubowski, J.A.8
  • 23
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • KYRIAKIS, J.M. & AVRUCH, J. (1996). Sounding the alarm: protein kinase cascades activated by stress and inflammation. J. Biol. Chem., 271, 24313-24316.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 27
    • 0028787224 scopus 로고
    • Cyclooxygenase-2: Regulation and relevance in inflammation
    • MITCHELL, J.A., LARKIN, S. & WILLIAMS, T.J. (1995). Cyclooxygenase-2: regulation and relevance in inflammation. Biochem. Pharmacol., 50, 1535-1542.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 1535-1542
    • Mitchell, J.A.1    Larkin, S.2    Williams, T.J.3
  • 29
    • 0032486481 scopus 로고    scopus 로고
    • The functions of five distinct mammalian phospholipase A2S in regulating arachidonic acid release. Type IIa and type V secretory phospholipase A2S are functionally redundant and act in concert with cytosolic phospholipase A2
    • MURAKAMI, M., SHIMBARA, S., KAMBE, T., KUWATA, H., WINSTEAD, M.V., TISCHFIELD, J.A. & KUDO, I. (1998). The functions of five distinct mammalian phospholipase A2S in regulating arachidonic acid release. Type IIa and type V secretory phospholipase A2S are functionally redundant and act in concert with cytosolic phospholipase A2. J. Biol. Chem., 273, 14411-14423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14411-14423
    • Murakami, M.1    Shimbara, S.2    Kambe, T.3    Kuwata, H.4    Winstead, M.V.5    Tischfield, J.A.6    Kudo, I.7
  • 30
    • 0027483122 scopus 로고
    • Phospholipase A2 in alveolar type II epithelial cells: Biochemical and immunologic characterization
    • NEAGOS, G.R., FEYSSA, A. & PETERS GOLDEN, M. (1993). Phospholipase A2 in alveolar type II epithelial cells: biochemical and immunologic characterization. Am. J. Physiol., 264, L261-L268.
    • (1993) Am. J. Physiol. , vol.264
    • Neagos, G.R.1    Feyssa, A.2    Peters Golden, M.3
  • 31
    • 0031559584 scopus 로고    scopus 로고
    • Evidence for involvement of NF-kB in the transcriptional control of COX-2 gene expression by TL-1β
    • NEWTON, R., KUITERT, L.M., BERGMANN, M., ADCOCK, I.M. & BARNES, P.J. (1997b). Evidence for involvement of NF-kB in the transcriptional control of COX-2 gene expression by TL-1β. Biochem. Biophys. Res. Commun., 237, 28-32.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 28-32
    • Newton, R.1    Kuitert, L.M.2    Bergmann, M.3    Adcock, I.M.4    Barnes, P.J.5
  • 33
    • 0033610923 scopus 로고    scopus 로고
    • 2 release by dexamethasone occurs by transcriptional and post-transcriptional mechanisms involving loss of polyadenylated mRNA
    • 2 release by dexamethasone occurs by transcriptional and post-transcriptional mechanisms involving loss of polyadenylated mRNA. J. Biol. Chem., 273, 32312-32321.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32312-32321
    • Newton, R.1    Seybold, J.2    Kuitert, L.M.E.3    Bergmann, M.4    Barnes, P.J.5
  • 34
    • 0030815847 scopus 로고    scopus 로고
    • Superinduction of COX-2 mRNA by cycloheximide and interleukin-1β involves increased transcription and correlates with increased NF-kappa B and JNK activation
    • NEWTON, R., STEVENS, D.A., HART, L.A., LINDSAY, M., ADCOCK, I.M. & BARNES, P.J. (1997c). Superinduction of COX-2 mRNA by cycloheximide and interleukin-1β involves increased transcription and correlates with increased NF-kappa B and JNK activation. FEBS Lett., 418, 135-138.
    • (1997) FEBS Lett. , vol.418 , pp. 135-138
    • Newton, R.1    Stevens, D.A.2    Hart, L.A.3    Lindsay, M.4    Adcock, I.M.5    Barnes, P.J.6
  • 35
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • PAWSON, T. & SCOTT, J.D. (1997). Signaling through scaffold, anchoring, and adaptor proteins. Science, 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 37
    • 0033605747 scopus 로고    scopus 로고
    • Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2
    • PICKARD, R.T., STRIFLER, B.A., KRAMER, R.M. & SHARP, J.D. (1999). Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J. Biol. Chem., 274, 8823-8831.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8823-8831
    • Pickard, R.T.1    Strifler, B.A.2    Kramer, R.M.3    Sharp, J.D.4
  • 38
    • 0031570028 scopus 로고    scopus 로고
    • Inhibition of prostaglandin endoperoxide synthase-2 expression in stimulated human monocytes by inhibitors of p38 mitogen-activated protein kinase
    • POULIOT, M., BAILLARGEON, J., LEE, J.C., CLELAND, L.G. & JAMES, M.J. (1997). Inhibition of prostaglandin endoperoxide synthase-2 expression in stimulated human monocytes by inhibitors of p38 mitogen-activated protein kinase. J. Immunol., 158, 4930-4937.
    • (1997) J. Immunol. , vol.158 , pp. 4930-4937
    • Pouliot, M.1    Baillargeon, J.2    Lee, J.C.3    Cleland, L.G.4    James, M.J.5
  • 39
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • RAINGEAUD, J., GUPTA, S., ROGERS, J.S., DICKENS, M., HAN, J., ULEVITCH, R.J. & DAVIS, R.J. (1995). Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem., 270, 7420-7426.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.S.3    Dickens, M.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 40
    • 0028930542 scopus 로고
    • Activation of cytosolic phospholipase A2 by basic fibroblast growth factor via a p42 mitogen-activated protein kinase-dependent phosphorylation pathway in endothelial cells
    • SA, G., MURUGESAN, G., JAYE, M., IVASHCHENKO, Y. & FOX, P.L. (1995). Activation of cytosolic phospholipase A2 by basic fibroblast growth factor via a p42 mitogen-activated protein kinase-dependent phosphorylation pathway in endothelial cells. J. Biol. Chem., 270, 2360-2366.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2360-2366
    • Sa, G.1    Murugesan, G.2    Jaye, M.3    Ivashchenko, Y.4    Fox, P.L.5
  • 43
    • 0029587744 scopus 로고
    • Calcium-mediated translocation of cytosolic phospholipase A2 to the nuclear envelope and endoplasmic reticulum
    • SCHIEVELLA, A.R., REGIER, M.K., SMITH, W.L. & LIN, L.L. (1995). Calcium-mediated translocation of cytosolic phospholipase A2 to the nuclear envelope and endoplasmic reticulum. J. Biol. Chem., 270, 30749-30754.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30749-30754
    • Schievella, A.R.1    Regier, M.K.2    Smith, W.L.3    Lin, L.L.4
  • 45
    • 0028206839 scopus 로고
    • Differential role of extra-and intracellular calcium in bradykinin and interleukin 1 alpha stimulation of arachidonic acid release from A549 cells
    • TOKUMOTO, H., CROXTALL, J.D. & FLOWER, R.J. (1994). Differential role of extra-and intracellular calcium in bradykinin and interleukin 1 alpha stimulation of arachidonic acid release from A549 cells. Biochim. Biophys. Acta, 1211, 301-309.
    • (1994) Biochim. Biophys. Acta , vol.1211 , pp. 301-309
    • Tokumoto, H.1    Croxtall, J.D.2    Flower, R.J.3
  • 47
    • 0033615737 scopus 로고    scopus 로고
    • On the diversity of secreted phospholipases A(2). Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes
    • published erratum appears in J Biol Chem 2000 Jan 21;275(3):2246
    • VALENTIN, E., GHOMASHCHI, F., GELB, M.H., LAZDUNSKI, M. & LAMBEAU, G. (1999). On the diversity of secreted phospholipases A(2). Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes [published erratum appears in J Biol Chem 2000 Jan 21;275(3):2246]. J. Biol. Chem., 274, 31195-31202.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31195-31202
    • Valentin, E.1    Ghomashchi, F.2    Gelb, M.H.3    Lazdunski, M.4    Lambeau, G.5
  • 48
    • 0028785005 scopus 로고
    • v-src induces prostaglandin synthase 2 gene expression by activation of the c-Jun N-terminal kinase and the c-Jun transcription factor
    • XIE, W. & HERSCHMAN, H.R. (1995). v-src induces prostaglandin synthase 2 gene expression by activation of the c-Jun N-terminal kinase and the c-Jun transcription factor. J. Biol. Chem., 270, 27622-27628.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27622-27628
    • Xie, W.1    Herschman, H.R.2
  • 49
    • 0029595394 scopus 로고
    • Transcriptional roles of nuclear factor kappa B and nuclear factor-interleukin-6 in the tumor necrosis factor alpha-dependent induction of cyclooxygenase-2 in MC3T3-E1 cells
    • YAMAMOTO, K., ARAKAWA,T., UEDA, N. & YAMAMOTO, S. (1995). Transcriptional roles of nuclear factor kappa B and nuclear factor-interleukin-6 in the tumor necrosis factor alpha-dependent induction of cyclooxygenase-2 in MC3T3-E1 cells. J. Biol. Chem., 270, 31315-31320.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31315-31320
    • Yamamoto, K.1    Arakawa, T.2    Ueda, N.3    Yamamoto, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.