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Volumn 81, Issue 3-4, 2006, Pages 126-135

Concomitant activation of extracellular signal-regulated kinase and induction of COX-2 stimulates maximum prostaglandin E2 synthesis in human airway epithelial cells

Author keywords

Airway epithelium; Cyclooxygenase 2; Extracellular signal regulated kinase; Inflammation; Phospholipase A2; Prostaglandin E2

Indexed keywords

CALCIMYCIN; CALCIUM ION; CYCLOOXYGENASE 2; INTERLEUKIN 1BETA; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE; PHORBOL 13 ACETATE 12 MYRISTATE; PROSTAGLANDIN E2; PROTEIN KINASE C; TUMOR NECROSIS FACTOR ALPHA;

EID: 33750504998     PISSN: 10988823     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.prostaglandins.2006.08.006     Document Type: Article
Times cited : (13)

References (45)
  • 2
    • 17944404406 scopus 로고    scopus 로고
    • Airway epithelium: more than just a barrier!
    • Folkerts G., and Nijkamp F.P. Airway epithelium: more than just a barrier!. Trends Pharmacol Sci 19 (1998) 334-341
    • (1998) Trends Pharmacol Sci , vol.19 , pp. 334-341
    • Folkerts, G.1    Nijkamp, F.P.2
  • 4
    • 0019913443 scopus 로고
    • The effect and interaction of bradykinin and prostaglandins on protein and collagen production by lung fibroblasts
    • Goldstein R.H., and Polgar P. The effect and interaction of bradykinin and prostaglandins on protein and collagen production by lung fibroblasts. J Biol Chem 257 (1982) 8630-8633
    • (1982) J Biol Chem , vol.257 , pp. 8630-8633
    • Goldstein, R.H.1    Polgar, P.2
  • 5
    • 0031730079 scopus 로고    scopus 로고
    • Expression of cyclo-oxygenase-2 in human airway smooth muscle is associated with profound reductions in cell growth
    • Belvisi M.G., Saunders M., Yacoub M., and Mitchell J.A. Expression of cyclo-oxygenase-2 in human airway smooth muscle is associated with profound reductions in cell growth. Br J Pharmacol 125 (1998) 1102-1108
    • (1998) Br J Pharmacol , vol.125 , pp. 1102-1108
    • Belvisi, M.G.1    Saunders, M.2    Yacoub, M.3    Mitchell, J.A.4
  • 7
    • 0032840848 scopus 로고    scopus 로고
    • PGE2 and dibutyryl cyclic adenosine monophosphate prolong eosinophil survival in vitro
    • Peacock C.D., Misso N.L., Watkins D.N., and Thompson P.J. PGE2 and dibutyryl cyclic adenosine monophosphate prolong eosinophil survival in vitro. J Allergy Clin Immunol 104 (1999) 153-162
    • (1999) J Allergy Clin Immunol , vol.104 , pp. 153-162
    • Peacock, C.D.1    Misso, N.L.2    Watkins, D.N.3    Thompson, P.J.4
  • 8
    • 0141956408 scopus 로고    scopus 로고
    • 2 concentrations and cyclooxygenase-2 expression in asthmatic subjects with sputum eosinophilia
    • 2 concentrations and cyclooxygenase-2 expression in asthmatic subjects with sputum eosinophilia. J Allergy Clin Immunol 112 (2003) 709-716
    • (2003) J Allergy Clin Immunol , vol.112 , pp. 709-716
    • Profita, M.1    Sala, A.2    Bonanno, A.3
  • 10
    • 0032903965 scopus 로고    scopus 로고
    • Protective effects of inhaled PGE2 on allergen-induced airway responses and airway inflammation
    • Gauvreau G.M., Watson R.M., and O'Byrne P.M. Protective effects of inhaled PGE2 on allergen-induced airway responses and airway inflammation. Am J Respir Crit Care Med 159 (1999) 31-36
    • (1999) Am J Respir Crit Care Med , vol.159 , pp. 31-36
    • Gauvreau, G.M.1    Watson, R.M.2    O'Byrne, P.M.3
  • 12
    • 0034943516 scopus 로고    scopus 로고
    • Mixed messages: modulation of inflammation and immune responses by prostaglandins and thromboxanes
    • Tilley S.L., Coffman T.M., and Koller B.H. Mixed messages: modulation of inflammation and immune responses by prostaglandins and thromboxanes. J Clin Invest 108 (2001) 15-23
    • (2001) J Clin Invest , vol.108 , pp. 15-23
    • Tilley, S.L.1    Coffman, T.M.2    Koller, B.H.3
  • 13
    • 0346961783 scopus 로고    scopus 로고
    • The lung as a privileged site for the beneficial actions of PGE2
    • Vancheri C., Mastruzzo C., Sortino M.A., and Crimi N. The lung as a privileged site for the beneficial actions of PGE2. Trends Immunol 25 (2004) 40-46
    • (2004) Trends Immunol , vol.25 , pp. 40-46
    • Vancheri, C.1    Mastruzzo, C.2    Sortino, M.A.3    Crimi, N.4
  • 14
    • 33646575324 scopus 로고    scopus 로고
    • Involvement of cyclooxygenase-2 and prostaglandins in the molecular pathogenesis of inflammatory lung diseases
    • Park G.Y., and Christman J.W. Involvement of cyclooxygenase-2 and prostaglandins in the molecular pathogenesis of inflammatory lung diseases. Am J Physiol Lung Cell Mol Physiol 290 (2006) L797-L805
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.290
    • Park, G.Y.1    Christman, J.W.2
  • 15
    • 0037967579 scopus 로고    scopus 로고
    • 2 release via the expression of cyclooxygenase-2 and microsomal prostaglandin E synthase
    • 2 release via the expression of cyclooxygenase-2 and microsomal prostaglandin E synthase. FEBS Lett 547 (2003) 75-79
    • (2003) FEBS Lett , vol.547 , pp. 75-79
    • Catley, M.C.1    Chivers, J.E.2    Cambridge, L.M.3
  • 16
    • 0037118905 scopus 로고    scopus 로고
    • Lipoteichoic acid-induced cyclooxygenase-2 expression requires activations of p44/42 and p38 mitogen-activated protein kinase signal pathways
    • Lin C.H., Kuan I.H., Wang C.H., et al. Lipoteichoic acid-induced cyclooxygenase-2 expression requires activations of p44/42 and p38 mitogen-activated protein kinase signal pathways. Eur J Pharmacol 450 (2002) 1-9
    • (2002) Eur J Pharmacol , vol.450 , pp. 1-9
    • Lin, C.H.1    Kuan, I.H.2    Wang, C.H.3
  • 17
    • 0034534697 scopus 로고    scopus 로고
    • Induction of prostaglandin endoperoxide synthase 2 by mitogen-activated protein kinase cascades
    • McGinty A., Foschi M., Chang Y.E., Han J., Dunn M.J., and Sorokin A. Induction of prostaglandin endoperoxide synthase 2 by mitogen-activated protein kinase cascades. Biochem J 352 (2000) 419-424
    • (2000) Biochem J , vol.352 , pp. 419-424
    • McGinty, A.1    Foschi, M.2    Chang, Y.E.3    Han, J.4    Dunn, M.J.5    Sorokin, A.6
  • 18
    • 15444339428 scopus 로고    scopus 로고
    • Ceramide regulates the transcription of cyclooxygenase-2. Evidence for involvement of extracellular signal-regulated kinase/c-Jun N-terminal kinase and p38 mitogen-activated protein kinase pathways
    • Subbaramaiah K., Chung W.J., and Dannenberg A.J. Ceramide regulates the transcription of cyclooxygenase-2. Evidence for involvement of extracellular signal-regulated kinase/c-Jun N-terminal kinase and p38 mitogen-activated protein kinase pathways. J Biol Chem 273 (1998) 32943-32949
    • (1998) J Biol Chem , vol.273 , pp. 32943-32949
    • Subbaramaiah, K.1    Chung, W.J.2    Dannenberg, A.J.3
  • 20
  • 22
    • 0035126796 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-induced cyclooxygenase-2 expression via sequential activation of ceramide-dependent mitogen-activated protein kinases, and IκB kinase 1/2 in human alveolar epithelial cells
    • Chen C.C., Sun Y.T., Chen J.J., and Chang Y.J. Tumor necrosis factor-α-induced cyclooxygenase-2 expression via sequential activation of ceramide-dependent mitogen-activated protein kinases, and IκB kinase 1/2 in human alveolar epithelial cells. Mol Pharmacol 59 (2001) 493-500
    • (2001) Mol Pharmacol , vol.59 , pp. 493-500
    • Chen, C.C.1    Sun, Y.T.2    Chen, J.J.3    Chang, Y.J.4
  • 23
    • 0042235524 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinases in influenza virus induction of prostaglandin E2 from arachidonic acid in bronchial epithelial cells
    • Mizumura K., Hashimoto S., Maruoka S., et al. Role of mitogen-activated protein kinases in influenza virus induction of prostaglandin E2 from arachidonic acid in bronchial epithelial cells. Clin Exp Allergy 33 (2003) 1244-1251
    • (2003) Clin Exp Allergy , vol.33 , pp. 1244-1251
    • Mizumura, K.1    Hashimoto, S.2    Maruoka, S.3
  • 25
    • 0022006760 scopus 로고
    • Establishment and identification of small cell lung cancer cell lines having classic and variant features
    • Carney D.N., Gazdar A.F., Bepler G., et al. Establishment and identification of small cell lung cancer cell lines having classic and variant features. Cancer Res 45 (1985) 2913-2923
    • (1985) Cancer Res , vol.45 , pp. 2913-2923
    • Carney, D.N.1    Gazdar, A.F.2    Bepler, G.3
  • 26
    • 0034763207 scopus 로고    scopus 로고
    • Regulation of human lung fibroblast phenotype and behaviour by vitronectin and vitronectin integrins
    • Scaffidi A.K., Moodley Y.P., Weichselbaum M., Thompson P.J., and Knight D.A. Regulation of human lung fibroblast phenotype and behaviour by vitronectin and vitronectin integrins. J Cell Sci 114 (2001) 3507-3516
    • (2001) J Cell Sci , vol.114 , pp. 3507-3516
    • Scaffidi, A.K.1    Moodley, Y.P.2    Weichselbaum, M.3    Thompson, P.J.4    Knight, D.A.5
  • 27
    • 0030751783 scopus 로고    scopus 로고
    • Regulation of the inducible cyclo-oxygenase pathway in human cultured airway epithelial (A549) cells by nitric oxide
    • Watkins D.N., Garlepp M.J., and Thompson P.J. Regulation of the inducible cyclo-oxygenase pathway in human cultured airway epithelial (A549) cells by nitric oxide. Br J Pharmacol 121 (1997) 1482-1488
    • (1997) Br J Pharmacol , vol.121 , pp. 1482-1488
    • Watkins, D.N.1    Garlepp, M.J.2    Thompson, P.J.3
  • 30
    • 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
    • Börsch-Haubold A.G., Pasquet S., and Watson S.P. 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 (1998) 28766-28772
    • (1998) J Biol Chem , vol.273 , pp. 28766-28772
    • Börsch-Haubold, A.G.1    Pasquet, S.2    Watson, S.P.3
  • 31
    • 0034283944 scopus 로고    scopus 로고
    • TNF-α-induced cyclooxygenase-2 expression in human lung epithelial cells: involvement of the phosholipase C-γ2, protein kinase C-α, tyrosine kinase, NF-κB-inducing kinase, and I-κB kinase 1/2 pathway
    • Chen C.C., Sun Y.T., Chen J.J., and Chiu K.T. TNF-α-induced cyclooxygenase-2 expression in human lung epithelial cells: involvement of the phosholipase C-γ2, protein kinase C-α, tyrosine kinase, NF-κB-inducing kinase, and I-κB kinase 1/2 pathway. J Immunol 165 (2000) 2719-2728
    • (2000) J Immunol , vol.165 , pp. 2719-2728
    • Chen, C.C.1    Sun, Y.T.2    Chen, J.J.3    Chiu, K.T.4
  • 32
    • 0033986555 scopus 로고    scopus 로고
    • Involvement of protein kinase C-γ in IL-1β-induced cyclooxygenase-2 expression in human pulmonary epithelial cells
    • Lin C.H., Sheu S.Y., Lee H.M., et al. Involvement of protein kinase C-γ in IL-1β-induced cyclooxygenase-2 expression in human pulmonary epithelial cells. Mol Pharmacol 57 (2000) 36-43
    • (2000) Mol Pharmacol , vol.57 , pp. 36-43
    • Lin, C.H.1    Sheu, S.Y.2    Lee, H.M.3
  • 33
    • 0035865073 scopus 로고    scopus 로고
    • Respiratory syncytial virus infection results in activation of multiple protein kinase C isoforms leading to activation of mitogen-activated protein kinase
    • Monick M., Staber J., Thomas K., and Hunninghake G. Respiratory syncytial virus infection results in activation of multiple protein kinase C isoforms leading to activation of mitogen-activated protein kinase. J Immunol 166 (2001) 2681-2687
    • (2001) J Immunol , vol.166 , pp. 2681-2687
    • Monick, M.1    Staber, J.2    Thomas, K.3    Hunninghake, G.4
  • 34
    • 0036081107 scopus 로고    scopus 로고
    • Dopamine activates ERKs in alveolar epithelial cells via Ras-PKC-dependent and Grb2/Sos-independent mechanisms
    • Guerrero C., Peske L., Lecuona E., Ridge K.M., and Sznajder J.I. Dopamine activates ERKs in alveolar epithelial cells via Ras-PKC-dependent and Grb2/Sos-independent mechanisms. Am J Physiol Lung Cell Mol Physiol 282 (2002) L1099-L1107
    • (2002) Am J Physiol Lung Cell Mol Physiol , vol.282
    • Guerrero, C.1    Peske, L.2    Lecuona, E.3    Ridge, K.M.4    Sznajder, J.I.5
  • 35
    • 0026453081 scopus 로고
    • Activation of the c-Raf protein kinase by protein kinase C phosphorylation
    • Sozeri O., Vollmer K., Liyanage M., et al. Activation of the c-Raf protein kinase by protein kinase C phosphorylation. Oncogene 7 (1992) 2259-2262
    • (1992) Oncogene , vol.7 , pp. 2259-2262
    • Sozeri, O.1    Vollmer, K.2    Liyanage, M.3
  • 36
    • 0029789967 scopus 로고    scopus 로고
    • Protein kinase C activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf
    • Ueda Y., Hirai S., Osada S., Suzuki A., Mizuno K., and Ohno S. Protein kinase C activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf. J Biol Chem 271 (1996) 23512-23519
    • (1996) J Biol Chem , vol.271 , pp. 23512-23519
    • Ueda, Y.1    Hirai, S.2    Osada, S.3    Suzuki, A.4    Mizuno, K.5    Ohno, S.6
  • 37
    • 0025851176 scopus 로고
    • 2+ ionophore A23187 in cultured Madin-Darby canine kidney cells
    • 2+ ionophore A23187 in cultured Madin-Darby canine kidney cells. Arch Biochem Biophys 288 (1991) 192-201
    • (1991) Arch Biochem Biophys , vol.288 , pp. 192-201
    • Yokota, K.1
  • 38
    • 0032608413 scopus 로고    scopus 로고
    • Endothelin-stimulated ERK activation in airway smooth-muscle cells requires calcium influx and Raf activation
    • Vichi P., Whelchel A., Knot H., Nelson M., Kolch W., and Posada J. Endothelin-stimulated ERK activation in airway smooth-muscle cells requires calcium influx and Raf activation. Am J Respir Cell Mol Biol 20 (1999) 99-105
    • (1999) Am J Respir Cell Mol Biol , vol.20 , pp. 99-105
    • Vichi, P.1    Whelchel, A.2    Knot, H.3    Nelson, M.4    Kolch, W.5    Posada, J.6
  • 39
    • 0029912853 scopus 로고    scopus 로고
    • 2 in norepinephrine-induced arachidonic acid release in rabbit aortic smooth muscle cells
    • 2 in norepinephrine-induced arachidonic acid release in rabbit aortic smooth muscle cells. J Biol Chem 271 (1996) 30149-30157
    • (1996) J Biol Chem , vol.271 , pp. 30149-30157
    • Muthalif, M.M.1    Benter, I.F.2    Uddin, M.R.3    Malik, K.U.4
  • 41
    • 0032787558 scopus 로고    scopus 로고
    • HGF triggers activation of the COX-2 gene in rat gastric epithelial cells: action mediated through the ERK2 signaling pathway
    • Jones M.K., Sasaki E., Halter F., et al. HGF triggers activation of the COX-2 gene in rat gastric epithelial cells: action mediated through the ERK2 signaling pathway. FASEB J 13 (1999) 2186-2194
    • (1999) FASEB J , vol.13 , pp. 2186-2194
    • Jones, M.K.1    Sasaki, E.2    Halter, F.3
  • 43
    • 33744812706 scopus 로고    scopus 로고
    • Streptococcus pneumoniae-induced p38 MAPK- and NF-κB-dependent COX-2 expression in human lung epithelium
    • Dje N'Guessan P., Hippenstiel S., Etouem M.O., et al. Streptococcus pneumoniae-induced p38 MAPK- and NF-κB-dependent COX-2 expression in human lung epithelium. Am J Physiol Lung Cell Mol Physiol 290 (2006) L1131-L1138
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.290
    • Dje N'Guessan, P.1    Hippenstiel, S.2    Etouem, M.O.3
  • 44
    • 0347379917 scopus 로고    scopus 로고
    • Cyclooxygenase-2 induction by bradykinin in human pulmonary artery smooth muscle cells is mediated by the cyclic AMP response element through a novel autocrine loop involving endogenous prostaglandin E2, E-prostanoid 2 (EP2), and EP4 receptors
    • Bradbury D.A., Newton R., Zhu Y.M., El-Haroun H., Corbett L., and Knox A.J. Cyclooxygenase-2 induction by bradykinin in human pulmonary artery smooth muscle cells is mediated by the cyclic AMP response element through a novel autocrine loop involving endogenous prostaglandin E2, E-prostanoid 2 (EP2), and EP4 receptors. J Biol Chem 278 (2003) 49954-49964
    • (2003) J Biol Chem , vol.278 , pp. 49954-49964
    • Bradbury, D.A.1    Newton, R.2    Zhu, Y.M.3    El-Haroun, H.4    Corbett, L.5    Knox, A.J.6
  • 45
    • 22344439814 scopus 로고    scopus 로고
    • Differential regulation of phosphorylation of the cAMP response element-binding protein after activation of EP2 and EP4 prostanoid receptors by prostaglandin E2
    • Fujino H., Salvi S., and Regan J.W. Differential regulation of phosphorylation of the cAMP response element-binding protein after activation of EP2 and EP4 prostanoid receptors by prostaglandin E2. Mol Pharmacol 68 (2005) 251-259
    • (2005) Mol Pharmacol , vol.68 , pp. 251-259
    • Fujino, H.1    Salvi, S.2    Regan, J.W.3


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