메뉴 건너뛰기




Volumn 143, Issue 2, 2014, Pages 287-299

Calcium/calmodulin-dependent protein kinase II regulates cyclooxygenase-2 expression and prostaglandin E2 production by activating cAMP-response element-binding protein in rat peritoneal macrophages

Author keywords

Calcium; Calmodulin; Calmodulin dependent kinase; CAMP response element binding protein; Cyclooxygenase 2; Prostaglandin E2

Indexed keywords

CALCIUM; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALMODULIN; CHELATING AGENT; CREBBP PROTEIN, RAT; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; CYCLOOXYGENASE 2; ENZYME ACTIVATOR; PROSTAGLANDIN E2; PROTEIN KINASE INHIBITOR; PTGS2 PROTEIN, RAT;

EID: 84908165185     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/imm.12309     Document Type: Article
Times cited : (23)

References (49)
  • 1
    • 33646451673 scopus 로고    scopus 로고
    • Preventive effect of Ginkgo biloba extract (GBB) on the lipopolysaccharide-induced expressions of inducible nitric oxide synthase and cyclooxygenase-2 via suppression of nuclear factor-κB in RAW 264.7 cells
    • Park YM, Won JH, Yun KJ, Ryu JH, Han YN, Choi SK, Lee KT. Preventive effect of Ginkgo biloba extract (GBB) on the lipopolysaccharide-induced expressions of inducible nitric oxide synthase and cyclooxygenase-2 via suppression of nuclear factor-κB in RAW 264.7 cells. Biol Pharm Bull 2006; 29:985-90.
    • (2006) Biol Pharm Bull , vol.29 , pp. 985-990
    • Park, Y.M.1    Won, J.H.2    Yun, K.J.3    Ryu, J.H.4    Han, Y.N.5    Choi, S.K.6    Lee, K.T.7
  • 3
    • 0036514213 scopus 로고    scopus 로고
    • The macrophage response to endotoxin requires platelet activating factor
    • Bulger EM, Arbabi S, Garcia I, Maier RV. The macrophage response to endotoxin requires platelet activating factor. Shock 2002; 17:173-9.
    • (2002) Shock , vol.17 , pp. 173-179
    • Bulger, E.M.1    Arbabi, S.2    Garcia, I.3    Maier, R.V.4
  • 4
    • 0027920980 scopus 로고
    • Pathogenic mechanisms of septic shock
    • Parillo JE. Pathogenic mechanisms of septic shock. N Engl J Med 1993; 328:1471-7.
    • (1993) N Engl J Med , vol.328 , pp. 1471-1477
    • Parillo, J.E.1
  • 5
    • 0030369193 scopus 로고    scopus 로고
    • Monocyte response to bacterial toxins, expression of cell surface receptors, and release of anti-inflammatory cytokines during sepsis
    • Astiz M, Saha D, Lustbader D, Lin R, Rackow E. Monocyte response to bacterial toxins, expression of cell surface receptors, and release of anti-inflammatory cytokines during sepsis. J Lab Clin Med 1996; 128:594-600.
    • (1996) J Lab Clin Med , vol.128 , pp. 594-600
    • Astiz, M.1    Saha, D.2    Lustbader, D.3    Lin, R.4    Rackow, E.5
  • 7
    • 3042665905 scopus 로고    scopus 로고
    • Cyclooxygenase as a target in lung cancer
    • Brown JR, DuBois RN. Cyclooxygenase as a target in lung cancer. Clin Cancer Res 2004; 10:4266s-9s.
    • (2004) Clin Cancer Res , vol.10 , pp. 4266s-4269s
    • Brown, J.R.1    DuBois, R.N.2
  • 9
    • 0028899434 scopus 로고
    • Proinflammatory cytokines regulate cyclooxygenase-2 mRNA expression in human macrophages
    • Arias-Negrete S, Keller K, Chadee K. Proinflammatory cytokines regulate cyclooxygenase-2 mRNA expression in human macrophages. Biochem Biophys Res Commun 1995; 208:582-9.
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 582-589
    • Arias-Negrete, S.1    Keller, K.2    Chadee, K.3
  • 12
    • 0038399752 scopus 로고    scopus 로고
    • 2 isoforms: a perspective
    • 2 isoforms: a perspective. Cell Signal 2003; 15:637-65.
    • (2003) Cell Signal , vol.15 , pp. 637-665
    • Chakraborti, S.1
  • 13
    • 21344450641 scopus 로고    scopus 로고
    • Non-prostaglandin eicosanoids in fever and anapyrexia
    • Kozak W, Fraifeld V. Non-prostaglandin eicosanoids in fever and anapyrexia. Front Biosci 2004; 9:3339-55.
    • (2004) Front Biosci , vol.9 , pp. 3339-3355
    • Kozak, W.1    Fraifeld, V.2
  • 14
    • 27544456457 scopus 로고    scopus 로고
    • Structural and functional difference between cyclooxygenases: fatty acid oxygenase with a critical role in cell signaling
    • Rouzer CA, Marnett LJ. Structural and functional difference between cyclooxygenases: fatty acid oxygenase with a critical role in cell signaling. Biochem Biophys Res Commun 2005; 338:34-44.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 34-44
    • Rouzer, C.A.1    Marnett, L.J.2
  • 15
    • 0034654533 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinase cascades in mediating lipopolysaccharide-stimulated induction of cyclooxygenase-2 and IL-1β in RAW264 macrophages
    • Caivano M, Cohen P. Role of mitogen-activated protein kinase cascades in mediating lipopolysaccharide-stimulated induction of cyclooxygenase-2 and IL-1β in RAW264 macrophages. J Immunol 2000; 164:3018-25.
    • (2000) J Immunol , vol.164 , pp. 3018-3025
    • Caivano, M.1    Cohen, P.2
  • 16
    • 0034733046 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 is required for macrophage arachidonic acid release by agonists that Do and Do not mobilize calcium. Novel role of mitogen-activated protein kinase pathways in cytosolic phospholipase A2 regulation
    • Gijón MA, Spencer DM, Siddiqi AR, Bonventre JV, Leslie CC. Cytosolic phospholipase A2 is required for macrophage arachidonic acid release by agonists that Do and Do not mobilize calcium. Novel role of mitogen-activated protein kinase pathways in cytosolic phospholipase A2 regulation. J Biol Chem 2000; 275:20146-56.
    • (2000) J Biol Chem , vol.275 , pp. 20146-20156
    • Gijón, M.A.1    Spencer, D.M.2    Siddiqi, A.R.3    Bonventre, J.V.4    Leslie, C.C.5
  • 17
    • 16644382118 scopus 로고    scopus 로고
    • Regulatory mechanism and physiological role of cytosolic phospholipase A2
    • Hirabayashi T, Murayama T, Shimizu T. Regulatory mechanism and physiological role of cytosolic phospholipase A2. Biol Pharm Bull 2004; 27:1168-73.
    • (2004) Biol Pharm Bull , vol.27 , pp. 1168-1173
    • Hirabayashi, T.1    Murayama, T.2    Shimizu, T.3
  • 18
    • 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 CC, Sun YT, Chen JJ, Chang YJ. 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 2001; 59:493-500.
    • (2001) Mol Pharmacol , vol.59 , pp. 493-500
    • Chen, C.C.1    Sun, Y.T.2    Chen, J.J.3    Chang, Y.J.4
  • 19
    • 0035920233 scopus 로고    scopus 로고
    • Cot kinase induces cyclooxygenase-2 expression in T cells through activation of the nuclear factor of activated T cells
    • de Gregorio R, Iniguez MA, Fresno M, Alemany S. Cot kinase induces cyclooxygenase-2 expression in T cells through activation of the nuclear factor of activated T cells. J Biol Chem 2001; 276:27003-9.
    • (2001) J Biol Chem , vol.276 , pp. 27003-27009
    • de Gregorio, R.1    Iniguez, M.A.2    Fresno, M.3    Alemany, S.4
  • 20
    • 0034008927 scopus 로고    scopus 로고
    • Transcriptional activation of the cyclooxygenase-2 gene in endotoxin-treated RAW 264.7 macrophages
    • Wadleigh DJ, Reddy ST, Kopp E, Ghosh S, Herschman HR. Transcriptional activation of the cyclooxygenase-2 gene in endotoxin-treated RAW 264.7 macrophages. J Biol Chem 2000; 275:6259-66.
    • (2000) J Biol Chem , vol.275 , pp. 6259-6266
    • Wadleigh, D.J.1    Reddy, S.T.2    Kopp, E.3    Ghosh, S.4    Herschman, H.R.5
  • 21
    • 0026516073 scopus 로고
    • Calcium-regulated phosphorylation within the leucine zipper of C/EBPβ
    • Wegner M, Cao Z, Rosenfeld MG. Calcium-regulated phosphorylation within the leucine zipper of C/EBPβ. Science 1992; 256:370-3.
    • (1992) Science , vol.256 , pp. 370-373
    • Wegner, M.1    Cao, Z.2    Rosenfeld, M.G.3
  • 22
    • 78650666211 scopus 로고    scopus 로고
    • The role of the transcription factor CREB in immune function
    • Wen AY, Sakamoto KM, Miller LS. The role of the transcription factor CREB in immune function. J Immunol 2010; 185:6413-9.
    • (2010) J Immunol , vol.185 , pp. 6413-6419
    • Wen, A.Y.1    Sakamoto, K.M.2    Miller, L.S.3
  • 23
    • 65249140538 scopus 로고    scopus 로고
    • CREB in the pathophysiology of cancer: implications for targeting transcription factors for cancer therapy
    • Sakamoto KM, Frank DA. CREB in the pathophysiology of cancer: implications for targeting transcription factors for cancer therapy. Clin Cancer Res 2009; 15:2583-7.
    • (2009) Clin Cancer Res , vol.15 , pp. 2583-2587
    • Sakamoto, K.M.1    Frank, D.A.2
  • 24
    • 0035430282 scopus 로고    scopus 로고
    • Transcriptional regulation by the phosphorylation-dependent factor CREB
    • Mayr B, Montminy M. Transcriptional regulation by the phosphorylation-dependent factor CREB. Nat Rev Mol Cell Biol 2001; 2:599-609.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 599-609
    • Mayr, B.1    Montminy, M.2
  • 25
    • 0027176490 scopus 로고
    • Protein-kinase-A-dependent activator in transcription factor CREB reveals new role for CREM repressers
    • Brindle P, Linke S, Montminy M. Protein-kinase-A-dependent activator in transcription factor CREB reveals new role for CREM repressers. Nature 1993; 364:821-4.
    • (1993) Nature , vol.364 , pp. 821-824
    • Brindle, P.1    Linke, S.2    Montminy, M.3
  • 26
    • 0035886020 scopus 로고    scopus 로고
    • βc cytokine receptor-induced stimulation of cAMP response element binding protein phosphorylation requires protein kinase C in myeloid cells: a novel cytokine signal transduction cascade
    • Gubina E, Luo X, Kwon E, Sakamoto K, Shi YF, Mufson RA. βc cytokine receptor-induced stimulation of cAMP response element binding protein phosphorylation requires protein kinase C in myeloid cells: a novel cytokine signal transduction cascade. J Immunol 2001; 167:4303-10.
    • (2001) J Immunol , vol.167 , pp. 4303-4310
    • Gubina, E.1    Luo, X.2    Kwon, E.3    Sakamoto, K.4    Shi, Y.F.5    Mufson, R.A.6
  • 27
    • 33845973015 scopus 로고    scopus 로고
    • 2+- and protein kinase C-dependent signaling pathway for nuclear factor-κB activation, inducible nitric-oxide synthase expression, and tumor necrosis factor-α production in lipopolysaccharide-stimulated rat peritoneal macrophages
    • 2+- and protein kinase C-dependent signaling pathway for nuclear factor-κB activation, inducible nitric-oxide synthase expression, and tumor necrosis factor-α production in lipopolysaccharide-stimulated rat peritoneal macrophages. J Biol Chem 2006; 281:31337-47.
    • (2006) J Biol Chem , vol.281 , pp. 31337-31347
    • Zhou, X.1    Yang, W.2    Li, J.3
  • 28
    • 79952752523 scopus 로고    scopus 로고
    • + T lymphocytes in the presence and absence of follicular dendritic cells: inhibition of replication mediated by α-1-antitrypsin through altered IκBα ubiquitination
    • + T lymphocytes in the presence and absence of follicular dendritic cells: inhibition of replication mediated by α-1-antitrypsin through altered IκBα ubiquitination. J Immunol 2011; 186:3148-55.
    • (2011) J Immunol , vol.186 , pp. 3148-3155
    • Zhou, X.1    Shapiro, L.2    Fellingham, G.3    Willardson, B.M.4    Burton, G.F.5
  • 30
    • 34547652103 scopus 로고    scopus 로고
    • 2 and IL-10 in the cross-regulation of dendritic cell-derived inflammatory mediators
    • 2 and IL-10 in the cross-regulation of dendritic cell-derived inflammatory mediators. Cell Mol Immunol 2006; 3:271-7.
    • (2006) Cell Mol Immunol , vol.3 , pp. 271-277
    • Harizi, H.1    Gualde, N.2
  • 31
    • 0028954821 scopus 로고
    • Expression and role of cyclooxygenase isoforms in alveolar and peritoneal macrophages
    • Wilborn J, DeWitt DL, Peters-Golden M. Expression and role of cyclooxygenase isoforms in alveolar and peritoneal macrophages. Am J Physiol 1995; 268:L294-301.
    • (1995) Am J Physiol , vol.268 , pp. L294-L301
    • Wilborn, J.1    DeWitt, D.L.2    Peters-Golden, M.3
  • 32
    • 0026718175 scopus 로고
    • Calmodulin trapping by calcium-calmodulin-dependent protein kinase
    • Meyer T, Hanson PI, Stryer L, Schulman H. Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science 1992; 256:1199-202.
    • (1992) Science , vol.256 , pp. 1199-1202
    • Meyer, T.1    Hanson, P.I.2    Stryer, L.3    Schulman, H.4
  • 33
    • 0037246364 scopus 로고    scopus 로고
    • Roles of cysteinyl leukotrienes in airway inflammation, smooth muscle function, and remodeling
    • Holgate ST, Peters-Golden M, Panettieri RA, Henderson WR. Roles of cysteinyl leukotrienes in airway inflammation, smooth muscle function, and remodeling. J Allergy Clin Immunol 2003; 111:S18-36.
    • (2003) J Allergy Clin Immunol , vol.111 , pp. S18-S36
    • Holgate, S.T.1    Peters-Golden, M.2    Panettieri, R.A.3    Henderson, W.R.4
  • 34
    • 0027175061 scopus 로고
    • Calcium release-activated calcium current in rat mast cells
    • Hoth M, Penner R. Calcium release-activated calcium current in rat mast cells. J Physiol 1993; 465:359-86.
    • (1993) J Physiol , vol.465 , pp. 359-386
    • Hoth, M.1    Penner, R.2
  • 35
    • 15544368216 scopus 로고    scopus 로고
    • Store-operated calcium channels
    • Parekh AB, Putney JW. Store-operated calcium channels. Physiol Rev 2005; 85:757-810.
    • (2005) Physiol Rev , vol.85 , pp. 757-810
    • Parekh, A.B.1    Putney, J.W.2
  • 36
    • 23944491249 scopus 로고    scopus 로고
    • Bacteroides fragilis-derived lipopolysaccharide produces cell activation and lethal toxicity via toll-like receptor 4
    • Mancuso G, Midiri A, Biondo C et al. Bacteroides fragilis-derived lipopolysaccharide produces cell activation and lethal toxicity via toll-like receptor 4. Infect Immun 2005; 73:5620-7.
    • (2005) Infect Immun , vol.73 , pp. 5620-5627
    • Mancuso, G.1    Midiri, A.2    Biondo, C.3
  • 37
    • 0042236994 scopus 로고    scopus 로고
    • JNK-interacting protein 3 associates with Toll-like receptor 4 and is involved in LPS-mediated JNK activation
    • Matsuguchi T, Masuda A, Sugimoto K, Nagai Y, Yoshikai Y. JNK-interacting protein 3 associates with Toll-like receptor 4 and is involved in LPS-mediated JNK activation. EMBO J 2003; 22:4455-64.
    • (2003) EMBO J , vol.22 , pp. 4455-4464
    • Matsuguchi, T.1    Masuda, A.2    Sugimoto, K.3    Nagai, Y.4    Yoshikai, Y.5
  • 38
    • 0031065203 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced biphasic inositol 1,4,5-trisphosphate response and tyrosine phosphorylation of 140-kilodalton protein in mouse peritoneal macrophages
    • Shinji H, Akagawa KS, Tsuji M, Maeda M, Yamada R, Matsuura K, Yamamoto S, Yoshida T. Lipopolysaccharide-induced biphasic inositol 1, 4, 5-trisphosphate response and tyrosine phosphorylation of 140-kilodalton protein in mouse peritoneal macrophages. J Immunol 1997; 158:1370-6.
    • (1997) J Immunol , vol.158 , pp. 1370-1376
    • Shinji, H.1    Akagawa, K.S.2    Tsuji, M.3    Maeda, M.4    Yamada, R.5    Matsuura, K.6    Yamamoto, S.7    Yoshida, T.8
  • 39
    • 0025817633 scopus 로고
    • Activation by bacterial lipopolysaccharide causes changes in the cytosolic free calcium concentration in single peritoneal macrophages
    • Letari O, Nicosia S, Chiavaroli C, Vacher P, Schlegel W. Activation by bacterial lipopolysaccharide causes changes in the cytosolic free calcium concentration in single peritoneal macrophages. J Immunol 1991; 147:980-3.
    • (1991) J Immunol , vol.147 , pp. 980-983
    • Letari, O.1    Nicosia, S.2    Chiavaroli, C.3    Vacher, P.4    Schlegel, W.5
  • 40
    • 84859735442 scopus 로고    scopus 로고
    • SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling
    • Palty R, Raveh A, Kaminsky I, Meller R, Reuveny E. SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling. Cell 2012; 149:425-38.
    • (2012) Cell , vol.149 , pp. 425-438
    • Palty, R.1    Raveh, A.2    Kaminsky, I.3    Meller, R.4    Reuveny, E.5
  • 45
    • 59449110657 scopus 로고    scopus 로고
    • Stromal interaction molecule (STIM) 1 and STIM2 calcium sensing regions exhibit distinct unfolding and oligomerization kinetics
    • Stathopulos PB, Zheng L, Ikura M. Stromal interaction molecule (STIM) 1 and STIM2 calcium sensing regions exhibit distinct unfolding and oligomerization kinetics. J Biol Chem 2009; 284:728-32.
    • (2009) J Biol Chem , vol.284 , pp. 728-732
    • Stathopulos, P.B.1    Zheng, L.2    Ikura, M.3
  • 47
    • 34347391261 scopus 로고    scopus 로고
    • CREB - a real culprit in oncogenesis
    • Siu YT, Jin DY. CREB - a real culprit in oncogenesis. FEBS J 2007; 274:3224-32.
    • (2007) FEBS J , vol.274 , pp. 3224-3232
    • Siu, Y.T.1    Jin, D.Y.2
  • 48
    • 0037184087 scopus 로고    scopus 로고
    • The role of cAMP-dependent signaling in receptor-recognized forms of α2-macroglobulin-induced cellular proliferation
    • Misra UK, Akabani G, Pizzo SV. The role of cAMP-dependent signaling in receptor-recognized forms of α2-macroglobulin-induced cellular proliferation. J Biol Chem 2002; 277:36509-20.
    • (2002) J Biol Chem , vol.277 , pp. 36509-36520
    • Misra, U.K.1    Akabani, G.2    Pizzo, S.V.3
  • 49
    • 52049121528 scopus 로고    scopus 로고
    • Calmodulin-kinases: modulators of neuronal development and plasticity
    • Wayman GA, Lee YS, Tokumitsu H, Silva A, Soderling TR. Calmodulin-kinases: modulators of neuronal development and plasticity. Neuron 2008; 59:914-31.
    • (2008) Neuron , vol.59 , pp. 914-931
    • Wayman, G.A.1    Lee, Y.S.2    Tokumitsu, H.3    Silva, A.4    Soderling, T.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.