메뉴 건너뛰기




Volumn 29, Issue 3, 2012, Pages 454-460

BAI, a 3-aminoindazole derivative, inhibits interleukin-1β-induced expression of cyclooxygenase-2 in A549 human airway cells

Author keywords

A549 cells; BAI; Cyclin dependent kinase; Cyclooxygenase 2; Histone H1; Interleukin 1

Indexed keywords

2 [(1,1' BIPHENYL) 4 YL] N [5 (1,1 DIOXO 1 LAMBDA 6 ISOTHIAZOLIDIN 2 YL) 1H INDAZOL 3 YL]ACETAMIDE; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 4; CYCLOOXYGENASE 2; HISTONE H1; I KAPPA B ALPHA; INDAZOLE DERIVATIVE; INTERLEUKIN 1BETA; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 84862975365     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm.2011.863     Document Type: Article
Times cited : (3)

References (43)
  • 1
    • 0029975669 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide H synthases-1 and -2
    • Smith WL and Dewitt DL: Prostaglandin endoperoxide H synthases-1 and -2. Adv Immunol 62: 167-215, 1996. (Pubitemid 26250630)
    • (1996) Advances in Immunology , vol.62 , pp. 167-215
    • Smith, W.L.1    DeWitt, D.L.2
  • 2
    • 0030479496 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2
    • DOI 10.1074/jbc.271.52.33157
    • Smith WL, Garavito RM and DeWitt DL: Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2. J Biol Chem 271: 33157-33160, 1996. (Pubitemid 27010118)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.52 , pp. 33157-33160
    • Smith, W.L.1    Garavito, R.M.2    DeWitt, D.L.3
  • 6
    • 28944455472 scopus 로고    scopus 로고
    • An update on nonsteroidal anti-inflammatory drugs and cyclooxygenase-2 inhibitors
    • Williams GW: An update on nonsteroidal anti-inflammatory drugs and cyclooxygenase-2 inhibitors. Curr Pain Headache Rep 9: 377-389, 2005.
    • (2005) Curr Pain Headache Rep , vol.9 , pp. 377-389
    • Williams, G.W.1
  • 8
    • 0028824312 scopus 로고
    • Transcriptional regulation of human prostaglandin-endoperoxide synthase-2 gene by lipopolysaccharide and phorbol ester in vascular endothelial cell. Involvement of both nuclear factor for interleukin-6 expression site and cAMP response element
    • Inoue H, Yokoyama C, Hara S, Tone Y and Tanabe T: Transcriptional regulation of human prostaglandin-endoperoxide synthase-2 gene by lipopolysaccharide and phorbol ester in vascular endothelial cell. Involvement of both nuclear factor for interleukin-6 expression site and cAMP response element. J Biol Chem 270: 24965-24971, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 24965-24971
    • Inoue, H.1    Yokoyama, C.2    Hara, S.3    Tone, Y.4    Tanabe, T.5
  • 10
    • 0028180129 scopus 로고
    • Induction of cyclooxygenase-2 by interleukin-1alpha. Evidence for post-transcriptional regulation
    • Ristimäki A, Garfinkel S, Wessendorf J, Maciag T and Hla T: Induction of cyclooxygenase-2 by interleukin-1alpha. Evidence for post-transcriptional regulation. J Biol Chem 269: 11769-11775, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 11769-11775
    • Ristimäki, A.1    Garfinkel, S.2    Wessendorf, J.3    Maciag, T.4    Hla, T.5
  • 11
    • 0027967245 scopus 로고
    • IL-1 beta stabilizes COX-2 mRNA in renal mesangial cells: Role of 3′-untranslated region
    • Srivastava SK, Tetsuka T, Daphna-Iken D and Morrison AR: IL-1 beta stabilizes COX-2 mRNA in renal mesangial cells: role of 3′-untranslated region. Am J Physiol 267: 504-508, 1994.
    • (1994) Am J Physiol , vol.267 , pp. 504-508
    • Srivastava, S.K.1    Tetsuka, T.2    Daphna-Iken, D.3    Morrison, A.R.4
  • 12
    • 0030815847 scopus 로고    scopus 로고
    • Superinduction of COX-2 mRNA by cycloheximide and interleukin-1beta involves increased transcription and correlates with increased NF-kappaB and JNK activation
    • DOI 10.1016/S0014-5793(97)01362-8, PII S0014579397013628
    • Newton R, Stevens DA, Hart LA, Lindsay M, Adcock IM and Barnes PJ: Super-induction of COX-2 mRNA by cyclohexamide and interleukin-1beta involves increased transcription and correlates with increased NF-kappaB and JNK activation. FEBS Lett 418: 135-138, 1997. (Pubitemid 27514432)
    • (1997) FEBS Letters , vol.418 , Issue.1-2 , 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
  • 13
    • 0037474226 scopus 로고    scopus 로고
    • Leptomycin B, an inhibitor of the nuclear export receptor CRM1, inhibits COX-2 expression
    • DOI 10.1074/jbc.C200620200
    • Jang BC, Muñoz-Najar U, Paik JH, Claffey K, Yoshida M and Hla T: Leptomycin B, an inhibitor of the nuclear export receptor CRM1, inhibits COX-2 expression. J Biol Chem 278: 2773-2776, 2003. (Pubitemid 36801177)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , pp. 2773-2776
    • Jang, B.-C.1    Munoz-Najar, U.2    Paik, J.-H.3    Claffey, K.4    Yoshida, M.5    Hla, T.6
  • 14
    • 34247505895 scopus 로고    scopus 로고
    • Regulation of intracellular cyclooxygenase levels by gene transcription and protein degradation
    • DOI 10.1016/j.plipres.2007.01.001, PII S0163782707000021
    • Kang YJ, Mbonye UR, DeLong CJ, Wada M and Smith WL: Regulation of intracellular cyclooxygenase levels by gene transcription and protein degradation. Prog Lipid Res 46: 108-125, 2007. (Pubitemid 46661865)
    • (2007) Progress in Lipid Research , vol.46 , Issue.2 , pp. 108-125
    • Kang, Y.-J.1    Mbonye, U.R.2    DeLong, C.J.3    Wada, M.4    Smith, W.L.5
  • 15
    • 43749094995 scopus 로고    scopus 로고
    • Two distinct pathways for cyclooxygenase-2 protein degradation
    • Mbonye UR, Yuan C, Harris CE, et al: Two distinct pathways for cyclooxygenase-2 protein degradation. J Biol Chem 283: 8611-8623, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 8611-8623
    • Mbonye, U.R.1    Yuan, C.2    Harris, C.E.3
  • 16
    • 0026730021 scopus 로고
    • Human cyclooxygenase-2 cDNA
    • Hla T and Neilson K: Human cyclooxygenase-2 cDNA. Proc Natl Acad Sci USA 89: 7384-7388, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7384-7388
    • Hla, T.1    Neilson, K.2
  • 17
    • 0027327231 scopus 로고
    • N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum
    • Otto JC, DeWitt DL and Smith WL: N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and ther orientations in the endoplasmic reticulum. J Biol Chem 268: 18234-18242, 1993. (Pubitemid 23260348)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.24 , pp. 18234-18242
    • Otto, J.C.1    DeWitt, D.L.2    Smith, W.L.3
  • 18
    • 0035852985 scopus 로고    scopus 로고
    • Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry
    • DOI 10.1021/bi002313c
    • Nemeth JF, Hochgesang GP, Marnett LJ and Caprioli RM: Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry. Biochemistry 40: 3109-3116, 2001. (Pubitemid 32205354)
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3109-3116
    • Nemeth, J.F.1    Hochensang Jr., G.P.2    Marnett, L.J.3    Caprioli, R.M.4
  • 19
    • 34948874369 scopus 로고    scopus 로고
    • Glucosamine hydrochloride specifically inhibits COX-2 by preventing COX-2 N-glycosylation and by increasing COX-2 protein turnover in a proteasome-dependent manner
    • Jang BC, Sung SH, Park JG, et al: Glucosamine hydrochloride specifically inhibits COX-2 by preventing COX-2 N-glycosylation and by increasing COX-2 protein turnover in a proteasome-dependent manner. J Biol Chem 282: 27622-27632, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 27622-27632
    • Jang, B.C.1    Sung, S.H.2    Park, J.G.3
  • 20
    • 0034671539 scopus 로고    scopus 로고
    • Serum withdrawal-induced post-transcriptional stabilization of cyclooxygenase-2 mRNA in MDA-MB-231 mammary carcinoma cells requires the activity of the p38 stress-activated protein kinase
    • DOI 10.1074/jbc.M003224200
    • Jang BC, Sanchez T, Schaefers HJ, et al: Serum withdrawal-induced post-transcriptional stabilization of cyclooxygenase-2 mRNA in MDA-MB-231 mammary carcinoma cells requires the activity of the p38 stress-activated protein kinase. J Biol Chem 275: 39507-39515, 2000. (Pubitemid 32058977)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 39507-39515
    • Jang, B.-C.1    Sanchez, T.2    Schaefers, H.-J.3    Trifan, O.C.4    Liu, C.H.5    Creminon, C.6    Huang, C.-K.7    Hla, T.8
  • 21
    • 0035963309 scopus 로고    scopus 로고
    • Role of p38 MAP kinases and ERK in mediating ultraviolet-B induced cyclooxygenase-2 gene expression in human keratinocytes
    • DOI 10.1038/sj.onc.1204530
    • Chen W, Tang Q, Gonzales MS and Bowden GT: Role of p38 MAP kinases and ERK in mediation ultraviolet-B induced cyclooxygenase- 2 gene expression in human keratinocytes. Oncogene 20: 3921-3926, 2001. (Pubitemid 32646203)
    • (2001) Oncogene , vol.20 , Issue.29 , pp. 3921-3926
    • Chen, W.1    Tang, Q.2    Gonzales, M.S.3    Bowden, G.T.4
  • 22
    • 33845225077 scopus 로고    scopus 로고
    • Tangeretin suppresses IL-1beta-induced cyclooxygenase (COX)-2 expression through inhibition of p38 MAPK, JNK, and AKT activation in human lung carcinoma cells
    • Chen KH, Weng MS and Lin JK: Tangeretin suppresses IL-1beta-induced cyclooxygenase (COX)-2 expression through inhibition of p38 MAPK, JNK, and AKT activation in human lung carcinoma cells. Biochem Pharmacol 73: 215-227, 2007.
    • (2007) Biochem Pharmacol , vol.73 , pp. 215-227
    • Chen, K.H.1    Weng, M.S.2    Lin, J.K.3
  • 24
    • 58149202051 scopus 로고    scopus 로고
    • Induction of CO-2 in human airway cells by manganese: Role of PI3K/PKB, p38 MAPK, PKCS, Src, and glutathione depletion
    • Jang BC: Induction of CO-2 in human airway cells by manganese: role of PI3K/PKB, p38 MAPK, PKCS, Src, and glutathione depletion. Toxicol In Vitro 23: 120-126, 2009.
    • (2009) Toxicol in Vitro , vol.23 , pp. 120-126
    • Jang, B.C.1
  • 26
    • 68049115404 scopus 로고    scopus 로고
    • Anticancer activity and differentially expressed genes in head and neck cancer cells treated with a novel cyclin-dependent kinase inhibitor
    • Shin HC, Song DW, Baek WK, et al: Anticancer activity and differentially expressed genes in head and neck cancer cells treated with a novel cyclin-dependent kinase inhibitor. Chemotherapy 55: 353-362, 2009.
    • (2009) Chemotherapy , vol.55 , pp. 353-362
    • Shin, H.C.1    Song, D.W.2    Baek, W.K.3
  • 28
    • 0038755585 scopus 로고    scopus 로고
    • 2, cyclooxygenase-1 and -2 expression by PMA, TNFalpha, LPS and M-CSF in human monocytes and macrophages
    • DOI 10.1023/A:1023495626568
    • Jiang YJ, Lu B, Choy PC and Hatch GM: Regulation of cytosolic phospholipase A2, cyclooxygenase-1 and -2 expression by PMA, TNF alpha, LPS and M-CSF in human monocytes and macrophages. Mol Cell Biochem 246: 31-38, 2003. (Pubitemid 36798719)
    • (2003) Molecular and Cellular Biochemistry , vol.246 , Issue.1-2 , pp. 31-38
    • Jiang, Y.J.1    Lu, B.2    Choy, P.C.3    Hatch, G.M.4
  • 29
    • 80053209811 scopus 로고    scopus 로고
    • Overexpression of cyclooxygenase-2 in NCI-H292 human alveolar epithelial carcinoma cells: Roles of p38 MAPK, ERK-1/2, and PI3K/PKB signaling proteins
    • Sung S, Park Y, Jo JR, et al: Overexpression of cyclooxygenase-2 in NCI-H292 human alveolar epithelial carcinoma cells: roles of p38 MAPK, ERK-1/2, and PI3K/PKB signaling proteins. J Cell Biochem 112: 3015-3024, 2011.
    • (2011) J Cell Biochem , vol.112 , pp. 3015-3024
    • Sung, S.1    Park, Y.2    Jo, J.R.3
  • 30
    • 0025266685 scopus 로고
    • Activation of in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B
    • Ghosh S and Baltimore D: Activation of in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature 344: 678-682, 1990.
    • (1990) Nature , vol.344 , pp. 678-682
    • Ghosh, S.1    Baltimore, D.2
  • 31
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • DOI 10.1083/jcb.83.2.403
    • Thoma F, Koller T and Klug A: Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J Biol Chem 83: 403-427, 1979. (Pubitemid 10205723)
    • (1979) Journal of Cell Biology , vol.83 , Issue.2 I , pp. 403-427
    • Thoma, F.1    Koller, T..2    Klug, A.3
  • 32
    • 0033151772 scopus 로고    scopus 로고
    • Histone H1: Location and role
    • Thomas JO: Histone H1: location and role. Curr Opin Cell Biol 11: 312-317, 1999.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 312-317
    • Thomas, J.O.1
  • 33
    • 33846488609 scopus 로고    scopus 로고
    • Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue
    • DOI 10.1074/mcp.M00255-MCP200
    • Wisniewski JR, Zougman A, Krüger S and Mann M: Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylation, methylation, and phosphorylation as well as differences between cell culture and tissue. Mol Cell Proteomics 6: 72-87, 2007. (Pubitemid 46152693)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.1 , pp. 72-87
    • Wisniewski, J.R.1    Zougman, A.2    Kruger, S.3    Mann, M.4
  • 34
    • 0030576509 scopus 로고    scopus 로고
    • Linker histone H1 regulates specific gene expression but not global transcription in vivo
    • DOI 10.1016/S0092-8674(00)80120-8
    • Shen X and Gorovsky MA: Linker histone H1 regulates specific gene expression but not global transcription in vivo. Cell 86: 475-483, 1996. (Pubitemid 26272087)
    • (1996) Cell , vol.86 , Issue.3 , pp. 475-483
    • Shen, X.1    Gorovsky, M.A.2
  • 35
    • 0035958006 scopus 로고    scopus 로고
    • Decreased expression of specific genes in yeast cells lacking histone H1
    • Hellauer K, Sirard E and Turcotte B: Decreased expression of specific genes in yeast cells lacking histone H1. J Biol Chem 276: 13587-13592, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 13587-13592
    • Hellauer, K.1    Sirard, E.2    Turcotte, B.3
  • 36
    • 0029155905 scopus 로고
    • Phosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei
    • Lu MJ, Mpoke SS, Dadd CA and Allis CD: Phosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei. Mol Biol Cell 6: 1077-1087, 1995.
    • (1995) Mol Biol Cell , vol.6 , pp. 1077-1087
    • Lu, M.J.1    Mpoke, S.S.2    Dadd, C.A.3    Allis, C.D.4
  • 37
    • 0029013311 scopus 로고
    • Linker histones are not essential and affect chromatin condensation in vivo
    • Shen X, Yu L, Weir JW and Gorovsky MA: Linker histones are not essential and affect chromatin condensation in vivo. Cell 82: 47-56, 1995.
    • (1995) Cell , vol.82 , pp. 47-56
    • Shen, X.1    Yu, L.2    Weir, J.W.3    Gorovsky, M.A.4
  • 38
    • 49249102932 scopus 로고    scopus 로고
    • Phosphorylation of the carboxy-terminal domain of histone H1: Effects on secondary structure and DNA condensation
    • Roque A, Ponte I, Arrondo JL and Suau P: Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation. Nucleic Acids Res 36: 4719-4726, 2008.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4719-4726
    • Roque, A.1    Ponte, I.2    Arrondo, J.L.3    Suau, P.4
  • 39
    • 0026545414 scopus 로고
    • Chromatin condensation: Does histone H1 dephosphorylation play a role?
    • Roth SY and Allis CD: Chromatin condensation: does histone H1 dephosphorylation play a role? Trends Biochem Sci 17: 93-98, 1992.
    • (1992) Trends Biochem Sci , vol.17 , pp. 93-98
    • Roth, S.Y.1    Allis, C.D.2
  • 41
    • 33744548700 scopus 로고    scopus 로고
    • Phosphorylation of the Linker Histone H1 by CDK Regulates Its Binding to HP1alpha
    • DOI 10.1016/j.molcel.2006.04.016, PII S1097276506002644
    • Hale TK, Contreras A, Morrison AJ and Herrera RE: Phosphorylation of the linker histone H1 by CDK regulates its binding to HP1alpha. Mol Cell 22: 693-699, 2006. (Pubitemid 43817599)
    • (2006) Molecular Cell , vol.22 , Issue.5 , pp. 693-699
    • Hale, T.K.1    Contreras, A.2    Morrison, A.J.3    Herrera, R.E.4
  • 42
    • 32944467415 scopus 로고    scopus 로고
    • The cyclin-dependent kinase 2 inhibitor down-regulates interleukin-1beta- mediated induction of cyclooxygenase-2 expression in human lung carcinoma cells
    • DOI 10.1158/0008-5472.CAN-05-3317
    • Mukhopadhyay P, Ali MA, Nandi A, Carreon P, Choy H and Saha D: The cyclin-dependent kinase 2 inhibitor down-regulates interleukin-1beta-mediated induction of cyclooxygenase-2 expression in human lung carcinoma cells. Cancer Res 66: 1758-1766, 2006. (Pubitemid 43259961)
    • (2006) Cancer Research , vol.66 , Issue.3 , pp. 1758-1766
    • Mukhopadhyay, P.1    Ali, M.A.2    Nandi, A.3    Carreon, P.4    Choy, H.5    Saha, D.6
  • 43
    • 57749117141 scopus 로고    scopus 로고
    • Fragment-based discovery of JAK-2 inhibitors
    • Antonysamy S, Hirst G, Park F, et al: Fragment-based discovery of JAK-2 inhibitors. Bioorg Med Chem Lett 19: 279-282, 2009.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 279-282
    • Antonysamy, S.1    Hirst, G.2    Park, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.