메뉴 건너뛰기




Volumn 9, Issue 4, 2009, Pages 499-507

Glycyrrhiza inflata-derived chalcones, Licochalcone A, Licochalcone B and Licochalcone D, inhibit phosphorylation of NF-κB p65 in LPS signaling pathway

Author keywords

Glycyrrhiza inflata; Licochalcone A; Licochalcone B; Licochalcone D; LPS; NF B

Indexed keywords

CHALCONE DERIVATIVE; CYCLIC AMP DEPENDENT PROTEIN KINASE; ECHINATIN; I KAPPA B; ISOLIQUIRITIGENIN; LICOCHALCONE A; LICOCHALCONE B; LICOCHALCONE C; LICOCHALCONE D; LIPOPOLYSACCHARIDE; LUCIFERASE; MONOCYTE CHEMOTACTIC PROTEIN 1; NITRIC OXIDE; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 61649115375     PISSN: 15675769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.intimp.2009.01.031     Document Type: Article
Times cited : (116)

References (41)
  • 1
    • 0014888273 scopus 로고
    • Pathology of inflammatory diseases
    • Suppl
    • Morson B.C. Pathology of inflammatory diseases. Proc R Soc Med 63 (1970) 63 Suppl
    • (1970) Proc R Soc Med , vol.63 , pp. 63
    • Morson, B.C.1
  • 2
    • 34249709500 scopus 로고    scopus 로고
    • Complexities of targeting innate immunity to treat infection
    • Brown K.L., Cosseau C., Gardy J.L., and Hancock R.E. Complexities of targeting innate immunity to treat infection. Trends Immunol 28 (2007) 260-266
    • (2007) Trends Immunol , vol.28 , pp. 260-266
    • Brown, K.L.1    Cosseau, C.2    Gardy, J.L.3    Hancock, R.E.4
  • 3
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S., Uematsu S., and Takeuchi O. Pathogen recognition and innate immunity. Cell 124 (2006) 783-801
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 4
    • 0029090285 scopus 로고
    • Molecular mechanism in tolerance to lipopolysaccharide
    • Ziegler-Heitbrock H.W. Molecular mechanism in tolerance to lipopolysaccharide. J Inflamm 45 (1995) 13-26
    • (1995) J Inflamm , vol.45 , pp. 13-26
    • Ziegler-Heitbrock, H.W.1
  • 5
    • 0034984262 scopus 로고    scopus 로고
    • Innate immunity and inflammation: a transcriptional paradigm
    • Hawiger J. Innate immunity and inflammation: a transcriptional paradigm. Immunol Res 23 (2001) 99-109
    • (2001) Immunol Res , vol.23 , pp. 99-109
    • Hawiger, J.1
  • 6
    • 0035104119 scopus 로고    scopus 로고
    • LPS induction of gene expression in human monocytes
    • Guha M., and Mackman N. LPS induction of gene expression in human monocytes. Cell Signal 13 (2001) 85-94
    • (2001) Cell Signal , vol.13 , pp. 85-94
    • Guha, M.1    Mackman, N.2
  • 7
    • 0027264083 scopus 로고
    • Nuclear factor kappa B, a mediator of lipopolysaccharide effects
    • Müller J.M., Ziegler-Heitbrock H.W., and Baeuerle P.A. Nuclear factor kappa B, a mediator of lipopolysaccharide effects. Immunobiology 187 (1993) 233-256
    • (1993) Immunobiology , vol.187 , pp. 233-256
    • Müller, J.M.1    Ziegler-Heitbrock, H.W.2    Baeuerle, P.A.3
  • 8
    • 0027939931 scopus 로고
    • Role of transcription factor NF-kappa B/Rel in induction of nitric oxide synthase
    • Xie Q.W., Kashiwabara Y., and Nathan C. Role of transcription factor NF-kappa B/Rel in induction of nitric oxide synthase. J Biol Chem 269 (1994) 4705-4708
    • (1994) J Biol Chem , vol.269 , pp. 4705-4708
    • Xie, Q.W.1    Kashiwabara, Y.2    Nathan, C.3
  • 9
    • 0027255749 scopus 로고
    • Promoter of the mouse gene encoding calcium-independent nitric oxide synthase confers inducibility by interferon gamma and bacterial lipopolysaccharide
    • Xie Q.W., Whisnant R., and Nathan C. Promoter of the mouse gene encoding calcium-independent nitric oxide synthase confers inducibility by interferon gamma and bacterial lipopolysaccharide. J Exp Med 177 (1993) 1779-1784
    • (1993) J Exp Med , vol.177 , pp. 1779-1784
    • Xie, Q.W.1    Whisnant, R.2    Nathan, C.3
  • 10
    • 0025186678 scopus 로고
    • Kappa B-type enhancers are involved in lipopolysaccharide-mediated transcriptional activation of the tumor necrosis factor alpha gene in primary macrophages
    • Shakhov A.N., Collart M.A., Vassalli P., Nedospasov S.A., and Jongeneel C.V. Kappa B-type enhancers are involved in lipopolysaccharide-mediated transcriptional activation of the tumor necrosis factor alpha gene in primary macrophages. J Exp Med 171 (1990) 35-47
    • (1990) J Exp Med , vol.171 , pp. 35-47
    • Shakhov, A.N.1    Collart, M.A.2    Vassalli, P.3    Nedospasov, S.A.4    Jongeneel, C.V.5
  • 11
    • 0031041059 scopus 로고    scopus 로고
    • Activation of the transcription factor NF-kappaB in lipopolysaccharide-stimulated U937 cells
    • Legrand-Poels S., Maniglia S., Boelaert J.R., and Piette J. Activation of the transcription factor NF-kappaB in lipopolysaccharide-stimulated U937 cells. Biochem Pharmacol 53 (1997) 339-346
    • (1997) Biochem Pharmacol , vol.53 , pp. 339-346
    • Legrand-Poels, S.1    Maniglia, S.2    Boelaert, J.R.3    Piette, J.4
  • 12
    • 0033938394 scopus 로고    scopus 로고
    • Differential induction of JE/MCP-1 in subclones from a murine macrophage cell line, RAW 264.7: role of kappaB-3 binding protein
    • Ueno M., Sonoda Y., Funakoshi M., Mukaida N., Nose K., and Kasahara T. Differential induction of JE/MCP-1 in subclones from a murine macrophage cell line, RAW 264.7: role of kappaB-3 binding protein. Cytokine 12 (2000) 207-219
    • (2000) Cytokine , vol.12 , pp. 207-219
    • Ueno, M.1    Sonoda, Y.2    Funakoshi, M.3    Mukaida, N.4    Nose, K.5    Kasahara, T.6
  • 13
    • 33749152085 scopus 로고    scopus 로고
    • Toll-like receptors: from the discovery of NFkappaB to new insights into transcriptional regulations in innate immunity
    • Doyle S.L., and O'Neill L.A. Toll-like receptors: from the discovery of NFkappaB to new insights into transcriptional regulations in innate immunity. Biochem Pharmacol 72 (2006) 1102-1113
    • (2006) Biochem Pharmacol , vol.72 , pp. 1102-1113
    • Doyle, S.L.1    O'Neill, L.A.2
  • 15
    • 0033574415 scopus 로고    scopus 로고
    • Toll-like receptor-4 mediates lipopolysaccharide-induced signal transduction
    • Chow J.C., Young D.W., Golenbock D.T., Christ W.J., and Gusovsky F. Toll-like receptor-4 mediates lipopolysaccharide-induced signal transduction. J Biol Chem 274 (1999) 10689-10692
    • (1999) J Biol Chem , vol.274 , pp. 10689-10692
    • Chow, J.C.1    Young, D.W.2    Golenbock, D.T.3    Christ, W.J.4    Gusovsky, F.5
  • 16
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB
    • DiDonato J.A., Hayakawa M., Rothwarf D.M., Zandi E., and Karin M. A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB. Nature 388 (1997) 548-554
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 17
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • Zandi E., Rothwarf D.M., Delhase M., Hayakawa M., and Karin M. The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 91 (1997) 243-252
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 18
    • 0030685825 scopus 로고    scopus 로고
    • IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation
    • Mercurio F., Zhu H., Murray B.W., Shevchenko A., Bennett B.L., Li J., et al. IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation. Science 278 (1997) 860-866
    • (1997) Science , vol.278 , pp. 860-866
    • Mercurio, F.1    Zhu, H.2    Murray, B.W.3    Shevchenko, A.4    Bennett, B.L.5    Li, J.6
  • 19
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation
    • Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F., et al. Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 93 (1998) 1231-1240
    • (1998) Cell , vol.93 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6
  • 20
    • 0025697325 scopus 로고
    • Formation of free radicals and nitric oxide derivative of hemoglobin in rats during shock syndrome
    • Westenberger U., Thanner S., Ruf H.H., Gersonde K., Sutter G., and Trentz O. Formation of free radicals and nitric oxide derivative of hemoglobin in rats during shock syndrome. Free Radic Res Commun 11 (1990) 167-178
    • (1990) Free Radic Res Commun , vol.11 , pp. 167-178
    • Westenberger, U.1    Thanner, S.2    Ruf, H.H.3    Gersonde, K.4    Sutter, G.5    Trentz, O.6
  • 21
    • 33751520650 scopus 로고    scopus 로고
    • Cellular reprogramming by gram-positive bacterial components: a review
    • Buckley J.M., Wang J.H., and Redmond H.P. Cellular reprogramming by gram-positive bacterial components: a review. J Leukoc Biol 80 (2006) 731-741
    • (2006) J Leukoc Biol , vol.80 , pp. 731-741
    • Buckley, J.M.1    Wang, J.H.2    Redmond, H.P.3
  • 22
    • 0027196986 scopus 로고
    • Mechanisms of endotoxin shock and endotoxin hypersensitivity
    • Galanos C., and Freudenberg M.A. Mechanisms of endotoxin shock and endotoxin hypersensitivity. Immunobiology 187 (1993) 346-356
    • (1993) Immunobiology , vol.187 , pp. 346-356
    • Galanos, C.1    Freudenberg, M.A.2
  • 23
    • 0000871575 scopus 로고    scopus 로고
    • Cellular activation mechanisms in septic shock
    • Downey J.S., and Han J. Cellular activation mechanisms in septic shock. Front Biosci 3 (1998) d468-d476
    • (1998) Front Biosci , vol.3
    • Downey, J.S.1    Han, J.2
  • 24
    • 0023734093 scopus 로고
    • Two new flavonoids and other constituents in licorice root: their relative astringency and radical scavenging effects
    • Hatano T., Kagawa H., Yasuhara T., and Okuda T. Two new flavonoids and other constituents in licorice root: their relative astringency and radical scavenging effects. Chem Pharm Bull 36 (1988) 2090-2097
    • (1988) Chem Pharm Bull , vol.36 , pp. 2090-2097
    • Hatano, T.1    Kagawa, H.2    Yasuhara, T.3    Okuda, T.4
  • 25
    • 0033785922 scopus 로고    scopus 로고
    • A drug over the millennia: pharmacognosy, chemistry, and pharmacology of licorice
    • Shibata S. A drug over the millennia: pharmacognosy, chemistry, and pharmacology of licorice. Yakugaku Zasshi 120 (2000) 849-862
    • (2000) Yakugaku Zasshi , vol.120 , pp. 849-862
    • Shibata, S.1
  • 26
    • 60549108717 scopus 로고    scopus 로고
    • Licochalcone A significantly suppresses LPS signaling pathway through the inhibition of NF-κB p65 phosphorylation at serine 276
    • in press
    • Furusawa J, Funakoshi-Tago M, Tago K, Mashino T, Inoue H, Sonoda Y, et al. Licochalcone A significantly suppresses LPS signaling pathway through the inhibition of NF-κB p65 phosphorylation at serine 276. Cell Signal. (in press).
    • Cell Signal
    • Furusawa, J.1    Funakoshi-Tago, M.2    Tago, K.3    Mashino, T.4    Inoue, H.5    Sonoda, Y.6
  • 27
    • 56549085955 scopus 로고    scopus 로고
    • Licochalcone A is a potent inhibitor of TEL-Jak2-mediated transformation through the specific inhibition of Stat3 activation
    • Funakoshi-Tago M., Tago K., Nishizawa C., Takahashi K., Mashino T., Iwata S., et al. Licochalcone A is a potent inhibitor of TEL-Jak2-mediated transformation through the specific inhibition of Stat3 activation. Biochem Pharmacol (Sep 19 2008)
    • (2008) Biochem Pharmacol
    • Funakoshi-Tago, M.1    Tago, K.2    Nishizawa, C.3    Takahashi, K.4    Mashino, T.5    Iwata, S.6
  • 28
    • 0031772683 scopus 로고    scopus 로고
    • Nitric oxide-mediated modulation of interleukin-8 production by a human glioblastoma cell line, T98G, cocultured with myeloid and monocytic cell lines
    • Oda T., Kasahara T., Matsuura M., and Mukaida N. Nitric oxide-mediated modulation of interleukin-8 production by a human glioblastoma cell line, T98G, cocultured with myeloid and monocytic cell lines. J Interferon Cytokine Res 18 (1998) 905-912
    • (1998) J Interferon Cytokine Res , vol.18 , pp. 905-912
    • Oda, T.1    Kasahara, T.2    Matsuura, M.3    Mukaida, N.4
  • 29
    • 0042707525 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced nuclear factor kappaB activation is impaired in focal adhesion kinase-deficient fibroblasts
    • Funakoshi-Tago M., Sonoda Y., Tanaka S., Hashimoto K., Tago K., Tominaga S., et al. Tumor necrosis factor-induced nuclear factor kappaB activation is impaired in focal adhesion kinase-deficient fibroblasts. J Biol Chem 278 (2003) 29359-29365
    • (2003) J Biol Chem , vol.278 , pp. 29359-29365
    • Funakoshi-Tago, M.1    Sonoda, Y.2    Tanaka, S.3    Hashimoto, K.4    Tago, K.5    Tominaga, S.6
  • 30
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300
    • Zhong H., Voll R.E., and Ghosh S. Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol Cell 1 (1998) 661-671
    • (1998) Mol Cell , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Ghosh, S.3
  • 31
    • 0032589462 scopus 로고    scopus 로고
    • IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain
    • Sakurai H., Chiba H., Miyoshi H., Sugita T., and Toriumi W. IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain. J Biol Chem 274 (1999) 30353-30356
    • (1999) J Biol Chem , vol.274 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 32
    • 38649129368 scopus 로고    scopus 로고
    • Inhibition of phorbol ester-dependent peroxiredoxin I gene activation by lipopolysaccharide via phosphorylation of RelA/p65 at serine 276 in monocytes
    • Wijayanti N., Naidu S., Kietzmann T., and Immenschuh S. Inhibition of phorbol ester-dependent peroxiredoxin I gene activation by lipopolysaccharide via phosphorylation of RelA/p65 at serine 276 in monocytes. Free Radic Biol Med 44 (2008) 699-710
    • (2008) Free Radic Biol Med , vol.44 , pp. 699-710
    • Wijayanti, N.1    Naidu, S.2    Kietzmann, T.3    Immenschuh, S.4
  • 33
    • 43249114058 scopus 로고    scopus 로고
    • Repression of gene expression by unphosphorylated NF-kappaB p65 through epigenetic mechanisms
    • Dong J., Jimi E., Zhong H., Hayden M.S., and Ghosh S. Repression of gene expression by unphosphorylated NF-kappaB p65 through epigenetic mechanisms. Genes Dev 22 (2008) 1159-1173
    • (2008) Genes Dev , vol.22 , pp. 1159-1173
    • Dong, J.1    Jimi, E.2    Zhong, H.3    Hayden, M.S.4    Ghosh, S.5
  • 34
    • 0029664650 scopus 로고    scopus 로고
    • Role of CSB/p38/RK stress response kinase in LPS and cytokine signaling mechanisms
    • Lee J.C., and Young P.R. Role of CSB/p38/RK stress response kinase in LPS and cytokine signaling mechanisms. J Leukoc Biol 59 (1996) 152-157
    • (1996) J Leukoc Biol , vol.59 , pp. 152-157
    • Lee, J.C.1    Young, P.R.2
  • 35
    • 0031919215 scopus 로고    scopus 로고
    • Antioxidative and superoxide scavenging activities of retrochalcones in Glycyrrhiza inflata
    • Haraguchi H., Ishikawa H., Mizutani K., Tamura Y., and Kinoshita T. Antioxidative and superoxide scavenging activities of retrochalcones in Glycyrrhiza inflata. Bioorg Med Chem 6 (1998) 339-347
    • (1998) Bioorg Med Chem , vol.6 , pp. 339-347
    • Haraguchi, H.1    Ishikawa, H.2    Mizutani, K.3    Tamura, Y.4    Kinoshita, T.5
  • 36
    • 0027381266 scopus 로고
    • Licochalcone A, a novel antiparasitic agent with potent activity against human pathogenic protozoan species of Leishmania
    • Chen M., Christensen S.B., Blom J., Lemmich E., Nadelmann L., Fich K., et al. Licochalcone A, a novel antiparasitic agent with potent activity against human pathogenic protozoan species of Leishmania. Antimicrob Agents Chemother 37 (1993) 2550-2556
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 2550-2556
    • Chen, M.1    Christensen, S.B.2    Blom, J.3    Lemmich, E.4    Nadelmann, L.5    Fich, K.6
  • 37
  • 38
    • 0034636021 scopus 로고    scopus 로고
    • Glucocorticoids repress NF-kappaB-driven genes by disturbing the interaction of p65 with the basal transcription machinery, irrespective of coactivator levels in the cell
    • De Bosscher K., Vanden Berghe W., Vermeulen L., Plaisance S., Boone E., and Haegeman G. Glucocorticoids repress NF-kappaB-driven genes by disturbing the interaction of p65 with the basal transcription machinery, irrespective of coactivator levels in the cell. Proc Natl Acad Sci U S A 97 (2000) 3919-3924
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3919-3924
    • De Bosscher, K.1    Vanden Berghe, W.2    Vermeulen, L.3    Plaisance, S.4    Boone, E.5    Haegeman, G.6
  • 39
    • 0036143130 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticoid antiproliferative effects: antagonism of transcription factor activity by glucocorticoid receptor
    • Almawi W.Y., and Melemedjian O.K. Molecular mechanisms of glucocorticoid antiproliferative effects: antagonism of transcription factor activity by glucocorticoid receptor. J Leukoc Biol 71 (2002) 9-15
    • (2002) J Leukoc Biol , vol.71 , pp. 9-15
    • Almawi, W.Y.1    Melemedjian, O.K.2
  • 40
    • 41149091553 scopus 로고    scopus 로고
    • Isoliquiritigenin isolated from the roots of Glycyrrhiza uralensis inhibits LPS-induced iNOS and COX-2 expression via the attenuation of NF-kappaB in RAW 264.7 macrophages
    • Kim J.Y., Park S.J., Yun K.J., Cho Y.W., Park H.J., and Lee K.T. Isoliquiritigenin isolated from the roots of Glycyrrhiza uralensis inhibits LPS-induced iNOS and COX-2 expression via the attenuation of NF-kappaB in RAW 264.7 macrophages. Eur J Pharmacol 584 (2008) 175-184
    • (2008) Eur J Pharmacol , vol.584 , pp. 175-184
    • Kim, J.Y.1    Park, S.J.2    Yun, K.J.3    Cho, Y.W.4    Park, H.J.5    Lee, K.T.6
  • 41
    • 0000676538 scopus 로고    scopus 로고
    • Inhibition of eukaryote serine/threonine-specific protein kinases by piceatannol
    • Wang B.H., Lu Z.X., and Polya G.M. Inhibition of eukaryote serine/threonine-specific protein kinases by piceatannol. Planta Med 64 (1998) 195-199
    • (1998) Planta Med , vol.64 , pp. 195-199
    • Wang, B.H.1    Lu, Z.X.2    Polya, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.