메뉴 건너뛰기




Volumn 237, Issue 3, 2009, Pages 357-365

Zinc protoporphyrin inhibition of lipopolysaccharide-, lipoteichoic acid-, and peptidoglycan-induced nitric oxide production through stimulating iNOS protein ubiquitination

Author keywords

Heme oxygenase; Inducible nitric oxide synthase; Nitric oxide; Ubiquitination

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BOVINE SERUM ALBUMIN; FERRIC PROTOPORPHYRIN; HEME OXYGENASE 1; INDUCIBLE NITRIC OXIDE SYNTHASE; LACTACYSTIN; LIPOPOLYSACCHARIDE; LIPOTEICHOIC ACID; MITOGEN ACTIVATED PROTEIN KINASE; N(G) NITROARGININE METHYL ESTER; NITRIC OXIDE; PEPTIDOGLYCAN; PROTOPORPHYRIN; PROTOPORPHYRIN TIN; PROTOPORPHYRIN ZINC; SMALL INTERFERING RNA; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; ZINC CHLORIDE;

EID: 65749117197     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2009.04.009     Document Type: Article
Times cited : (18)

References (35)
  • 2
    • 38949110010 scopus 로고    scopus 로고
    • Negative feedback regulation of lipopolysaccharide-induced inducible nitric oxide synthase gene expression by heme oxygenase-1 induction in macrophages
    • Ashino T., Yamanaka R., Yamamoto M., Shimokawa H., Sekikawa K., Iwakura Y., Shioda S., Numazawa S., and Yoshida T. Negative feedback regulation of lipopolysaccharide-induced inducible nitric oxide synthase gene expression by heme oxygenase-1 induction in macrophages. Mol. Immunol. 45 (2008) 2106-2115
    • (2008) Mol. Immunol. , vol.45 , pp. 2106-2115
    • Ashino, T.1    Yamanaka, R.2    Yamamoto, M.3    Shimokawa, H.4    Sekikawa, K.5    Iwakura, Y.6    Shioda, S.7    Numazawa, S.8    Yoshida, T.9
  • 3
    • 0025819677 scopus 로고
    • Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species
    • Balla G., Vercellotti G.M., Muller-Eberhard U., Eaton J., and Jacob H.S. Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species. Lab. Invest. 64 (1991) 648-655
    • (1991) Lab. Invest. , vol.64 , pp. 648-655
    • Balla, G.1    Vercellotti, G.M.2    Muller-Eberhard, U.3    Eaton, J.4    Jacob, H.S.5
  • 6
    • 33750467637 scopus 로고    scopus 로고
    • Role of inducible nitric oxide synthase and NADPH oxidase in early control of Burkholderia pseudomallei infection in mice
    • Breitbach K., Klocke S., Tschernig T., van Rooijen N., Baumann U., and Steinmetz I. Role of inducible nitric oxide synthase and NADPH oxidase in early control of Burkholderia pseudomallei infection in mice. Infect. Immun. 74 (2006) 6300-6309
    • (2006) Infect. Immun. , vol.74 , pp. 6300-6309
    • Breitbach, K.1    Klocke, S.2    Tschernig, T.3    van Rooijen, N.4    Baumann, U.5    Steinmetz, I.6
  • 7
    • 23444456772 scopus 로고    scopus 로고
    • Regulation of immune responses by L-arginine metabolism
    • Bronte V., and Zanovello P. Regulation of immune responses by L-arginine metabolism. Nat. Rev. Immunol. 5 (2005) 641-654
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 641-654
    • Bronte, V.1    Zanovello, P.2
  • 8
    • 39749124150 scopus 로고    scopus 로고
    • Cytotoxic effects of metal protoporphyrins in glioblastoma cells: roles of albumin, reactive oxygen species, and heme oxygenase-1
    • Chow J.M., Huang G.C., Lin H.Y., Shen S.C., Yang L.Y., and Chen Y.C. Cytotoxic effects of metal protoporphyrins in glioblastoma cells: roles of albumin, reactive oxygen species, and heme oxygenase-1. Toxicol. Lett. 177 (2008) 97-107
    • (2008) Toxicol. Lett. , vol.177 , pp. 97-107
    • Chow, J.M.1    Huang, G.C.2    Lin, H.Y.3    Shen, S.C.4    Yang, L.Y.5    Chen, Y.C.6
  • 9
    • 0029561920 scopus 로고
    • Role for intracellular platelet-activating factor in the circulatory failure in a model of gram-positive shock
    • De Kimpe S.J., Thiemermann C., and Vane J.R. Role for intracellular platelet-activating factor in the circulatory failure in a model of gram-positive shock. Br. J. Pharmacol. 116 (1995) 3191-3198
    • (1995) Br. J. Pharmacol. , vol.116 , pp. 3191-3198
    • De Kimpe, S.J.1    Thiemermann, C.2    Vane, J.R.3
  • 10
    • 0036887571 scopus 로고    scopus 로고
    • Protective effect of HO-1 against oxidative stress in human hepatoma cell line (HepG2) is independent of telomerase enzyme activity
    • Ghattas M.H., Chuang L.T., Kappas A., and Abraham N.G. Protective effect of HO-1 against oxidative stress in human hepatoma cell line (HepG2) is independent of telomerase enzyme activity. Int. J. Biochem. Cell. Biol. 34 (2002) 1619-1628
    • (2002) Int. J. Biochem. Cell. Biol. , vol.34 , pp. 1619-1628
    • Ghattas, M.H.1    Chuang, L.T.2    Kappas, A.3    Abraham, N.G.4
  • 11
    • 42749088840 scopus 로고    scopus 로고
    • Carbon monoxide decreases the level of iNOS protein and active dimer in IL-1beta-stimulated hepatocytes
    • Kim H.S., Loughran P.A., and Billiar T.R. Carbon monoxide decreases the level of iNOS protein and active dimer in IL-1beta-stimulated hepatocytes. Nitric Oxide 18 (2008) 256-265
    • (2008) Nitric Oxide , vol.18 , pp. 256-265
    • Kim, H.S.1    Loughran, P.A.2    Billiar, T.R.3
  • 12
    • 0037126022 scopus 로고    scopus 로고
    • Ubiquitination of inducible nitric oxide synthase is required for its degradation
    • Kolodziejski P.J., Musial A., Koo J.S., and Eissa N.T. Ubiquitination of inducible nitric oxide synthase is required for its degradation. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 12315-12320
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12315-12320
    • Kolodziejski, P.J.1    Musial, A.2    Koo, J.S.3    Eissa, N.T.4
  • 13
    • 40849106315 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase and p38 mitogen-activated protein kinase mediate double-strand RNA-induced inducible nitric oxide synthase expression in microglial cells
    • Kong P.J., Lee H.J., Lee S.H., Kim S.Y., Lee S.N., Chun W.J., and Kim S.S. c-Jun N-terminal kinase and p38 mitogen-activated protein kinase mediate double-strand RNA-induced inducible nitric oxide synthase expression in microglial cells. Neurosci. Lett. 433 (2008) 215-218
    • (2008) Neurosci. Lett. , vol.433 , pp. 215-218
    • Kong, P.J.1    Lee, H.J.2    Lee, S.H.3    Kim, S.Y.4    Lee, S.N.5    Chun, W.J.6    Kim, S.S.7
  • 14
    • 0032710987 scopus 로고    scopus 로고
    • Zinc protoporphyrin: a metabolite with a mission
    • Review
    • Labbé R.F., Vreman H.J., and Stevenson D.K. Zinc protoporphyrin: a metabolite with a mission. Clin. Chem. 45 (1999) 2060-2072 Review
    • (1999) Clin. Chem. , vol.45 , pp. 2060-2072
    • Labbé, R.F.1    Vreman, H.J.2    Stevenson, D.K.3
  • 17
    • 0141888287 scopus 로고    scopus 로고
    • Ihibition of lipopolysaccharide-induced nitric oxide production by flavonoids in RAW264.7 macrophages involves heme oxygenase-1
    • Lin H.Y., Juan S.H., Shen S.C., Hsu F.L., and Chen Y.C. Ihibition of lipopolysaccharide-induced nitric oxide production by flavonoids in RAW264.7 macrophages involves heme oxygenase-1. Biochem. Pharmacol. 66 (2003) 1821-1832
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1821-1832
    • Lin, H.Y.1    Juan, S.H.2    Shen, S.C.3    Hsu, F.L.4    Chen, Y.C.5
  • 18
    • 11144263729 scopus 로고    scopus 로고
    • Anti-inflammatory effect of heme oxygenase 1: glycosylation and nitric oxide inhibition in macrophages
    • Lin H.Y., Shen S.C., and Chen Y.C. Anti-inflammatory effect of heme oxygenase 1: glycosylation and nitric oxide inhibition in macrophages. J. Cell. Physiol. 202 (2005) 579-590
    • (2005) J. Cell. Physiol. , vol.202 , pp. 579-590
    • Lin, H.Y.1    Shen, S.C.2    Chen, Y.C.3
  • 19
    • 48249113845 scopus 로고    scopus 로고
    • MAPK kinase kinase-1 is essential for cytokine-induced c-Jun NH2-terminal kinase and nuclear factor-kappaB activation in human pancreatic islet cells
    • Mokhtari D., Myers J.W., and Welsh N. MAPK kinase kinase-1 is essential for cytokine-induced c-Jun NH2-terminal kinase and nuclear factor-kappaB activation in human pancreatic islet cells. Diabetes 57 (2008) 1896-1904
    • (2008) Diabetes , vol.57 , pp. 1896-1904
    • Mokhtari, D.1    Myers, J.W.2    Welsh, N.3
  • 20
    • 0035968305 scopus 로고    scopus 로고
    • Inducible nitric-oxide synthase is regulated by the proteasome degradation pathway
    • Musial A., and Eissa N.T. Inducible nitric-oxide synthase is regulated by the proteasome degradation pathway. J. Biol. Chem. 276 (2001) 24268-24273
    • (2001) J. Biol. Chem. , vol.276 , pp. 24268-24273
    • Musial, A.1    Eissa, N.T.2
  • 22
    • 12144273503 scopus 로고    scopus 로고
    • Development of vascular biology over the past 10 years: heme oxygenase-1 in cardiovascular homeostasis
    • Ohta K., and Yachie A. Development of vascular biology over the past 10 years: heme oxygenase-1 in cardiovascular homeostasis. J. Endovasc. Ther. 11 Suppl 2 (2004) II140-II150
    • (2004) J. Endovasc. Ther. , vol.11 , Issue.SUPPL. 2
    • Ohta, K.1    Yachie, A.2
  • 23
    • 0032928798 scopus 로고    scopus 로고
    • Involvement of mitogen-activated protein kinase homologues in the regulation of lipopolysaccharidemediated induction of cyclo-oxygenase-2 but not nitric oxide synthase in RAW 264.7 macrophages
    • Paul A., Cuenda A., Bryant C.E., Murray J., Chilvers E.R., Cohen P., Gould G.W., and Plevin R. Involvement of mitogen-activated protein kinase homologues in the regulation of lipopolysaccharidemediated induction of cyclo-oxygenase-2 but not nitric oxide synthase in RAW 264.7 macrophages. Cell. Signal. 11 (1999) 491-497
    • (1999) Cell. Signal. , vol.11 , pp. 491-497
    • Paul, A.1    Cuenda, A.2    Bryant, C.E.3    Murray, J.4    Chilvers, E.R.5    Cohen, P.6    Gould, G.W.7    Plevin, R.8
  • 24
    • 0033842260 scopus 로고    scopus 로고
    • Influence of heme oxygenase inhibitors on the basal tissue enzymatic activity and smooth muscle relaxation of internal anal sphincter
    • Rattan S., and Chakder S. Influence of heme oxygenase inhibitors on the basal tissue enzymatic activity and smooth muscle relaxation of internal anal sphincter. J. Pharmacol. Exp. Ther. 294 (2000) 1009-1016
    • (2000) J. Pharmacol. Exp. Ther. , vol.294 , pp. 1009-1016
    • Rattan, S.1    Chakder, S.2
  • 25
    • 58149288675 scopus 로고    scopus 로고
    • Differential production of IL-23 and IL-12 by myeloid-derived dendritic cells in response to TLR agonists
    • Roses R.E., Xu S., Xu M., Koldovsky U., Koski G., and Czerniecki B.J. Differential production of IL-23 and IL-12 by myeloid-derived dendritic cells in response to TLR agonists. J. Immunol. 181 (2008) 5120-5127
    • (2008) J. Immunol. , vol.181 , pp. 5120-5127
    • Roses, R.E.1    Xu, S.2    Xu, M.3    Koldovsky, U.4    Koski, G.5    Czerniecki, B.J.6
  • 27
    • 0027406116 scopus 로고
    • Regulation of heme oxygenase and metallothionein gene expression by the heme analogs, cobalt-, and tin-protoporphyrin
    • Smith A., Alam J., Escriba P.V., and Morgan W.T. Regulation of heme oxygenase and metallothionein gene expression by the heme analogs, cobalt-, and tin-protoporphyrin. J. Biol. Chem. 268 (1993) 7365-7371
    • (1993) J. Biol. Chem. , vol.268 , pp. 7365-7371
    • Smith, A.1    Alam, J.2    Escriba, P.V.3    Morgan, W.T.4
  • 28
    • 49649119361 scopus 로고    scopus 로고
    • HO-1 and JAK-2/STAT-1 signals are involved in preferential inhibition of iNOS over COX-2 gene expression by newly synthesized tetrahydroisoquinoline alkaloid, CKD712, in cells activated with lipopolysacchride
    • Tsoyi K., Kim H.J., Shin J.S., Kim D.H., Cho H.J., Lee S.S., Ahn S.K., Yun-Choi H.S., Lee J.H., Seo H.G., and Chang K.C. HO-1 and JAK-2/STAT-1 signals are involved in preferential inhibition of iNOS over COX-2 gene expression by newly synthesized tetrahydroisoquinoline alkaloid, CKD712, in cells activated with lipopolysacchride. Cell. Signal. 20 (2008) 1839-1847
    • (2008) Cell. Signal. , vol.20 , pp. 1839-1847
    • Tsoyi, K.1    Kim, H.J.2    Shin, J.S.3    Kim, D.H.4    Cho, H.J.5    Lee, S.S.6    Ahn, S.K.7    Yun-Choi, H.S.8    Lee, J.H.9    Seo, H.G.10    Chang, K.C.11
  • 30
    • 24944568241 scopus 로고    scopus 로고
    • 6-(Methylsulfinyl)hexyl isothiocyanate suppresses inducible nitric oxide synthase expression through the inhibition of Janus kinase 2-mediated JNK pathway in lipopolysaccharide-activated murine macrophages
    • Uto T., Fujii M., and Hou D.X. 6-(Methylsulfinyl)hexyl isothiocyanate suppresses inducible nitric oxide synthase expression through the inhibition of Janus kinase 2-mediated JNK pathway in lipopolysaccharide-activated murine macrophages. Biochem. Pharmacol. 70 (2005) 1211-1221
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1211-1221
    • Uto, T.1    Fujii, M.2    Hou, D.X.3
  • 31
    • 0036883907 scopus 로고    scopus 로고
    • Blocking NO synthesis: how, where and why?
    • Vallance P., and Leiper J. Blocking NO synthesis: how, where and why?. Nat. Rev. Drug Discov. 1 (2002) 939-950
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 939-950
    • Vallance, P.1    Leiper, J.2
  • 32
    • 4043058702 scopus 로고    scopus 로고
    • Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats
    • Wang W.W., Smith D.L., and Zucker S.D. Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats. Hepatology 40 (2004) 424-433
    • (2004) Hepatology , vol.40 , pp. 424-433
    • Wang, W.W.1    Smith, D.L.2    Zucker, S.D.3
  • 34
    • 0035282719 scopus 로고    scopus 로고
    • Unique effects of zinc protoporphyrin on HO-1 induction and apoptosis
    • Yang G., Nguyen X., Ou J., Rekulapelli P., Stevenson D.K., and Dennery P.A. Unique effects of zinc protoporphyrin on HO-1 induction and apoptosis. Blood 97 (2001) 1306-1313
    • (2001) Blood , vol.97 , pp. 1306-1313
    • Yang, G.1    Nguyen, X.2    Ou, J.3    Rekulapelli, P.4    Stevenson, D.K.5    Dennery, P.A.6
  • 35
    • 43549109194 scopus 로고    scopus 로고
    • Anti-inflammatory activity of 4-methoxyhonokiol is a function of the inhibition of iNOS and COX-2 expression in RAW 264.7 macrophages via NF-kappaB, JNK and p38 MAPK inactivation
    • Zhou H.Y., Shin E.M., Guo L.Y., Youn U.J., Bae K., Kang S.S., Zou L.B., and Kim Y.S. Anti-inflammatory activity of 4-methoxyhonokiol is a function of the inhibition of iNOS and COX-2 expression in RAW 264.7 macrophages via NF-kappaB, JNK and p38 MAPK inactivation. Eur. J. Pharmacol. 586 (2008) 340-349
    • (2008) Eur. J. Pharmacol. , vol.586 , pp. 340-349
    • Zhou, H.Y.1    Shin, E.M.2    Guo, L.Y.3    Youn, U.J.4    Bae, K.5    Kang, S.S.6    Zou, L.B.7    Kim, Y.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.