메뉴 건너뛰기




Volumn 16, Issue 4, 2010, Pages 265-272

Enhanced induction of a histamine-forming enzyme, histidine decarboxylase, in mice primed with NOD1 or NOD2 ligand in response to various Toll-like receptor agonists

Author keywords

histamine; lipid A; NOD1; NOD2; Toll like receptors

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; CASPASE RECRUITMENT DOMAIN PROTEIN 4; GLUDAPCIN; HEPTANOYL GAMMA DEXTRO GLUTAMYL 2,6 DIAMINOPIMELOYL DEXTRO ALANINE; HISTIDINE DECARBOXYLASE; LIPID A; MURAMYL DIPEPTIDE; POLYINOSINIC POLYCYTIDYLIC ACID; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 1; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 6; TOLL LIKE RECEPTOR AGONIST;

EID: 77955246366     PISSN: 17534259     EISSN: 17534267     Source Type: Journal    
DOI: 10.1177/1753425909341070     Document Type: Article
Times cited : (13)

References (26)
  • 2
    • 0038615855 scopus 로고    scopus 로고
    • Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan
    • Girardin SE, Boneca IG, Carneiro Lam et al. Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science 2003 ; 300: 1584-1587.
    • (2003) Science , vol.300 , pp. 1584-1587
    • Girardin, S.E.1    Boneca, I.G.2    Lam, C.3
  • 3
    • 0038824980 scopus 로고    scopus 로고
    • An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
    • Chamaillard M., Hashimoto M., Horie Y. et al. An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nat Immunol 2003 ; 4: 702-707.
    • (2003) Nat Immunol , vol.4 , pp. 702-707
    • Chamaillard, M.1    Hashimoto, M.2    Horie, Y.3
  • 4
    • 0037458665 scopus 로고    scopus 로고
    • Host recognition of bacterial muramyl dipeptide mediated through NOD2
    • Inohara N., Ogura Y., Fontalba A. et al. Host recognition of bacterial muramyl dipeptide mediated through NOD2. J Biol Chem 2003 ; 278: 5509-5512.
    • (2003) J Biol Chem , vol.278 , pp. 5509-5512
    • Inohara, N.1    Ogura, Y.2    Fontalba, A.3
  • 5
    • 0012722659 scopus 로고    scopus 로고
    • Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection
    • Girardin SE, Boneca IG, Viala J. et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J Biol Chem 2003 ; 278: 8869-8872.
    • (2003) J Biol Chem , vol.278 , pp. 8869-8872
    • Girardin, S.E.1    Boneca, I.G.2    Viala, J.3
  • 6
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira S., Takeda K. Toll-like receptor signalling. Nat Rev Immunol 2004 ; 4: 499-511.
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 7
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S., Uematsu S., Takeuchi O. Pathogen recognition and innate immunity. Cell 2006 ; 124: 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 8
    • 0034922923 scopus 로고    scopus 로고
    • Discrimination of bacterial lipoproteins by Toll-like receptor 6
    • Takeuchi O., Kawai T., Mühlradt PF et al. Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int Immunol 2001 ; 13: 933-940.
    • (2001) Int Immunol , vol.13 , pp. 933-940
    • Takeuchi, O.1    Kawai, T.2    Mühlradt, P.F.3
  • 9
    • 0036570698 scopus 로고    scopus 로고
    • Trends in histamine research: New functions during immune responses and hematopoiesis
    • Schneider E., Rolli-Derkinderen M., Arock M., Dy M. Trends in histamine research: new functions during immune responses and hematopoiesis. Trends Immunol 2002 ; 23: 255-263.
    • (2002) Trends Immunol , vol.23 , pp. 255-263
    • Schneider, E.1    Rolli-Derkinderen, M.2    Arock, M.3    Dy, M.4
  • 10
    • 0024563522 scopus 로고
    • Induction of histidine and ornithine decarboxylase activities in mouse tissues by recombinant interleukin-1 and tumor necrosis factor
    • Endo Y. Induction of histidine and ornithine decarboxylase activities in mouse tissues by recombinant interleukin-1 and tumor necrosis factor. Biochem Pharmacol 1989 ; 38: 1287-1292.
    • (1989) Biochem Pharmacol , vol.38 , pp. 1287-1292
    • Endo, Y.1
  • 11
    • 0026717380 scopus 로고
    • GM-CSF and G-CSF stimulate the synthesis of histamine and putrescine in the hematopoietic organs in vivo
    • Endo Y., Kikuchi T., Takeda Y., Nitta Y., Rikiishi H., Kumagai K. GM-CSF and G-CSF stimulate the synthesis of histamine and putrescine in the hematopoietic organs in vivo. Immunol Lett 1992 ; 33: 9-14.
    • (1992) Immunol Lett , vol.33 , pp. 9-14
    • Endo, Y.1    Kikuchi, T.2    Takeda, Y.3    Nitta, Y.4    Rikiishi, H.5    Kumagai, K.6
  • 12
    • 4344698401 scopus 로고    scopus 로고
    • Histamine production via mast cell-independent induction of histidine decarboxylase in response to lipopolysaccharide and interleukin-1
    • Wu X., Yoshida A., Sasano T., Iwakura Y., Endo Y. Histamine production via mast cell-independent induction of histidine decarboxylase in response to lipopolysaccharide and interleukin-1. Int Immunopharmacol 2004 ; 4: 513-520.
    • (2004) Int Immunopharmacol , vol.4 , pp. 513-520
    • Wu, X.1    Yoshida, A.2    Sasano, T.3    Iwakura, Y.4    Endo, Y.5
  • 13
    • 0028952433 scopus 로고
    • Effects of macrophage depletion on the induction of histidine decarboxylase by lipopolysaccharide, interleukin 1 and tumour necrosis factor
    • Endo Y., Nakamura M., Nitta Y., Kumagai K. Effects of macrophage depletion on the induction of histidine decarboxylase by lipopolysaccharide, interleukin 1 and tumour necrosis factor. Br J Pharmacol 1995 ; 114: 187-193.
    • (1995) Br J Pharmacol , vol.114 , pp. 187-193
    • Endo, Y.1    Nakamura, M.2    Nitta, Y.3    Kumagai, K.4
  • 14
    • 0025176722 scopus 로고
    • Priming effect of muramyl peptides for induction by lipopolysaccharide of tumor necrosis factor production in mice
    • Parant M., Parant F., Vinit M. -A, Jupin C., Noso Y., Chedid L. Priming effect of muramyl peptides for induction by lipopolysaccharide of tumor necrosis factor production in mice. J Leukoc Biol 1990 ; 47: 164-169.
    • (1990) J Leukoc Biol , vol.47 , pp. 164-169
    • Parant, M.1    Parant, F.2    Vinit, M.3    Jupin, C.4    Noso, Y.5    Chedid, L.6
  • 15
    • 0036453023 scopus 로고    scopus 로고
    • Enhancement of endotoxin activity by muramyldipeptide
    • Takada H., Yokoyama S., Yang S. Enhancement of endotoxin activity by muramyldipeptide. J Endotoxin Res 2002 ; 8: 337-342.
    • (2002) J Endotoxin Res , vol.8 , pp. 337-342
    • Takada, H.1    Yokoyama, S.2    Yang, S.3
  • 16
    • 33750557881 scopus 로고    scopus 로고
    • Enhancement of TLR-mediated innate immune responses by peptidoglycans through NOD signaling
    • Takada H., Uehara A. Enhancement of TLR-mediated innate immune responses by peptidoglycans through NOD signaling. Curr Pharm Design 2006 ; 12: 4163-4172.
    • (2006) Curr Pharm Design , vol.12 , pp. 4163-4172
    • Takada, H.1    Uehara, A.2
  • 17
    • 0034548225 scopus 로고    scopus 로고
    • The N-terminal lipopeptide of a 44-kDa membrane-bound lipoprotein of Mycoplasma salivarium is responsible for the expression of intercellular adhesion molecule-1 on the cell surface of normal human gingival fibroblasts
    • Shibata K., Hasebe A., Into T., Yamada M., Watanabe T. The N-terminal lipopeptide of a 44-kDa membrane-bound lipoprotein of Mycoplasma salivarium is responsible for the expression of intercellular adhesion molecule-1 on the cell surface of normal human gingival fibroblasts. J Immunol 2000 ; 165: 6538-6544.
    • (2000) J Immunol , vol.165 , pp. 6538-6544
    • Shibata, K.1    Hasebe, A.2    Into, T.3    Yamada, M.4    Watanabe, T.5
  • 18
    • 4243643363 scopus 로고
    • The immunomodulatory activities of acylpeptides
    • Azuma I, Jolles G., (eds) Berlin: Springer
    • Goto T., Aoki H. The immunomodulatory activities of acylpeptides. In: Azuma I, Jolles G., (eds) Immunostimulants: Now and Tomorrow. Berlin: Springer, 1987 ; 99-108.
    • (1987) Immunostimulants: Now and Tomorrow , pp. 99-108
    • Goto, T.1    Aoki, H.2
  • 19
    • 0032102947 scopus 로고    scopus 로고
    • Induction of histidine decarboxylase in skeletal muscle in mice by electrical stimulation, prolonged walking and interleukin-1
    • Endo Y., Tabata T., Kuroda H., Tadano T., Matsushima K., Watanabe M. Induction of histidine decarboxylase in skeletal muscle in mice by electrical stimulation, prolonged walking and interleukin-1. J Physiol 1998 ; 509: 587-598.
    • (1998) J Physiol , vol.509 , pp. 587-598
    • Endo, Y.1    Tabata, T.2    Kuroda, H.3    Tadano, T.4    Matsushima, K.5    Watanabe, M.6
  • 20
    • 0033870717 scopus 로고    scopus 로고
    • Elevation of histidine decarboxylase activity in the mandible of mice by Prevotella intermedia lipopolysaccharide and its augmentation by an aminobisphosphonate
    • Funayama H., Mayanagi H., Takada H., Endo Y. Elevation of histidine decarboxylase activity in the mandible of mice by Prevotella intermedia lipopolysaccharide and its augmentation by an aminobisphosphonate. Arch Oral Biol 2000 ; 45: 787-795.
    • (2000) Arch Oral Biol , vol.45 , pp. 787-795
    • Funayama, H.1    Mayanagi, H.2    Takada, H.3    Endo, Y.4
  • 21
    • 0023108997 scopus 로고
    • Enhancement of endotoxin lethality and generation of anaphylactoid reactions by lipopolysaccharides in muramyl-dipeptide-treated mice
    • Takada H., Galanos C. Enhancement of endotoxin lethality and generation of anaphylactoid reactions by lipopolysaccharides in muramyl-dipeptide-treated mice. Infect Immun 1987 ; 55: 409-413.
    • (1987) Infect Immun , vol.55 , pp. 409-413
    • Takada, H.1    Galanos, C.2
  • 23
    • 0000675671 scopus 로고
    • Muramyl dipeptide and derivatives
    • Stewart-Tull DES., ed. Chichester, UK: John Wiley
    • Takada H., Kotani S. Muramyl dipeptide and derivatives. In: Stewart-Tull DES., ed. The Theory and Practical Application of Adjuvants. Chichester, UK: John Wiley, 1995 ; 171-202.
    • (1995) The Theory and Practical Application of Adjuvants , pp. 171-202
    • Takada, H.1    Kotani, S.2
  • 24
    • 12444259829 scopus 로고    scopus 로고
    • Muramyldipeptide and diaminopimelic acid-containing desmuramylpeptides in combination with chemically synthesized Toll-like receptor agonists synergistically induced production of interleukin-8 in a NOD2- and NOD1-dependent manner, respectively, in human monocytic cells in culture
    • Uehara A., Yang S., Fujimoto Y. et al. Muramyldipeptide and diaminopimelic acid-containing desmuramylpeptides in combination with chemically synthesized Toll-like receptor agonists synergistically induced production of interleukin-8 in a NOD2- and NOD1-dependent manner, respectively, in human monocytic cells in culture. Cell Microbiol 2005 ; 7: 53-61.
    • (2005) Cell Microbiol , vol.7 , pp. 53-61
    • Uehara, A.1    Yang, S.2    Fujimoto, Y.3
  • 25
    • 0035078190 scopus 로고    scopus 로고
    • Synergistic effect of muramyldipeptide with lipopolysaccharide or lipoteichoic acid to induce inflammatory cytokines in human monocytic cells in culture
    • Yang S., Tamai R., Akashi S. et al. Synergistic effect of muramyldipeptide with lipopolysaccharide or lipoteichoic acid to induce inflammatory cytokines in human monocytic cells in culture. Infect Immun 2001 ; 69: 2045-2053.
    • (2001) Infect Immun , vol.69 , pp. 2045-2053
    • Yang, S.1    Tamai, R.2    Akashi, S.3
  • 26
    • 33846936219 scopus 로고    scopus 로고
    • RICK/RIP2 mediates innate immune responses induced through Nod1 and Nod2 but not TLRs
    • Park J-H., Kim Y-G., McDonald C. et al. RICK/RIP2 mediates innate immune responses induced through Nod1 and Nod2 but not TLRs. J Immunol 2007 ; 178: 2380-2386.
    • (2007) J Immunol , vol.178 , pp. 2380-2386
    • Park, J.-H.1    Kim, Y.-G.2    McDonald, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.