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Volumn 142, Issue 5, 2007, Pages 587-595

CEL-I, an invertebrate N-acetylgalactosamine-specific C-type lectin, induces TNF-α and G-CSF production by mouse macrophage cell line RAW264.7 cells

Author keywords

C type lectin; Cucumaria echinata; Cytokines; Granulocyte colony stimulating factor; Macrophage cell line; Tumour necrosis factor

Indexed keywords

CARBOHYDRATE; FLUORESCEIN ISOTHIOCYANATE; GRANULOCYTE COLONY STIMULATING FACTOR; LECTIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; N ACETYLGALACTOSAMINE; PHYTOHEMAGGLUTININ; PROTEIN CEL I; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 38849180050     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm164     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 0015510673 scopus 로고
    • Lectins: Cell-agglutinating and sugar-specific proteins
    • Sharon, N. and Lis, H. (1972) Lectins: cell-agglutinating and sugar-specific proteins. Science 177, 949-959
    • (1972) Science , vol.177 , pp. 949-959
    • Sharon, N.1    Lis, H.2
  • 2
    • 0033952460 scopus 로고    scopus 로고
    • A subunit vaccine candidate region of the Entamoeba histolytica galactose-adherence lectin promotes interleukin-12 gene transcription and protein production in human macrophages
    • Campbell, D., Mann, B.J., and Chadee, K. (2000) A subunit vaccine candidate region of the Entamoeba histolytica galactose-adherence lectin promotes interleukin-12 gene transcription and protein production in human macrophages. Eur. J. Immunol. 30, 423-430
    • (2000) Eur. J. Immunol , vol.30 , pp. 423-430
    • Campbell, D.1    Mann, B.J.2    Chadee, K.3
  • 3
    • 0034618769 scopus 로고    scopus 로고
    • Activation of murine macrophage-like cells by granulocytin
    • Fujita, Y., Homman, K.J., and Natori, S. (2000) Activation of murine macrophage-like cells by granulocytin. Biochem. Biophys. Res. Comm. 275, 850-853
    • (2000) Biochem. Biophys. Res. Comm , vol.275 , pp. 850-853
    • Fujita, Y.1    Homman, K.J.2    Natori, S.3
  • 4
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity
    • Dodd, R.B. and Drickamer, K. (2001) Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity. Glycobiol. 11, 71R-79R
    • (2001) Glycobiol , vol.11
    • Dodd, R.B.1    Drickamer, K.2
  • 5
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: A historical introduction and overview
    • Kilpatrick, D.C. (2002) Animal lectins: a historical introduction and overview. Biochim. Biophys. Acta 1572, 187-197
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 187-197
    • Kilpatrick, D.C.1
  • 6
    • 0019320938 scopus 로고
    • Purification of lectin induced in the hemolymph of Sarcophaga peregrina larvae on injury
    • Komano, H., Mizuno, D., and Natori, S. (1980) Purification of lectin induced in the hemolymph of Sarcophaga peregrina larvae on injury. J. Biol. Chem. 255, 2919-2924
    • (1980) J. Biol. Chem , vol.255 , pp. 2919-2924
    • Komano, H.1    Mizuno, D.2    Natori, S.3
  • 8
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer, K. (1988) Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263, 9557-9560
    • (1988) J. Biol. Chem , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 10
    • 0023644774 scopus 로고
    • The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina
    • Giga, Y., Ikai, A., and Takahashi, K. (1987) The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina. J. Biol. Chem. 262, 6197-6203
    • (1987) J. Biol. Chem , vol.262 , pp. 6197-6203
    • Giga, Y.1    Ikai, A.2    Takahashi, K.3
  • 11
    • 0025370820 scopus 로고
    • The amino-acid sequences of multiple lectins of the acorn barnacle Megabalanus rosa and its homology with animal lectins
    • Muramoto, K. and Kamiya, H. (1990) The amino-acid sequences of multiple lectins of the acorn barnacle Megabalanus rosa and its homology with animal lectins. Biochim. Biophys. Acta 1039, 42-51
    • (1990) Biochim. Biophys. Acta , vol.1039 , pp. 42-51
    • Muramoto, K.1    Kamiya, H.2
  • 12
    • 0025058737 scopus 로고
    • A calcium-dependent galactose-binding lectin from the tunicate Polyandrocarpa misakiensis
    • Suzuki, T., Takagi, T., Furukohri, T., Kawamura, K., and Nakauchi, M. (1990) A calcium-dependent galactose-binding lectin from the tunicate Polyandrocarpa misakiensis. J. Biol. Chem. 265, 1274-1281
    • (1990) J. Biol. Chem , vol.265 , pp. 1274-1281
    • Suzuki, T.1    Takagi, T.2    Furukohri, T.3    Kawamura, K.4    Nakauchi, M.5
  • 13
    • 0028213875 scopus 로고
    • Amino acid sequence of a lectin from the sea cucumber, Stichopus japonicus, and its structural relationship to the C-type animal lectin family
    • Himeshima, T., Hatakeyama, T., and Yamasaki, N. (1994) Amino acid sequence of a lectin from the sea cucumber, Stichopus japonicus, and its structural relationship to the C-type animal lectin family. J. Biochem. 115, 689-692
    • (1994) J. Biochem , vol.115 , pp. 689-692
    • Himeshima, T.1    Hatakeyama, T.2    Yamasaki, N.3
  • 15
    • 0028967311 scopus 로고
    • Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane
    • Hatakeyama, T., Nagatomo, H., and Yamasaki, N. (1995) Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane. J. Biol. Chem. 270, 3560-3564
    • (1995) J. Biol. Chem , vol.270 , pp. 3560-3564
    • Hatakeyama, T.1    Nagatomo, H.2    Yamasaki, N.3
  • 16
    • 0029927152 scopus 로고    scopus 로고
    • Oligomerization of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata induced by the binding of carbohydrate ligands
    • Hatakeyama, T., Furukawa, M., Nagatomo, H., Yamasaki, N., and Mori, T. (1996) Oligomerization of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata induced by the binding of carbohydrate ligands. J. Biol. Chem. 271, 16915-16920
    • (1996) J. Biol. Chem , vol.271 , pp. 16915-16920
    • Hatakeyama, T.1    Furukawa, M.2    Nagatomo, H.3    Yamasaki, N.4    Mori, T.5
  • 17
    • 0030910331 scopus 로고    scopus 로고
    • Temperature-and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines
    • Oda, T., Tsuru, M., Hatakeyama, T., Nagatomo, H., Muramatsu, T., and Yamasaki, N. (1997) Temperature-and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines. J. Biochem. 121, 560-567
    • (1997) J. Biochem , vol.121 , pp. 560-567
    • Oda, T.1    Tsuru, M.2    Hatakeyama, T.3    Nagatomo, H.4    Muramatsu, T.5    Yamasaki, N.6
  • 18
    • 0036369409 scopus 로고    scopus 로고
    • Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-D-galactosamine-specific C-type lectin, CEL-I, from the Holothuroidea, Cucumaria echinata
    • Hatakeyama, T., Matsuo, N., Shiba, K., Nishinohara, S., Yamasaki, N., Sugawara, H., and Aoyagi, H. (2002) Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-D-galactosamine-specific C-type lectin, CEL-I, from the Holothuroidea, Cucumaria echinata. Biosci. Biotechnol. Biochem. 66, 157-163
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 157-163
    • Hatakeyama, T.1    Matsuo, N.2    Shiba, K.3    Nishinohara, S.4    Yamasaki, N.5    Sugawara, H.6    Aoyagi, H.7
  • 19
    • 1642463060 scopus 로고    scopus 로고
    • Characterization of recombinant CEL-I, a GalNAc-specific C-type lectin, expressed in Escherichia coli using an artificial synthetic gene
    • Hatakeyama, T., Shiba, K., Matsuo, N., Fujimoto, T., Fujimoto, T., Oda, T., Sugawara, H., and Aoyagi, H. (2004) Characterization of recombinant CEL-I, a GalNAc-specific C-type lectin, expressed in Escherichia coli using an artificial synthetic gene. J. Biochem. 135, 101-107
    • (2004) J. Biochem , vol.135 , pp. 101-107
    • Hatakeyama, T.1    Shiba, K.2    Matsuo, N.3    Fujimoto, T.4    Fujimoto, T.5    Oda, T.6    Sugawara, H.7    Aoyagi, H.8
  • 21
    • 0001867122 scopus 로고
    • Surface carbohydrate alterations of mutant mammalian cells selected for resistance to plant lectins
    • Lennarz, W.J, ed, pp, Plenum Press, New York
    • Stanley, P. (1981) Surface carbohydrate alterations of mutant mammalian cells selected for resistance to plant lectins. in The Biochemistry of Glycoproteins and Proteoglycans (Lennarz, W.J., ed.), pp. 161-190 Plenum Press, New York
    • (1981) The Biochemistry of Glycoproteins and Proteoglycans , pp. 161-190
    • Stanley, P.1
  • 23
    • 15744374487 scopus 로고    scopus 로고
    • The synergistic effect of phytohemagglutinin and interferon-γ on the expression of tumor necrosis factor-a from RAW264.7 cells
    • Chang, S.H., Mun, S.H., Ko, N.Y., Lee, J.H., Jun, M.H., Seo, J.Y., Kim, Y.M., Choi, W.S., and Her, E. (2005) The synergistic effect of phytohemagglutinin and interferon-γ on the expression of tumor necrosis factor-a from RAW264.7 cells. Immunol. Letters 98, 137-143
    • (2005) Immunol. Letters , vol.98 , pp. 137-143
    • Chang, S.H.1    Mun, S.H.2    Ko, N.Y.3    Lee, J.H.4    Jun, M.H.5    Seo, J.Y.6    Kim, Y.M.7    Choi, W.S.8    Her, E.9
  • 24
    • 0030296710 scopus 로고    scopus 로고
    • Early calcium signaling and calcium requirements for the IL-2 receptor expression and IL-12 production in stimulated lymphocytes
    • Komada, H., Nakabayashi, H., Hara, M., and Izutsu, K. (1996) Early calcium signaling and calcium requirements for the IL-2 receptor expression and IL-12 production in stimulated lymphocytes. Cellular Immunol. 173, 215-220
    • (1996) Cellular Immunol , vol.173 , pp. 215-220
    • Komada, H.1    Nakabayashi, H.2    Hara, M.3    Izutsu, K.4
  • 25
    • 33748761969 scopus 로고    scopus 로고
    • Regulation of lipopolysaccharide-induced interleukin-12 production by activation of repressor element GA-12 through hyperactivation of the ERK pathway
    • Sato, S., Matsuura, M., and Hirai, Y. (2006) Regulation of lipopolysaccharide-induced interleukin-12 production by activation of repressor element GA-12 through hyperactivation of the ERK pathway. Clin. Vacctine Immunol. 13, 876-883
    • (2006) Clin. Vacctine Immunol , vol.13 , pp. 876-883
    • Sato, S.1    Matsuura, M.2    Hirai, Y.3
  • 26
    • 0028535921 scopus 로고
    • Lipopolysaccharide signals activation of tumor necrosis factor biosynthesis through the Ras/Raf-1/MEK/MAPK pathway
    • Geppert, T.D., Whitehurst, P.T., and Beutler, B. (1994) Lipopolysaccharide signals activation of tumor necrosis factor biosynthesis through the Ras/Raf-1/MEK/MAPK pathway. Mol. Med. 1, 93-103
    • (1994) Mol. Med , vol.1 , pp. 93-103
    • Geppert, T.D.1    Whitehurst, P.T.2    Beutler, B.3
  • 27
    • 33846530025 scopus 로고    scopus 로고
    • Induction of multiple cytokine secretion from RAW264.7 cells by alginate oligosaccharides
    • Yamamoto, Y., Kurachi, M., Yamaguchi, K., and Oda, T. (2007) Induction of multiple cytokine secretion from RAW264.7 cells by alginate oligosaccharides. Biosci. Biotechnol. Biochem. 71, 238-241
    • (2007) Biosci. Biotechnol. Biochem , vol.71 , pp. 238-241
    • Yamamoto, Y.1    Kurachi, M.2    Yamaguchi, K.3    Oda, T.4
  • 28
    • 23644436849 scopus 로고    scopus 로고
    • Structure-activity relationship of alginate oligosaccharides in the induction of cytokine production from RAW264.7 cells
    • Iwamoto, M., Kurachi, M., Nakashima, T., Kim, D., Yamaguchi, K., Oda, T., Iwamoto, Y., and Muramatsu, T. (2005) Structure-activity relationship of alginate oligosaccharides in the induction of cytokine production from RAW264.7 cells. FEBS Letters 579, 4423-4429
    • (2005) FEBS Letters , vol.579 , pp. 4423-4429
    • Iwamoto, M.1    Kurachi, M.2    Nakashima, T.3    Kim, D.4    Yamaguchi, K.5    Oda, T.6    Iwamoto, Y.7    Muramatsu, T.8
  • 29
    • 4944244272 scopus 로고    scopus 로고
    • Immunomodulatory role of native and heat denatured agglutinin from Abrus precatorius
    • Tripathi, T. and Maiti, T.K. (2005) Immunomodulatory role of native and heat denatured agglutinin from Abrus precatorius. Inter. J. Bichem. Cell Biol. 37, 451-462
    • (2005) Inter. J. Bichem. Cell Biol , vol.37 , pp. 451-462
    • Tripathi, T.1    Maiti, T.K.2
  • 30
    • 0037333373 scopus 로고    scopus 로고
    • Stimulation of murine macrophages by native and heat denatured lectin from Abrus precatorius
    • Tripathi, T. and Maiti, T.K. (2003) Stimulation of murine macrophages by native and heat denatured lectin from Abrus precatorius. Inter. Immunopharmacol. 3, 233-244
    • (2003) Inter. Immunopharmacol , vol.3 , pp. 233-244
    • Tripathi, T.1    Maiti, T.K.2
  • 31
    • 1542358177 scopus 로고    scopus 로고
    • Induction of cytokines by toxins that have an identical RNA N-glycosidase activity: Shiga toxin, ricin, and modeccin
    • Yamasaki, C., Nishikawa, K., Zeng, X.T., Katayama, Y., Natori, Y., Komatsu, N., Oda, T., and Natori, Y. (2004) Induction of cytokines by toxins that have an identical RNA N-glycosidase activity: Shiga toxin, ricin, and modeccin. Biochim. Biophys. Acta 1671, 44-50
    • (2004) Biochim. Biophys. Acta , vol.1671 , pp. 44-50
    • Yamasaki, C.1    Nishikawa, K.2    Zeng, X.T.3    Katayama, Y.4    Natori, Y.5    Komatsu, N.6    Oda, T.7    Natori, Y.8
  • 32
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., Yuan, L.C., Bonifacino, J.S., and Klausner, R.D. (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56, 801-813
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 33
    • 0025975785 scopus 로고
    • Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin, and Pseudomonas toxin
    • Yoshida, T., Chen, C., Zhang, M., and Wu, H.C. (1991) Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin, and Pseudomonas toxin. Exp. Cell Res. 192, 389-395
    • (1991) Exp. Cell Res , vol.192 , pp. 389-395
    • Yoshida, T.1    Chen, C.2    Zhang, M.3    Wu, H.C.4
  • 34
    • 0020265159 scopus 로고
    • Entry of the toxin protein abrin, modeccin, ricin and diphtheria toxin into cells. II. Effect of pH, metabolic inhibitors and ionophores and evidence for penetration from endocytic vesicles
    • Sandvig, K. and Olsnes, S. (1982) Entry of the toxin protein abrin, modeccin, ricin and diphtheria toxin into cells. II. Effect of pH, metabolic inhibitors and ionophores and evidence for penetration from endocytic vesicles. J. Biol. Chem. 257, 7504-7513
    • (1982) J. Biol. Chem , vol.257 , pp. 7504-7513
    • Sandvig, K.1    Olsnes, S.2
  • 35
    • 0028049994 scopus 로고
    • Secretion of TNF from a rat mast cell line is a brefeldin A-sensitive and a calcium/protein kinase C-regulated process
    • Baumgartner, R.A., Yamada, K., Deramo, V.A., and Beaven, M.A. (1994) Secretion of TNF from a rat mast cell line is a brefeldin A-sensitive and a calcium/protein kinase C-regulated process. J. Immunol. 153, 2609
    • (1994) J. Immunol , vol.153 , pp. 2609
    • Baumgartner, R.A.1    Yamada, K.2    Deramo, V.A.3    Beaven, M.A.4
  • 36
    • 2942629605 scopus 로고    scopus 로고
    • Lebectin, a novel C-type lectin from Macrovipera lebetina venom, inhibits integrin-mediated adhesion, migration and invasion of human tumour cells
    • Sarry, S., Berther, V., Galvete, J.J., Secchi, J., Marvaldi, J., Ayeb, M.E., Marrakchi, N., and Luis, J. (2004) Lebectin, a novel C-type lectin from Macrovipera lebetina venom, inhibits integrin-mediated adhesion, migration and invasion of human tumour cells. Lab. Invest. 84, 573-581
    • (2004) Lab. Invest , vol.84 , pp. 573-581
    • Sarry, S.1    Berther, V.2    Galvete, J.J.3    Secchi, J.4    Marvaldi, J.5    Ayeb, M.E.6    Marrakchi, N.7    Luis, J.8
  • 37
    • 0032787349 scopus 로고    scopus 로고
    • The effect of a lectin from the venom of the snake, Bothrops jararacussu, on tumor cell proliferation
    • Pereira-Bittencout, M., Carvalho, D.D., Gagliardi, A.R., and Collins, D.C. (1999) The effect of a lectin from the venom of the snake, Bothrops jararacussu, on tumor cell proliferation. Anticancer Res. 19, 4023-4025
    • (1999) Anticancer Res , vol.19 , pp. 4023-4025
    • Pereira-Bittencout, M.1    Carvalho, D.D.2    Gagliardi, A.R.3    Collins, D.C.4
  • 38
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood, J. and Cheresh, D. (2002) Role of integrins in cell invasion and migration. Nat. Rev. Cancer 2, 91-100
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.1    Cheresh, D.2
  • 40
    • 34250808941 scopus 로고    scopus 로고
    • Involvement of tyrosine kinase and MAP kinase in the production of TNF-α and IL-1β by macrophage in vitro on treatment with phytohemagglutinin
    • Kesherwani, V. and Sodhi, A. (2007) Involvement of tyrosine kinase and MAP kinase in the production of TNF-α and IL-1β by macrophage in vitro on treatment with phytohemagglutinin. J. Interferon Cyto. Res. 27, 497-505
    • (2007) J. Interferon Cyto. Res , vol.27 , pp. 497-505
    • Kesherwani, V.1    Sodhi, A.2


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