메뉴 건너뛰기




Volumn 60, Issue 1, 2012, Pages 162-170

Fibronectin inhibits cytokine production induced by CpG DNA in macrophages without direct binding to DNA

Author keywords

CpG DNA; DNA binding domain; Fibronectin; Inflammatory cytokine; Macrophages

Indexed keywords

BOVINE SERUM ALBUMIN; COLLAGEN; CPG OLIGODEOXYNUCLEOTIDE; DIVALENT CATION; FIBRONECTIN; IMIQUIMOD; LAMININ; LIPOPOLYSACCHARIDE; PLASMID DNA; POLYINOSINIC POLYCYTIDYLIC ACID; TOLL LIKE RECEPTOR 9; TUMOR NECROSIS FACTOR ALPHA;

EID: 84865439661     PISSN: 10434666     EISSN: 10960023     Source Type: Journal    
DOI: 10.1016/j.cyto.2012.06.237     Document Type: Article
Times cited : (3)

References (41)
  • 2
    • 85001433916 scopus 로고
    • Fibronectin: current concepts of its structure and functions
    • Ruoslahti E., Engvall E., Hayman E.G. Fibronectin: current concepts of its structure and functions. Collagen Rel Res 1981, 1:95-128.
    • (1981) Collagen Rel Res , vol.1 , pp. 95-128
    • Ruoslahti, E.1    Engvall, E.2    Hayman, E.G.3
  • 3
    • 0025744802 scopus 로고
    • Fibronectin: from gene to protein
    • Schwarzbauer J.E. Fibronectin: from gene to protein. Curr Opin Cell Biol 1991, 3:786-791.
    • (1991) Curr Opin Cell Biol , vol.3 , pp. 786-791
    • Schwarzbauer, J.E.1
  • 4
    • 0026728514 scopus 로고
    • Activated T lymphocytes and macrophages secrete fibronectin which strongly supports cell adhesion
    • Hershkoviz R., Alon R., Gilat D., Lider O. Activated T lymphocytes and macrophages secrete fibronectin which strongly supports cell adhesion. Cell Immunol 1992, 141:352-361.
    • (1992) Cell Immunol , vol.141 , pp. 352-361
    • Hershkoviz, R.1    Alon, R.2    Gilat, D.3    Lider, O.4
  • 7
    • 0024459352 scopus 로고
    • Plasma fibronectin synthesis in normal and injured humans as determined by stable isotope incorporation
    • Thompson C., Blumenstock F.A., Saba T.M., Feustel P.J., Kaplan J.E., Fortune J.B., et al. Plasma fibronectin synthesis in normal and injured humans as determined by stable isotope incorporation. J Clin Invest. 1989, 84:1226-1235.
    • (1989) J Clin Invest. , vol.84 , pp. 1226-1235
    • Thompson, C.1    Blumenstock, F.A.2    Saba, T.M.3    Feustel, P.J.4    Kaplan, J.E.5    Fortune, J.B.6
  • 8
    • 33845575428 scopus 로고    scopus 로고
    • Monocyte macrophage differentiation in vitro: fibronectin-dependent upregulation of certain macrophage-specific activities
    • Sudhakaran P.R., Radhika A., Jacob S.S. Monocyte macrophage differentiation in vitro: fibronectin-dependent upregulation of certain macrophage-specific activities. Glycoconjugate J 2007, 24:49-55.
    • (2007) Glycoconjugate J , vol.24 , pp. 49-55
    • Sudhakaran, P.R.1    Radhika, A.2    Jacob, S.S.3
  • 9
    • 30944431723 scopus 로고    scopus 로고
    • Soluble fibronectin induces chemokine gene expression in renal tubular epithelial cells
    • Ren L., Blanchette J.B., White L.R., Clark S.A., Heffner D.J., Tibbles L.A., et al. Soluble fibronectin induces chemokine gene expression in renal tubular epithelial cells. Kidney Int. 2005, 68:2111-2120.
    • (2005) Kidney Int. , vol.68 , pp. 2111-2120
    • Ren, L.1    Blanchette, J.B.2    White, L.R.3    Clark, S.A.4    Heffner, D.J.5    Tibbles, L.A.6
  • 11
    • 0021913546 scopus 로고
    • Primary structure of a glycosylated DNA-binding domain in human plasma fibronectin
    • Pande H., Calaycay J., Hawke D., Ben-Avram C.M., Shively J.E. Primary structure of a glycosylated DNA-binding domain in human plasma fibronectin. J Biol Chem 1985, 260:2301-2306.
    • (1985) J Biol Chem , vol.260 , pp. 2301-2306
    • Pande, H.1    Calaycay, J.2    Hawke, D.3    Ben-Avram, C.M.4    Shively, J.E.5
  • 12
    • 0019775179 scopus 로고
    • Differences in domain structures between plasma and cellular fibronectins
    • Hayashi M., Yamada K.M. Differences in domain structures between plasma and cellular fibronectins. J Biol Chem 1981, 256:11292-11300.
    • (1981) J Biol Chem , vol.256 , pp. 11292-11300
    • Hayashi, M.1    Yamada, K.M.2
  • 13
  • 14
    • 0022414405 scopus 로고
    • Primary structure of a DNA- and heparin-binding domain (Domain III) in human plasma fibronectin
    • Calaycay J., Pande H., Lee T., Borsi L., Siri A., Shively J.E., et al. Primary structure of a DNA- and heparin-binding domain (Domain III) in human plasma fibronectin. J Biol Chem 1985, 260:12136-12141.
    • (1985) J Biol Chem , vol.260 , pp. 12136-12141
    • Calaycay, J.1    Pande, H.2    Lee, T.3    Borsi, L.4    Siri, A.5    Shively, J.E.6
  • 15
    • 0020321677 scopus 로고
    • Divalent cation modulation of fibronectin binding to heparin and to DNA
    • Hayashi M., Yamada K.M. Divalent cation modulation of fibronectin binding to heparin and to DNA. J Biol Chem 1982, 257:5263-5267.
    • (1982) J Biol Chem , vol.257 , pp. 5263-5267
    • Hayashi, M.1    Yamada, K.M.2
  • 18
    • 0036318851 scopus 로고    scopus 로고
    • Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments
    • Ahmad-Nejad P., Hacker H., Rutz M., Bauer S., Vabulas R.M., Wagner H. Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments. Eur J Immunol 2002, 32:1958-1968.
    • (2002) Eur J Immunol , vol.32 , pp. 1958-1968
    • Ahmad-Nejad, P.1    Hacker, H.2    Rutz, M.3    Bauer, S.4    Vabulas, R.M.5    Wagner, H.6
  • 20
    • 1642388358 scopus 로고    scopus 로고
    • Restricted cytokine production from mouse peritoneal macrophages in culture in spite of extensive uptake of plasmid DNA
    • Yasuda K., Kawano H., Yamane I., Ogawa Y., Yoshinaga T., Nishikawa M., et al. Restricted cytokine production from mouse peritoneal macrophages in culture in spite of extensive uptake of plasmid DNA. Immunology 2004, 111:282-290.
    • (2004) Immunology , vol.111 , pp. 282-290
    • Yasuda, K.1    Kawano, H.2    Yamane, I.3    Ogawa, Y.4    Yoshinaga, T.5    Nishikawa, M.6
  • 21
    • 33846936329 scopus 로고    scopus 로고
    • DNA and its cationic lipid complexes induce CpG motif-dependent activation of murine dendritic cells
    • Yoshinaga T., Yasuda K., Ogawa Y., Nishikawa M., Takakura Y. DNA and its cationic lipid complexes induce CpG motif-dependent activation of murine dendritic cells. Immunology 2007, 120:295-302.
    • (2007) Immunology , vol.120 , pp. 295-302
    • Yoshinaga, T.1    Yasuda, K.2    Ogawa, Y.3    Nishikawa, M.4    Takakura, Y.5
  • 22
    • 55749107627 scopus 로고    scopus 로고
    • Cellular activation by plasmid DNA in various macrophages in primary culture
    • Yoshida H., Nishikawa M., Yasuda S., Mizuno Y., Takakura Y. Cellular activation by plasmid DNA in various macrophages in primary culture. J Pharm Sci 2008, 97:4575-4585.
    • (2008) J Pharm Sci , vol.97 , pp. 4575-4585
    • Yoshida, H.1    Nishikawa, M.2    Yasuda, S.3    Mizuno, Y.4    Takakura, Y.5
  • 23
    • 0036838909 scopus 로고    scopus 로고
    • Cutting edge: impaired Toll-like receptor expression and function in aging
    • Renshaw M., Rockwell J., Engleman C., Gewirtz A., Katz J., Sambhara S. Cutting edge: impaired Toll-like receptor expression and function in aging. J Immunol 2002, 169:4697-4701.
    • (2002) J Immunol , vol.169 , pp. 4697-4701
    • Renshaw, M.1    Rockwell, J.2    Engleman, C.3    Gewirtz, A.4    Katz, J.5    Sambhara, S.6
  • 24
    • 0032931559 scopus 로고    scopus 로고
    • Gene expression and antitumor effects following direct interferon (IFN)-gamma gene transfer with naked plasmid DNA and DC-chol liposome complexes in mice
    • Nomura T., Yasuda K., Yamada T., Okamoto S., Mahato R.I., Watanabe Y., et al. Gene expression and antitumor effects following direct interferon (IFN)-gamma gene transfer with naked plasmid DNA and DC-chol liposome complexes in mice. Gene Ther 1999, 6:121-129.
    • (1999) Gene Ther , vol.6 , pp. 121-129
    • Nomura, T.1    Yasuda, K.2    Yamada, T.3    Okamoto, S.4    Mahato, R.I.5    Watanabe, Y.6
  • 25
    • 0029984358 scopus 로고    scopus 로고
    • CpG motifs present in bacteria DNA rapidly induce lymphocytes to secrete interleukin 6, interleukin 12, and interferon gamma
    • Klinman D.M., Yi A.K., Beaucage S.L., Conover J., Krieg A.M. CpG motifs present in bacteria DNA rapidly induce lymphocytes to secrete interleukin 6, interleukin 12, and interferon gamma. P Natl Acad Sci USA 1996, 93:2879-2883.
    • (1996) P Natl Acad Sci USA , vol.93 , pp. 2879-2883
    • Klinman, D.M.1    Yi, A.K.2    Beaucage, S.L.3    Conover, J.4    Krieg, A.M.5
  • 26
    • 0030816325 scopus 로고    scopus 로고
    • Macrophages sense pathogens via DNA motifs: induction of tumor necrosis factor-alpha-mediated shock
    • Sparwasser T., Miethke T., Lipford G., Erdmann A., Hacker H., Heeg K., et al. Macrophages sense pathogens via DNA motifs: induction of tumor necrosis factor-alpha-mediated shock. Eur J Immunol 1997, 27:1671-1679.
    • (1997) Eur J Immunol , vol.27 , pp. 1671-1679
    • Sparwasser, T.1    Miethke, T.2    Lipford, G.3    Erdmann, A.4    Hacker, H.5    Heeg, K.6
  • 28
    • 0032476602 scopus 로고    scopus 로고
    • CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation
    • Hacker H., Mischak H., Miethke T., Liptay S., Schmid R., Sparwasser T., et al. CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation. Embo J 1998, 17:6230-6240.
    • (1998) Embo J , vol.17 , pp. 6230-6240
    • Hacker, H.1    Mischak, H.2    Miethke, T.3    Liptay, S.4    Schmid, R.5    Sparwasser, T.6
  • 29
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3
    • Alexopoulou L., Holt A.C., Medzhitov R., Flavell R.A. Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 2001, 413:732-738.
    • (2001) Nature , vol.413 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 30
    • 34547143110 scopus 로고    scopus 로고
    • DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
    • Takaoka A., Wang Z., Choi M.K., Yanai H., Negishi H., Ban T., et al. DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature 2007, 448:501-505.
    • (2007) Nature , vol.448 , pp. 501-505
    • Takaoka, A.1    Wang, Z.2    Choi, M.K.3    Yanai, H.4    Negishi, H.5    Ban, T.6
  • 31
    • 44449157593 scopus 로고    scopus 로고
    • Regulation of innate immune responses by DAI (DLM-1/ZBP1) and other DNA-sensing molecules
    • Wang Z., Choi M.K., Ban T., Yanai H., Negishi H., Lu Y., et al. Regulation of innate immune responses by DAI (DLM-1/ZBP1) and other DNA-sensing molecules. P Natl Acad Sci USA 2008, 105:5477-5482.
    • (2008) P Natl Acad Sci USA , vol.105 , pp. 5477-5482
    • Wang, Z.1    Choi, M.K.2    Ban, T.3    Yanai, H.4    Negishi, H.5    Lu, Y.6
  • 32
    • 0030904729 scopus 로고    scopus 로고
    • Fibronectin enhances in vitro lipopolysaccharide priming of polymorphonuclear leukocytes
    • Bortolussi R., Rajaraman K., Qing G., Rajaraman R. Fibronectin enhances in vitro lipopolysaccharide priming of polymorphonuclear leukocytes. Blood 1997, 89:4182-4189.
    • (1997) Blood , vol.89 , pp. 4182-4189
    • Bortolussi, R.1    Rajaraman, K.2    Qing, G.3    Rajaraman, R.4
  • 33
    • 0019875880 scopus 로고
    • Methylation of CpG sequences in eukaryotic DNA
    • Gruenbaum Y., Stein R., Cedar H., Razin A. Methylation of CpG sequences in eukaryotic DNA. FEBS Lett 1981, 124:67-71.
    • (1981) FEBS Lett , vol.124 , pp. 67-71
    • Gruenbaum, Y.1    Stein, R.2    Cedar, H.3    Razin, A.4
  • 34
    • 0037378005 scopus 로고    scopus 로고
    • The molecular basis for the lack of immunostimulatory activity of vertebrate DNA
    • Stacey K.J., Young G.R., Clark F., Sester D.P., Roberts T.L., Naik S., et al. The molecular basis for the lack of immunostimulatory activity of vertebrate DNA. J Immunol 2003, 170:3614-3620.
    • (2003) J Immunol , vol.170 , pp. 3614-3620
    • Stacey, K.J.1    Young, G.R.2    Clark, F.3    Sester, D.P.4    Roberts, T.L.5    Naik, S.6
  • 35
    • 21844438276 scopus 로고    scopus 로고
    • A Toll for lupus
    • Anders H.J. A Toll for lupus. Lupus 2005, 14:417-422.
    • (2005) Lupus , vol.14 , pp. 417-422
    • Anders, H.J.1
  • 36
    • 11844290125 scopus 로고    scopus 로고
    • Cutting edge: species-specific TLR9-mediated recognition of CpG and non-CpG phosphorothioate-modified oligonucleotides
    • Roberts T.L., Sweet M.J., Hume D.A., Stacey K.J. Cutting edge: species-specific TLR9-mediated recognition of CpG and non-CpG phosphorothioate-modified oligonucleotides. J Immunol 2005, 174:605-608.
    • (2005) J Immunol , vol.174 , pp. 605-608
    • Roberts, T.L.1    Sweet, M.J.2    Hume, D.A.3    Stacey, K.J.4
  • 37
    • 18644383289 scopus 로고    scopus 로고
    • Endosomal translocation of vertebrate DNA activates dendritic cells via TLR9-dependent and -independent pathways
    • Yasuda K., Yu P., Kirschning C.J., Schlatter B., Schmitz F., Heit A., et al. Endosomal translocation of vertebrate DNA activates dendritic cells via TLR9-dependent and -independent pathways. J Immunol 2005, 174:6129-6136.
    • (2005) J Immunol , vol.174 , pp. 6129-6136
    • Yasuda, K.1    Yu, P.2    Kirschning, C.J.3    Schlatter, B.4    Schmitz, F.5    Heit, A.6
  • 38
    • 32944462310 scopus 로고    scopus 로고
    • CpG motif-independent activation of TLR9 upon endosomal translocation of " natural" phosphodiester DNA
    • Yasuda K., Rutz M., Schlatter B., Metzger J., Luppa P.B., Schmitz F., et al. CpG motif-independent activation of TLR9 upon endosomal translocation of " natural" phosphodiester DNA. Eur J Immunol 2006, 36:431-436.
    • (2006) Eur J Immunol , vol.36 , pp. 431-436
    • Yasuda, K.1    Rutz, M.2    Schlatter, B.3    Metzger, J.4    Luppa, P.B.5    Schmitz, F.6
  • 39
    • 40249088259 scopus 로고    scopus 로고
    • The DNA sugar backbone 2' deoxyribose determines toll-like receptor 9 activation
    • Haas T., Metzger J., Schmitz F., Heit A., Muller T., Latz E., et al. The DNA sugar backbone 2' deoxyribose determines toll-like receptor 9 activation. Immunity 2008, 28:315-323.
    • (2008) Immunity , vol.28 , pp. 315-323
    • Haas, T.1    Metzger, J.2    Schmitz, F.3    Heit, A.4    Muller, T.5    Latz, E.6
  • 40
    • 0036222620 scopus 로고    scopus 로고
    • Human Toll-like receptor 4 recognizes host-specific LPS modifications
    • Hajjar A.M., Ernst R.K., Tsai J.H., Wilson C.B., Miller S.I. Human Toll-like receptor 4 recognizes host-specific LPS modifications. Nat Immunol 2002, 3:354-359.
    • (2002) Nat Immunol , vol.3 , pp. 354-359
    • Hajjar, A.M.1    Ernst, R.K.2    Tsai, J.H.3    Wilson, C.B.4    Miller, S.I.5
  • 41
    • 47049114564 scopus 로고    scopus 로고
    • Single-stranded oligonucleotides can inhibit cytokine production induced by human toll-like receptor 3
    • Ranjith-Kumar C.T., Duffy K.E., Jordan J.L., Eaton-Bassiri A., Vaughan R., Hoose S.A., et al. Single-stranded oligonucleotides can inhibit cytokine production induced by human toll-like receptor 3. Mol Cell Biol. 2008, 28:4507-4519.
    • (2008) Mol Cell Biol. , vol.28 , pp. 4507-4519
    • Ranjith-Kumar, C.T.1    Duffy, K.E.2    Jordan, J.L.3    Eaton-Bassiri, A.4    Vaughan, R.5    Hoose, S.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.