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Volumn 423, Issue 1, 2012, Pages 164-169

Single-chain variable fragment intrabody impairs LPS-induced inflammatory responses by interfering with the interaction between the WASP N-terminal domain and Btk in macrophages

Author keywords

Bruton's tyrosine kinase; Intrabody; LPS signaling; Macrophage; Phosphorylation; Wiskott Aldrich syndrome protein

Indexed keywords

BRUTON TYROSINE KINASE; CD11B ANTIGEN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; INTERLEUKIN 6; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PROTEIN SH3; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; TOLL LIKE RECEPTOR 4; TUMOR NECROSIS FACTOR ALPHA;

EID: 84862686544     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.05.105     Document Type: Article
Times cited : (4)

References (23)
  • 1
    • 0027937223 scopus 로고
    • Isolation of a novel gene mutation in Wiskott-Aldrich syndrome
    • Derry J.M., Ochs H.D., Francke U. Isolation of a novel gene mutation in Wiskott-Aldrich syndrome. Cell 1994, 78:635-644.
    • (1994) Cell , vol.78 , pp. 635-644
    • Derry, J.M.1    Ochs, H.D.2    Francke, U.3
  • 2
    • 0036717243 scopus 로고    scopus 로고
    • WASP in immune-system organization and function
    • Thrasher A.J. WASP in immune-system organization and function. Nat. Rev. Immunol. 2002, 2:635-646.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 635-646
    • Thrasher, A.J.1
  • 3
    • 0032528414 scopus 로고    scopus 로고
    • Monocytes from Wiskott-Aldrich patients display reduced chemotaxis and lack of cell polarization in response to monocyte chemoattractant protein-1 and formyl-methionyl-leucyl phenylalanine
    • Badolato R., Sozzani S., Malacarne F., Bresciani S., Fiorini M., Borsatti A., Albertini A., Mantovani A., Ugazio A.G., Notarangelo L.D. Monocytes from Wiskott-Aldrich patients display reduced chemotaxis and lack of cell polarization in response to monocyte chemoattractant protein-1 and formyl-methionyl-leucyl phenylalanine. J. Immunol. 1998, 161:1026-1033.
    • (1998) J. Immunol. , vol.161 , pp. 1026-1033
    • Badolato, R.1    Sozzani, S.2    Malacarne, F.3    Bresciani, S.4    Fiorini, M.5    Borsatti, A.6    Albertini, A.7    Mantovani, A.8    Ugazio, A.G.9    Notarangelo, L.D.10
  • 5
    • 0034192223 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein is necessary for efficient IgG-mediated phagocytosis
    • Lorenzi R., Brickell P.M., Katz D.R., Kinnon C., Thrasher A.J. Wiskott-Aldrich syndrome protein is necessary for efficient IgG-mediated phagocytosis. Blood 2000, 95:2943-2946.
    • (2000) Blood , vol.95 , pp. 2943-2946
    • Lorenzi, R.1    Brickell, P.M.2    Katz, D.R.3    Kinnon, C.4    Thrasher, A.J.5
  • 6
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Klm A.S., Kakalls L.T., Abdul-Manan N., Llu G.A., Rosen M.K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 2000, 404:151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Klm, A.S.1    Kakalls, L.T.2    Abdul-Manan, N.3    Llu, G.A.4    Rosen, M.K.5
  • 7
    • 68449092963 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome: immunodeficiency resulting from defective cell migration and impaired immunostimulatory activation
    • Bouma G., Burns S.O., Thrasher A.J. Wiskott-Aldrich syndrome: immunodeficiency resulting from defective cell migration and impaired immunostimulatory activation. Immunobiology 2009, 214:778-790.
    • (2009) Immunobiology , vol.214 , pp. 778-790
    • Bouma, G.1    Burns, S.O.2    Thrasher, A.J.3
  • 9
    • 0035887776 scopus 로고    scopus 로고
    • Overexpression of the Wiskott-Aldrich syndrome protein N-terminal domain in transgenic mice inhibits T cell proliferative response via TCR signaling without affecting cytoskeletal rearrangements
    • Sato M., Tsuji N.M., Gotoh H., Yamashita K., Hashimoto K., Tadotsu N., Yamanaka H., Sekikawa K., Hashimoto Y. Overexpression of the Wiskott-Aldrich syndrome protein N-terminal domain in transgenic mice inhibits T cell proliferative response via TCR signaling without affecting cytoskeletal rearrangements. J. Immunol. 2001, 167:4701-4709.
    • (2001) J. Immunol. , vol.167 , pp. 4701-4709
    • Sato, M.1    Tsuji, N.M.2    Gotoh, H.3    Yamashita, K.4    Hashimoto, K.5    Tadotsu, N.6    Yamanaka, H.7    Sekikawa, K.8    Hashimoto, Y.9
  • 10
    • 34548553236 scopus 로고    scopus 로고
    • Impaired LPS-induced signaling in microglia overexpressing the Wiskott-Aldrich syndrome protein N-terminal domain
    • Sato M., Ogihara K., Sawahata R., Sekikawa K., Kitani H. Impaired LPS-induced signaling in microglia overexpressing the Wiskott-Aldrich syndrome protein N-terminal domain. Int. Immunol. 2007, 19:901-911.
    • (2007) Int. Immunol. , vol.19 , pp. 901-911
    • Sato, M.1    Ogihara, K.2    Sawahata, R.3    Sekikawa, K.4    Kitani, H.5
  • 11
    • 84855813364 scopus 로고    scopus 로고
    • Critical roles of the WASP N-terminal domain and Btk in LPS-induced inflammatory response in macrophages
    • Sakuma C., Sato M., Takenouchi T., Chiba J., Kitani H. Critical roles of the WASP N-terminal domain and Btk in LPS-induced inflammatory response in macrophages. PLoS ONE 2012, 7:e30351.
    • (2012) PLoS ONE , vol.7
    • Sakuma, C.1    Sato, M.2    Takenouchi, T.3    Chiba, J.4    Kitani, H.5
  • 12
    • 28244456225 scopus 로고    scopus 로고
    • Intrabodies against the EVH1 domain of Wiskott-Aldrich syndrome protein inhibit T cell receptor signaling in transgenic mice T cells
    • Sato M., Iwaya R., Ogihara K., Sawahata R., Kitani H., Chiba J., Kurosawa Y., Sekikawa K. Intrabodies against the EVH1 domain of Wiskott-Aldrich syndrome protein inhibit T cell receptor signaling in transgenic mice T cells. FEBS J. 2005, 272:6131-6144.
    • (2005) FEBS J. , vol.272 , pp. 6131-6144
    • Sato, M.1    Iwaya, R.2    Ogihara, K.3    Sawahata, R.4    Kitani, H.5    Chiba, J.6    Kurosawa, Y.7    Sekikawa, K.8
  • 13
    • 0242552020 scopus 로고    scopus 로고
    • P38 Mitogen-activated protein kinase is crucially involved in osteoclast differentiation but not in cytokine production, phagocytosis, or dendritic cell differentiation of bone marrow macrophages
    • Li X., Udagawa N., Takami M., Sato N., Kobayashi Y., Takahashi N. P38 Mitogen-activated protein kinase is crucially involved in osteoclast differentiation but not in cytokine production, phagocytosis, or dendritic cell differentiation of bone marrow macrophages. Endocrinology 2003, 144:4999-5005.
    • (2003) Endocrinology , vol.144 , pp. 4999-5005
    • Li, X.1    Udagawa, N.2    Takami, M.3    Sato, N.4    Kobayashi, Y.5    Takahashi, N.6
  • 14
    • 0034886143 scopus 로고    scopus 로고
    • Toll-like receptors: critical proteins linking innate and acquired immunity
    • Akira S., Takeda K., Kaisyo T. Toll-like receptors: critical proteins linking innate and acquired immunity. Nat. Immunol. 2001, 2:675-680.
    • (2001) Nat. Immunol. , vol.2 , pp. 675-680
    • Akira, S.1    Takeda, K.2    Kaisyo, T.3
  • 15
    • 4744370253 scopus 로고    scopus 로고
    • Signal transduction by the lipopolysaccharide receptor, Toll-like receptor-4
    • Palsson-Mcdermott E.M., O'Neill L.A.J. Signal transduction by the lipopolysaccharide receptor, Toll-like receptor-4. Immunology 2004, 113:153-162.
    • (2004) Immunology , vol.113 , pp. 153-162
    • Palsson-Mcdermott, E.M.1    O'Neill, L.A.J.2
  • 16
    • 34547788305 scopus 로고    scopus 로고
    • The Troll in Toll: Mal and Tram as bridges for TLR2 and TLR4 signaling
    • Sheedy F.J., O'Neill L.A.J. The Troll in Toll: Mal and Tram as bridges for TLR2 and TLR4 signaling. J. Leukoc. Biol. 2007, 82:196-203.
    • (2007) J. Leukoc. Biol. , vol.82 , pp. 196-203
    • Sheedy, F.J.1    O'Neill, L.A.J.2
  • 17
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signaling
    • O'Neill L.A.J., Bowie A.G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signaling. Nat. Rev. Immunol. 2007, 7:353-364.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 353-364
    • O'Neill, L.A.J.1    Bowie, A.G.2
  • 18
    • 33744543517 scopus 로고    scopus 로고
    • MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction
    • Gray P., Dunne A., Brikos C., Jefferies C.A., Doyle S.L., O'Neill L.A.J. MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction. J. Biol. Chem. 2006, 281:10489-10495.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10489-10495
    • Gray, P.1    Dunne, A.2    Brikos, C.3    Jefferies, C.A.4    Doyle, S.L.5    O'Neill, L.A.J.6
  • 19
    • 11244285329 scopus 로고    scopus 로고
    • Constitutive and Interleukin-1-inducible phosphorylation of p65 NF-κB at serine 536 is mediated by multiple protein kinases including IκB kinase (IKK)-α, IKKβ, IKKε, TRAF family member-associated (TANK)-binding kinase 1 (TBK1), and an unknown kinase and couples p65 to TATA-binding protein-associated fac
    • Buss H., Dorrie A., Schmitz M.L., Hoffmann E., Resch K., Kracht M. Constitutive and Interleukin-1-inducible phosphorylation of p65 NF-κB at serine 536 is mediated by multiple protein kinases including IκB kinase (IKK)-α, IKKβ, IKKε, TRAF family member-associated (TANK)-binding kinase 1 (TBK1), and an unknown kinase and couples p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription. J. Biol. Chem. 2004, 279:55633-55643.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55633-55643
    • Buss, H.1    Dorrie, A.2    Schmitz, M.L.3    Hoffmann, E.4    Resch, K.5    Kracht, M.6
  • 20
    • 0037851769 scopus 로고    scopus 로고
    • IKKβ plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide
    • Yang F., Tang E., Guan K., Wang C. IKKβ plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide. J. Immunol. 2003, 170:5630-5635.
    • (2003) J. Immunol. , vol.170 , pp. 5630-5635
    • Yang, F.1    Tang, E.2    Guan, K.3    Wang, C.4
  • 21
    • 21244503601 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase is involved in p65-mediated transactivation and phosphorylation of p65 on Serine 536 during NFκB activation by lipopolysaccharide
    • Doyle S.L., Jefferies C.A., O'Neill L.A.J. Bruton's tyrosine kinase is involved in p65-mediated transactivation and phosphorylation of p65 on Serine 536 during NFκB activation by lipopolysaccharide. J. Biol. Chem. 2005, 280:23496-23501.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23496-23501
    • Doyle, S.L.1    Jefferies, C.A.2    O'Neill, L.A.J.3
  • 22
    • 0037087438 scopus 로고    scopus 로고
    • Macrophage effector functions controlled by Bruton's tyrosine kinase are more crucial than the cytokine balance of T cell responses for microfilarial clearance
    • Mukhopadhyay S., Mohanty M., Mangla A., George A., Bal V., Rath S., Ravindran B. Macrophage effector functions controlled by Bruton's tyrosine kinase are more crucial than the cytokine balance of T cell responses for microfilarial clearance. J. Immunol. 2002, 168:2914-2921.
    • (2002) J. Immunol. , vol.168 , pp. 2914-2921
    • Mukhopadhyay, S.1    Mohanty, M.2    Mangla, A.3    George, A.4    Bal, V.5    Rath, S.6    Ravindran, B.7


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