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Volumn 46, Issue 15, 2009, Pages 3141-3150

In-silico cell surface modeling reveals mechanism for initial steps of B-cell receptor signal transduction

Author keywords

B cell receptor; Cell surface dynamics; Diffusion; Lipid rafts; Monte Carlo method

Indexed keywords

B LYMPHOCYTE RECEPTOR; PROTEIN KINASE LYN;

EID: 68749120548     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2009.03.027     Document Type: Article
Times cited : (9)

References (41)
  • 1
    • 0032100706 scopus 로고    scopus 로고
    • Affinity dependence of the B-cell response to antigen: a threshold, a ceiling, and the importance of off-rate
    • Batista F.D., and Neuberger M.S. Affinity dependence of the B-cell response to antigen: a threshold, a ceiling, and the importance of off-rate. Immunity 8 (1998) 751-759
    • (1998) Immunity , vol.8 , pp. 751-759
    • Batista, F.D.1    Neuberger, M.S.2
  • 2
    • 0016326987 scopus 로고
    • Model for the binding of multivalent antigen to cells
    • Bell G.I. Model for the binding of multivalent antigen to cells. Nature 248 (1974) 430-431
    • (1974) Nature , vol.248 , pp. 430-431
    • Bell, G.I.1
  • 4
    • 0033818309 scopus 로고    scopus 로고
    • B-cell antigen receptor competence regulates B-lymphocyte selection and survival
    • Buhl A.M., Nemazee D., Cambier J.C., Rickert R., and Hertz M. B-cell antigen receptor competence regulates B-lymphocyte selection and survival. Immunol. Rev. 176 (2000) 141-153
    • (2000) Immunol. Rev. , vol.176 , pp. 141-153
    • Buhl, A.M.1    Nemazee, D.2    Cambier, J.C.3    Rickert, R.4    Hertz, M.5
  • 6
    • 0033431772 scopus 로고    scopus 로고
    • A role for lipid rafts in B-cell antigen receptor signaling and antigen targeting
    • Cheng P.C., Dykstra M.L., Mitchell R.N., and Pierce S.K. A role for lipid rafts in B-cell antigen receptor signaling and antigen targeting. J. Exp. Med. 190 (1999) 1549-1560
    • (1999) J. Exp. Med. , vol.190 , pp. 1549-1560
    • Cheng, P.C.1    Dykstra, M.L.2    Mitchell, R.N.3    Pierce, S.K.4
  • 7
    • 0034955304 scopus 로고    scopus 로고
    • Floating the raft hypothesis: lipid rafts play a role in immune cell activation
    • Cherukuri A., Dykstra M., and Pierce S.K. Floating the raft hypothesis: lipid rafts play a role in immune cell activation. Immunity 14 (2001) 657-660
    • (2001) Immunity , vol.14 , pp. 657-660
    • Cherukuri, A.1    Dykstra, M.2    Pierce, S.K.3
  • 9
    • 37349077033 scopus 로고    scopus 로고
    • CD19 is essential for B-cell activation by promoting B-cell receptor-antigen microcluster formation in response to membrane-bound ligand
    • Depoil D., Fleire S., Treanor B.L., Weber M., Harwood N.E., Marchbank K.L., Tybulewicz V.L., and Batista F.D. CD19 is essential for B-cell activation by promoting B-cell receptor-antigen microcluster formation in response to membrane-bound ligand. Nat. Immunol. 9 (2008) 63-72
    • (2008) Nat. Immunol. , vol.9 , pp. 63-72
    • Depoil, D.1    Fleire, S.2    Treanor, B.L.3    Weber, M.4    Harwood, N.E.5    Marchbank, K.L.6    Tybulewicz, V.L.7    Batista, F.D.8
  • 10
    • 0042689324 scopus 로고
    • Molecular determinants of immunogenicity: the immunon model of immune response
    • Dintzis H.M., Dintzis R.Z., and Vogelstein B. Molecular determinants of immunogenicity: the immunon model of immune response. Proc. Natl. Acad. Sci. U.S.A 73 (1976) 3671-3675
    • (1976) Proc. Natl. Acad. Sci. U.S.A , vol.73 , pp. 3671-3675
    • Dintzis, H.M.1    Dintzis, R.Z.2    Vogelstein, B.3
  • 11
    • 0024395440 scopus 로고
    • The immunogenicity of soluble haptenated polymers is determined by molecular mass and hapten valence
    • Dintzis R.Z., Okajima M., Middleton M.H., Greene G., and Dintzis H.M. The immunogenicity of soluble haptenated polymers is determined by molecular mass and hapten valence. J. Immunol. 143 (1989) 1239-1244
    • (1989) J. Immunol. , vol.143 , pp. 1239-1244
    • Dintzis, R.Z.1    Okajima, M.2    Middleton, M.H.3    Greene, G.4    Dintzis, H.M.5
  • 12
    • 0021352499 scopus 로고
    • The interaction of monoclonal antibodies with MHC class I antigens on mouse spleen cells. I Analysis of the mechanism of binding
    • Dower S.K., Ozato K., and Segal D.M. The interaction of monoclonal antibodies with MHC class I antigens on mouse spleen cells. I Analysis of the mechanism of binding. J. Immunol. 132 (1984) 751-758
    • (1984) J. Immunol. , vol.132 , pp. 751-758
    • Dower, S.K.1    Ozato, K.2    Segal, D.M.3
  • 13
    • 0023107205 scopus 로고
    • Analysis of the interaction of antibodies with immunoglobulin idiotypes on neoplastic B lymphocytes: implications for immunotherapy
    • Elliott T.J., Glennie M.J., McBride H.M., and Stevenson G.T. Analysis of the interaction of antibodies with immunoglobulin idiotypes on neoplastic B lymphocytes: implications for immunotherapy. J. Immunol. 138 (1987) 981-988
    • (1987) J. Immunol. , vol.138 , pp. 981-988
    • Elliott, T.J.1    Glennie, M.J.2    McBride, H.M.3    Stevenson, G.T.4
  • 15
    • 0000308038 scopus 로고    scopus 로고
    • Time-resolved dynamics of proton transfer in proteinous systems
    • Gutman M., and Nachliel E. Time-resolved dynamics of proton transfer in proteinous systems. Annu. Rev. Phys. Chem. 48 (1997) 329-356
    • (1997) Annu. Rev. Phys. Chem. , vol.48 , pp. 329-356
    • Gutman, M.1    Nachliel, E.2
  • 16
    • 0025868702 scopus 로고
    • Resolution and characterization of pro-B and pre-pro-B-cell stages in normal mouse bone marrow
    • Hardy R.R., Carmack C.E., Shinton S.A., Kemp J.D., and Hayakawa K. Resolution and characterization of pro-B and pre-pro-B-cell stages in normal mouse bone marrow. J. Exp. Med. 173 (1991) 1213-1225
    • (1991) J. Exp. Med. , vol.173 , pp. 1213-1225
    • Hardy, R.R.1    Carmack, C.E.2    Shinton, S.A.3    Kemp, J.D.4    Hayakawa, K.5
  • 17
    • 0027447188 scopus 로고
    • Elimination of self-reactive B lymphocytes proceeds in two stages: arrested development and cell death
    • Hartley S.B., Cooke M.P., Fulcher D.A., Harris A.W., Cory S., Basten A., and Goodnow C.C. Elimination of self-reactive B lymphocytes proceeds in two stages: arrested development and cell death. Cell 72 (1993) 325-335
    • (1993) Cell , vol.72 , pp. 325-335
    • Hartley, S.B.1    Cooke, M.P.2    Fulcher, D.A.3    Harris, A.W.4    Cory, S.5    Basten, A.6    Goodnow, C.C.7
  • 18
    • 0016717551 scopus 로고
    • Influence of molecular structure on the tolerogenicity of bacterial dextrans. I The alpha1-6-linked epitope of dextran B512
    • Howard J.G., Vicari G., and Courtenay B.M. Influence of molecular structure on the tolerogenicity of bacterial dextrans. I The alpha1-6-linked epitope of dextran B512. Immunology 29 (1975) 585-597
    • (1975) Immunology , vol.29 , pp. 585-597
    • Howard, J.G.1    Vicari, G.2    Courtenay, B.M.3
  • 19
    • 0032938887 scopus 로고    scopus 로고
    • Antigen receptor signaling induces differential tyrosine kinase activation and population stability in B-cell lymphoma
    • Hsueh R.C., Hammill A.K., Marches R., Uhr J.W., and Scheuermann R.H. Antigen receptor signaling induces differential tyrosine kinase activation and population stability in B-cell lymphoma. Curr. Top. Microbiol. Immunol. 246 (1999) 299-304
    • (1999) Curr. Top. Microbiol. Immunol. , vol.246 , pp. 299-304
    • Hsueh, R.C.1    Hammill, A.K.2    Marches, R.3    Uhr, J.W.4    Scheuermann, R.H.5
  • 20
    • 21244441843 scopus 로고    scopus 로고
    • Independent trafficking of Ig-alpha/Ig-beta and mu-heavy chain is facilitated by dissociation of the B-cell antigen receptor complex
    • Kim J.H., Cramer L., Mueller H., Wilson B., and Vilen B.J. Independent trafficking of Ig-alpha/Ig-beta and mu-heavy chain is facilitated by dissociation of the B-cell antigen receptor complex. J. Immunol. 175 (2005) 147-154
    • (2005) J. Immunol. , vol.175 , pp. 147-154
    • Kim, J.H.1    Cramer, L.2    Mueller, H.3    Wilson, B.4    Vilen, B.J.5
  • 21
    • 0034691152 scopus 로고    scopus 로고
    • B-cell receptor expression level determines the fate of developing B lymphocytes: receptor editing versus selection
    • Kouskoff V., Lacaud G., Pape K., Retter M., and Nemazee D. B-cell receptor expression level determines the fate of developing B lymphocytes: receptor editing versus selection. Proc. Natl. Acad. Sci. U.S.A 97 (2000) 7435-7439
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 7435-7439
    • Kouskoff, V.1    Lacaud, G.2    Pape, K.3    Retter, M.4    Nemazee, D.5
  • 22
    • 0000387536 scopus 로고
    • B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72
    • Law D.A., Chan V.W., Datta S.K., and DeFranco A.L. B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72. Lyn and Fyn Curr. Biol. 3 (1993) 645-657
    • (1993) Lyn and Fyn Curr. Biol. , vol.3 , pp. 645-657
    • Law, D.A.1    Chan, V.W.2    Datta, S.K.3    DeFranco, A.L.4
  • 23
    • 0019154473 scopus 로고
    • The kinetics of antibody binding to membrane antigens in solution and at the cell surface
    • Mason D.W., and Williams A.F. The kinetics of antibody binding to membrane antigens in solution and at the cell surface. Biochem. J. 187 (1980) 1-20
    • (1980) Biochem. J. , vol.187 , pp. 1-20
    • Mason, D.W.1    Williams, A.F.2
  • 24
    • 0025735935 scopus 로고
    • Affinity requirements for induction of sequential phases of human B-cell activation by membrane IgM-cross-linking ligands
    • Mongini P.K., Blessinger C.A., and Dalton J.P. Affinity requirements for induction of sequential phases of human B-cell activation by membrane IgM-cross-linking ligands. J. Immunol. 146 (1991) 1791-1800
    • (1991) J. Immunol. , vol.146 , pp. 1791-1800
    • Mongini, P.K.1    Blessinger, C.A.2    Dalton, J.P.3
  • 25
    • 11144334189 scopus 로고    scopus 로고
    • Antigen epitope density dependent cell surface discrimination and the role of the lipid rafts
    • Ref type: conference proceeding
    • Nudelman G., and Louzoun Y. Antigen epitope density dependent cell surface discrimination and the role of the lipid rafts. METMBS (2004) 429-435 Ref type: conference proceeding
    • (2004) METMBS , pp. 429-435
    • Nudelman, G.1    Louzoun, Y.2
  • 26
    • 31444437250 scopus 로고    scopus 로고
    • Cell surface dynamics: the balance between diffusion, aggregation and endocytosis
    • Nudelman G., and Louzoun Y. Cell surface dynamics: the balance between diffusion, aggregation and endocytosis. Syst. Biol. (Stevenage) 153 (2006) 34-42
    • (2006) Syst. Biol. (Stevenage) , vol.153 , pp. 34-42
    • Nudelman, G.1    Louzoun, Y.2
  • 27
    • 0036481264 scopus 로고    scopus 로고
    • Lipid rafts and B-cell activation
    • Pierce S.K. Lipid rafts and B-cell activation. Nat. Rev. Immunol. 2 (2002) 96-105
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 96-105
    • Pierce, S.K.1
  • 28
    • 0030890949 scopus 로고    scopus 로고
    • Initiation and processing of signals from the B-cell antigen receptor
    • Reth M., and Wienands J. Initiation and processing of signals from the B-cell antigen receptor. Annu. Rev. Immunol. 15 (1997) 453-479
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 453-479
    • Reth, M.1    Wienands, J.2
  • 29
    • 0025200578 scopus 로고
    • Proton dissociation dynamics in the aqueous layer of multilamellar phospholipid vesicles
    • Rochel S., Nachliel E., Huppert D., and Gutman M. Proton dissociation dynamics in the aqueous layer of multilamellar phospholipid vesicles. J. Membr. Biol. 118 (1990) 225-232
    • (1990) J. Membr. Biol. , vol.118 , pp. 225-232
    • Rochel, S.1    Nachliel, E.2    Huppert, D.3    Gutman, M.4
  • 31
    • 0023727485 scopus 로고
    • Anti-IgM-mediated B-cell signaling. Molecular analysis of ligand binding requisites for human B-cell clonal expansion and tolerance
    • Rudich S.M., Roux K.H., Winchester R.J., and Mongini P.K. Anti-IgM-mediated B-cell signaling. Molecular analysis of ligand binding requisites for human B-cell clonal expansion and tolerance. J. Exp. Med. 168 (1988) 247-266
    • (1988) J. Exp. Med. , vol.168 , pp. 247-266
    • Rudich, S.M.1    Roux, K.H.2    Winchester, R.J.3    Mongini, P.K.4
  • 32
    • 0022352682 scopus 로고
    • Human B-cell activation. Evidence for diverse signals provided by various monoclonal anti-IgM antibodies
    • Rudich S.M., Winchester R., and Mongini P.K. Human B-cell activation. Evidence for diverse signals provided by various monoclonal anti-IgM antibodies. J. Exp. Med. 162 (1985) 1236-1255
    • (1985) J. Exp. Med. , vol.162 , pp. 1236-1255
    • Rudich, S.M.1    Winchester, R.2    Mongini, P.K.3
  • 33
    • 0034874786 scopus 로고    scopus 로고
    • Structure and function of Syk protein-tyrosine kinase
    • Sada K., Takano T., Yanagi S., and Yamamura H. Structure and function of Syk protein-tyrosine kinase. J. Biochem. (Tokyo) 130 (2001) 177-186
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 177-186
    • Sada, K.1    Takano, T.2    Yanagi, S.3    Yamamura, H.4
  • 35
    • 33744476136 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer in living cells reveals dynamic membrane changes in the initiation of B-cell signaling
    • Sohn H.W., Tolar P., Jin T., and Pierce S.K. Fluorescence resonance energy transfer in living cells reveals dynamic membrane changes in the initiation of B-cell signaling. Proc. Natl. Acad. Sci. U.S.A 103 (2006) 8143-8148
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 8143-8148
    • Sohn, H.W.1    Tolar, P.2    Jin, T.3    Pierce, S.K.4
  • 36
    • 48249124978 scopus 로고    scopus 로고
    • Membrane heterogeneities in the formation of B-cell receptor-Lyn kinase microclusters and the immune synapse
    • Sohn H.W., Tolar P., and Pierce S.K. Membrane heterogeneities in the formation of B-cell receptor-Lyn kinase microclusters and the immune synapse. J. Cell Biol. 182 (2008) 367-379
    • (2008) J. Cell Biol. , vol.182 , pp. 367-379
    • Sohn, H.W.1    Tolar, P.2    Pierce, S.K.3
  • 37
    • 27544446258 scopus 로고    scopus 로고
    • The initiation of antigen-induced B-cell antigen receptor signaling viewed in living cells by fluorescence resonance energy transfer
    • Tolar P., Sohn H.W., and Pierce S.K. The initiation of antigen-induced B-cell antigen receptor signaling viewed in living cells by fluorescence resonance energy transfer. Nat. Immunol. 6 (2005) 1168-1176
    • (2005) Nat. Immunol. , vol.6 , pp. 1168-1176
    • Tolar, P.1    Sohn, H.W.2    Pierce, S.K.3
  • 38
    • 38949180982 scopus 로고    scopus 로고
    • Viewing the antigen-induced initiation of B-cell activation in living cells
    • Tolar P., Sohn H.W., and Pierce S.K. Viewing the antigen-induced initiation of B-cell activation in living cells. Immunol. Rev. 221 (2008) 64-76
    • (2008) Immunol. Rev. , vol.221 , pp. 64-76
    • Tolar, P.1    Sohn, H.W.2    Pierce, S.K.3
  • 39
    • 0021061430 scopus 로고
    • The binding of monoclonal antibodies to cell-surface molecules. A quantitative analysis with immunoglobulin G against two alloantigenic determinants of the human transplantation antigen HLA-A2
    • Ways J.P., and Parham P. The binding of monoclonal antibodies to cell-surface molecules. A quantitative analysis with immunoglobulin G against two alloantigenic determinants of the human transplantation antigen HLA-A2. Biochem. J. 216 (1983) 423-432
    • (1983) Biochem. J. , vol.216 , pp. 423-432
    • Ways, J.P.1    Parham, P.2
  • 41
    • 0038827018 scopus 로고    scopus 로고
    • A lipid raft environment enhances Lyn kinase activity by protecting the active site tyrosine from dephosphorylation
    • Young R.M., Holowka D., and Baird B. A lipid raft environment enhances Lyn kinase activity by protecting the active site tyrosine from dephosphorylation. J. Biol. Chem. 278 (2003) 20746-20752
    • (2003) J. Biol. Chem. , vol.278 , pp. 20746-20752
    • Young, R.M.1    Holowka, D.2    Baird, B.3


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