메뉴 건너뛰기




Volumn 103, Issue , 2014, Pages 241-253

Phosphoproteomic analyses reveal that galectin-1 augments the dynamics of B-cell receptor signaling

Author keywords

B cell activation; B cell receptor; Galectin 1; Phosphoproteome

Indexed keywords

B LYMPHOCYTE RECEPTOR; BRUTON TYROSINE KINASE; CALCIUM; CYCLIC AMP DEPENDENT PROTEIN KINASE; GALECTIN 1; GRANZYME A; INTERLEUKIN 3; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C GAMMA; PHOSPHOPEPTIDE; PHOSPHOSERINE; PHOSPHOTHREONINE; PHOSPHOTYROSINE; PROTEIN KINASE SYK; TELOMERASE; ANTI-IGM; ANTIIDIOTYPIC ANTIBODY; LYMPHOCYTE ANTIGEN RECEPTOR; PHOSPHOPROTEIN;

EID: 84899801182     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.03.031     Document Type: Article
Times cited : (14)

References (46)
  • 3
    • 75749101401 scopus 로고    scopus 로고
    • Galectins: regulators of acute and chronic inflammation
    • Liu F.T., Rabinovich G.A. Galectins: regulators of acute and chronic inflammation. Ann N Y Acad Sci 2010, 1183:158-182.
    • (2010) Ann N Y Acad Sci , vol.1183 , pp. 158-182
    • Liu, F.T.1    Rabinovich, G.A.2
  • 4
    • 58149286593 scopus 로고    scopus 로고
    • Galectin-1 promotes immunoglobulin production during plasma cell differentiation
    • Tsai C.M., Chiu Y.K., Hsu T.L., Lin I.Y., Hsieh S.L., Lin K.I. Galectin-1 promotes immunoglobulin production during plasma cell differentiation. J Immunol 2008, 181:4570-4579.
    • (2008) J Immunol , vol.181 , pp. 4570-4579
    • Tsai, C.M.1    Chiu, Y.K.2    Hsu, T.L.3    Lin, I.Y.4    Hsieh, S.L.5    Lin, K.I.6
  • 5
    • 0034974155 scopus 로고    scopus 로고
    • Regulated expression of galectin-1 during B-cell activation and implications for T-cell apoptosis
    • Zuniga E., Rabinovich G.A., Iglesias M.M., Gruppi A. Regulated expression of galectin-1 during B-cell activation and implications for T-cell apoptosis. J Leukoc Biol 2001, 70:73-79.
    • (2001) J Leukoc Biol , vol.70 , pp. 73-79
    • Zuniga, E.1    Rabinovich, G.A.2    Iglesias, M.M.3    Gruppi, A.4
  • 6
    • 84878942469 scopus 로고    scopus 로고
    • Nurse-like cells control the activity of chronic lymphocytic leukemia B cells via galectin-1
    • Croci D.O., Morande P.E., Dergan-Dylon S., Borge M., Toscano M.A., Stupirski J.C., et al. Nurse-like cells control the activity of chronic lymphocytic leukemia B cells via galectin-1. Leukemia 2012, 27:1413-1416.
    • (2012) Leukemia , vol.27 , pp. 1413-1416
    • Croci, D.O.1    Morande, P.E.2    Dergan-Dylon, S.3    Borge, M.4    Toscano, M.A.5    Stupirski, J.C.6
  • 7
    • 59149097542 scopus 로고    scopus 로고
    • Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling
    • Garner O.B., Baum L.G. Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling. Biochem Soc Trans 2008, 36:1472-1477.
    • (2008) Biochem Soc Trans , vol.36 , pp. 1472-1477
    • Garner, O.B.1    Baum, L.G.2
  • 8
    • 67349258025 scopus 로고    scopus 로고
    • Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation
    • Rabinovich G.A., Toscano M.A. Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat Rev Immunol 2009, 9:338-352.
    • (2009) Nat Rev Immunol , vol.9 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.A.2
  • 11
    • 70350371721 scopus 로고    scopus 로고
    • Galectin-1 co-clusters CD43/CD45 on dendritic cells and induces cell activation and migration through Syk and protein kinase C signaling
    • Fulcher J.A., Chang M.H., Wang S., Almazan T., Hashimi S.T., Eriksson A.U., et al. Galectin-1 co-clusters CD43/CD45 on dendritic cells and induces cell activation and migration through Syk and protein kinase C signaling. J Biol Chem 2009, 284:26860-26870.
    • (2009) J Biol Chem , vol.284 , pp. 26860-26870
    • Fulcher, J.A.1    Chang, M.H.2    Wang, S.3    Almazan, T.4    Hashimi, S.T.5    Eriksson, A.U.6
  • 12
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127:635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6
  • 13
    • 0029068171 scopus 로고
    • Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation
    • Rowley R.B., Burkhardt A.L., Chao H.G., Matsueda G.R., Bolen J.B. Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation. J Biol Chem 1995, 270:11590-11594.
    • (1995) J Biol Chem , vol.270 , pp. 11590-11594
    • Rowley, R.B.1    Burkhardt, A.L.2    Chao, H.G.3    Matsueda, G.R.4    Bolen, J.B.5
  • 14
    • 0028905060 scopus 로고
    • Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE
    • Shiue L., Zoller M.J., Brugge J.S. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J Biol Chem 1995, 270:10498-10502.
    • (1995) J Biol Chem , vol.270 , pp. 10498-10502
    • Shiue, L.1    Zoller, M.J.2    Brugge, J.S.3
  • 15
    • 0028793187 scopus 로고
    • Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate Lyn and Syk tyrosine kinases
    • Johnson S.A., Pleiman C.M., Pao L., Schneringer J., Hippen K., Cambier J.C. Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate Lyn and Syk tyrosine kinases. J Immunol 1995, 155:4596-4603.
    • (1995) J Immunol , vol.155 , pp. 4596-4603
    • Johnson, S.A.1    Pleiman, C.M.2    Pao, L.3    Schneringer, J.4    Hippen, K.5    Cambier, J.C.6
  • 16
    • 0033988729 scopus 로고    scopus 로고
    • Intermediary signaling effectors coupling the B-cell receptor to the nucleus
    • Gold M.R. Intermediary signaling effectors coupling the B-cell receptor to the nucleus. Curr Top Microbiol Immunol 2000, 245:77-134.
    • (2000) Curr Top Microbiol Immunol , vol.245 , pp. 77-134
    • Gold, M.R.1
  • 17
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • van Anken E., Romijn E.P., Maggioni C., Mezghrani A., Sitia R., Braakman I., et al. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 2003, 18:243-253.
    • (2003) Immunity , vol.18 , pp. 243-253
    • van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6
  • 18
    • 0023729241 scopus 로고
    • Altered immunoglobulin expression and functional silencing of self-reactive B lymphocytes in transgenic mice
    • Goodnow C.C., Crosbie J., Adelstein S., Lavoie T.B., Smith-Gill S.J., Brink R.A., et al. Altered immunoglobulin expression and functional silencing of self-reactive B lymphocytes in transgenic mice. Nature 1988, 334:676-682.
    • (1988) Nature , vol.334 , pp. 676-682
    • Goodnow, C.C.1    Crosbie, J.2    Adelstein, S.3    Lavoie, T.B.4    Smith-Gill, S.J.5    Brink, R.A.6
  • 19
    • 17044413339 scopus 로고    scopus 로고
    • Altered migration, recruitment, and somatic hypermutation in the early response of marginal zone B cells to T cell-dependent antigen
    • Phan T.G., Gardam S., Basten A., Brink R. Altered migration, recruitment, and somatic hypermutation in the early response of marginal zone B cells to T cell-dependent antigen. J Immunol 2005, 174:4567-4578.
    • (2005) J Immunol , vol.174 , pp. 4567-4578
    • Phan, T.G.1    Gardam, S.2    Basten, A.3    Brink, R.4
  • 20
    • 0037390660 scopus 로고    scopus 로고
    • B cell receptor-independent stimuli trigger immunoglobulin (Ig) class switch recombination and production of IgG autoantibodies by anergic self-reactive B cells
    • Phan T.G., Amesbury M., Gardam S., Crosbie J., Hasbold J., Hodgkin P.D., et al. B cell receptor-independent stimuli trigger immunoglobulin (Ig) class switch recombination and production of IgG autoantibodies by anergic self-reactive B cells. J Exp Med 2003, 197:845-860.
    • (2003) J Exp Med , vol.197 , pp. 845-860
    • Phan, T.G.1    Amesbury, M.2    Gardam, S.3    Crosbie, J.4    Hasbold, J.5    Hodgkin, P.D.6
  • 21
    • 79951655546 scopus 로고    scopus 로고
    • Pathway-selective suppression of chemokine receptor signaling in B cells by LPS through downregulation of PLC-beta2
    • Shirakawa A.K., Liao F., Zhang H.H., Hedrick M.N., Singh S.P., Wu D., et al. Pathway-selective suppression of chemokine receptor signaling in B cells by LPS through downregulation of PLC-beta2. Cell Mol Immunol 2010, 7:428-439.
    • (2010) Cell Mol Immunol , vol.7 , pp. 428-439
    • Shirakawa, A.K.1    Liao, F.2    Zhang, H.H.3    Hedrick, M.N.4    Singh, S.P.5    Wu, D.6
  • 22
    • 78149388475 scopus 로고    scopus 로고
    • An informatics-assisted label-free quantitation strategy that depicts phosphoproteomic profiles in lung cancer cell invasion
    • Wang Y.T., Tsai C.F., Hong T.C., Tsou C.C., Lin P.Y., Pan S.H., et al. An informatics-assisted label-free quantitation strategy that depicts phosphoproteomic profiles in lung cancer cell invasion. J Proteome Res 2010, 9:5582-5597.
    • (2010) J Proteome Res , vol.9 , pp. 5582-5597
    • Wang, Y.T.1    Tsai, C.F.2    Hong, T.C.3    Tsou, C.C.4    Lin, P.Y.5    Pan, S.H.6
  • 23
    • 76649139789 scopus 로고    scopus 로고
    • IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation
    • Tsou C.C., Tsai C.F., Tsui Y.H., Sudhir P.R., Wang Y.T., Chen Y.J., et al. IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation. Mol Cell Proteomics 2010, 9:131-144.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 131-144
    • Tsou, C.C.1    Tsai, C.F.2    Tsui, Y.H.3    Sudhir, P.R.4    Wang, Y.T.5    Chen, Y.J.6
  • 24
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap
    • Olsen J.V., de Godoy L.M., Li G., Macek B., Mortensen P., Pesch R., et al. Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap. Mol Cell Proteomics 2005, 4:2010-2021.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 2010-2021
    • Olsen, J.V.1    de Godoy, L.M.2    Li, G.3    Macek, B.4    Mortensen, P.5    Pesch, R.6
  • 26
    • 0038175144 scopus 로고    scopus 로고
    • GoMiner: a resource for biological interpretation of genomic and proteomic data
    • Zeeberg B.R., Feng W., Wang G., Wang M.D., Fojo A.T., Sunshine M., et al. GoMiner: a resource for biological interpretation of genomic and proteomic data. Genome Biol 2003, 4:R28.
    • (2003) Genome Biol , vol.4
    • Zeeberg, B.R.1    Feng, W.2    Wang, G.3    Wang, M.D.4    Fojo, A.T.5    Sunshine, M.6
  • 27
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz D., Gygi S.P. An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat Biotechnol 2005, 23:1391-1398.
    • (2005) Nat Biotechnol , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 29
    • 0033624638 scopus 로고    scopus 로고
    • Phospholipase Cgamma2 is essential in the functions of B cell and several Fc receptors
    • Wang D., Feng J., Wen R., Marine J.C., Sangster M.Y., Parganas E., et al. Phospholipase Cgamma2 is essential in the functions of B cell and several Fc receptors. Immunity 2000, 13:25-35.
    • (2000) Immunity , vol.13 , pp. 25-35
    • Wang, D.1    Feng, J.2    Wen, R.3    Marine, J.C.4    Sangster, M.Y.5    Parganas, E.6
  • 30
    • 0026573224 scopus 로고
    • Human recombinant IL-3 is a growth factor for normal B cells
    • Xia X., Li L., Choi Y.S. Human recombinant IL-3 is a growth factor for normal B cells. J Immunol 1992, 148:491-497.
    • (1992) J Immunol , vol.148 , pp. 491-497
    • Xia, X.1    Li, L.2    Choi, Y.S.3
  • 32
    • 18244366881 scopus 로고    scopus 로고
    • B lymphocyte stimulator activates p38 mitogen-activated protein kinase in human Ig class switch recombination
    • Yamada T., Zhang K., Yamada A., Zhu D., Saxon A. B lymphocyte stimulator activates p38 mitogen-activated protein kinase in human Ig class switch recombination. Am J Respir Cell Mol Biol 2005, 32:388-394.
    • (2005) Am J Respir Cell Mol Biol , vol.32 , pp. 388-394
    • Yamada, T.1    Zhang, K.2    Yamada, A.3    Zhu, D.4    Saxon, A.5
  • 33
    • 59249095812 scopus 로고    scopus 로고
    • Hematopoietic protein tyrosine phosphatase mediates beta2-adrenergic receptor-induced regulation of p38 mitogen-activated protein kinase in B lymphocytes
    • McAlees J.W., Sanders V.M. Hematopoietic protein tyrosine phosphatase mediates beta2-adrenergic receptor-induced regulation of p38 mitogen-activated protein kinase in B lymphocytes. Mol Cell Biol 2009, 29:675-686.
    • (2009) Mol Cell Biol , vol.29 , pp. 675-686
    • McAlees, J.W.1    Sanders, V.M.2
  • 34
    • 0037199989 scopus 로고    scopus 로고
    • Regulation of signaling in B cells through the phosphorylation of Syk on linker region tyrosines. A mechanism for negative signaling by the Lyn tyrosine kinase
    • Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L. Regulation of signaling in B cells through the phosphorylation of Syk on linker region tyrosines. A mechanism for negative signaling by the Lyn tyrosine kinase. J Biol Chem 2002, 277:31703-31714.
    • (2002) J Biol Chem , vol.277 , pp. 31703-31714
    • Hong, J.J.1    Yankee, T.M.2    Harrison, M.L.3    Geahlen, R.L.4
  • 35
    • 79953187997 scopus 로고    scopus 로고
    • Discovery of mouse spleen signaling responses to anthrax using label-free quantitative phosphoproteomics via mass spectrometry
    • [M110 000927]
    • Manes N.P., Dong L., Zhou W., Du X., Reghu N., Kool A.C., et al. Discovery of mouse spleen signaling responses to anthrax using label-free quantitative phosphoproteomics via mass spectrometry. Mol Cell Proteomics 2011, 10. [M110 000927].
    • (2011) Mol Cell Proteomics , vol.10
    • Manes, N.P.1    Dong, L.2    Zhou, W.3    Du, X.4    Reghu, N.5    Kool, A.C.6
  • 36
    • 0037352170 scopus 로고    scopus 로고
    • Involvement of PI3K/Akt pathway in cell cycle progression, apoptosis, and neoplastic transformation: a target for cancer chemotherapy
    • Chang F., Lee J.T., Navolanic P.M., Steelman L.S., Shelton J.G., Blalock W.L., et al. Involvement of PI3K/Akt pathway in cell cycle progression, apoptosis, and neoplastic transformation: a target for cancer chemotherapy. Leukemia 2003, 17:590-603.
    • (2003) Leukemia , vol.17 , pp. 590-603
    • Chang, F.1    Lee, J.T.2    Navolanic, P.M.3    Steelman, L.S.4    Shelton, J.G.5    Blalock, W.L.6
  • 37
    • 0034161763 scopus 로고    scopus 로고
    • Regulation of the calcium/NF-AT T cell activation pathway by the D2 domain of CD45
    • Wang Y., Liang L., Esselman W.J. Regulation of the calcium/NF-AT T cell activation pathway by the D2 domain of CD45. J Immunol 2000, 164:2557-2564.
    • (2000) J Immunol , vol.164 , pp. 2557-2564
    • Wang, Y.1    Liang, L.2    Esselman, W.J.3
  • 39
    • 61849141064 scopus 로고    scopus 로고
    • Tyrosine kinases and their substrates in B lymphocytes
    • Kurosaki T., Hikida M. Tyrosine kinases and their substrates in B lymphocytes. Immunol Rev 2009, 228:132-148.
    • (2009) Immunol Rev , vol.228 , pp. 132-148
    • Kurosaki, T.1    Hikida, M.2
  • 40
    • 0033178727 scopus 로고    scopus 로고
    • CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells
    • Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M., et al. CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells. J Immunol 1999, 163:1321-1326.
    • (1999) J Immunol , vol.163 , pp. 1321-1326
    • Katagiri, T.1    Ogimoto, M.2    Hasegawa, K.3    Arimura, Y.4    Mitomo, K.5    Okada, M.6
  • 41
    • 0032534071 scopus 로고    scopus 로고
    • Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B cell activation includes a site that negatively regulates signaling
    • Keshvara L.M., Isaacson C.C., Yankee T.M., Sarac R., Harrison M.L., Geahlen R.L. Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B cell activation includes a site that negatively regulates signaling. J Immunol 1998, 161:5276-5283.
    • (1998) J Immunol , vol.161 , pp. 5276-5283
    • Keshvara, L.M.1    Isaacson, C.C.2    Yankee, T.M.3    Sarac, R.4    Harrison, M.L.5    Geahlen, R.L.6
  • 42
    • 34249285831 scopus 로고    scopus 로고
    • Mining phosphopeptide signals in liquid chromatography-mass spectrometry data for protein phosphorylation analysis
    • Wu H.Y., Tseng V.S., Liao P.C. Mining phosphopeptide signals in liquid chromatography-mass spectrometry data for protein phosphorylation analysis. J Proteome Res 2007, 6:1812-1821.
    • (2007) J Proteome Res , vol.6 , pp. 1812-1821
    • Wu, H.Y.1    Tseng, V.S.2    Liao, P.C.3
  • 43
    • 51649121098 scopus 로고    scopus 로고
    • Immunoaffinity enrichments followed by mass spectrometric detection for studying global protein tyrosine phosphorylation
    • Bergstrom Lind S., Molin M., Savitski M.M., Emilsson L., Astrom J., Hedberg L., et al. Immunoaffinity enrichments followed by mass spectrometric detection for studying global protein tyrosine phosphorylation. J Proteome Res 2008, 7:2897-2910.
    • (2008) J Proteome Res , vol.7 , pp. 2897-2910
    • Bergstrom Lind, S.1    Molin, M.2    Savitski, M.M.3    Emilsson, L.4    Astrom, J.5    Hedberg, L.6
  • 44
    • 0041524094 scopus 로고    scopus 로고
    • A reinvestigation of the multisite phosphorylation of the transcription factor c-Jun
    • Morton S., Davis R.J., McLaren A., Cohen P. A reinvestigation of the multisite phosphorylation of the transcription factor c-Jun. EMBO J 2003, 22:3876-3886.
    • (2003) EMBO J , vol.22 , pp. 3876-3886
    • Morton, S.1    Davis, R.J.2    McLaren, A.3    Cohen, P.4
  • 45
    • 34247397364 scopus 로고    scopus 로고
    • Galectin-1 expression in cancer-associated stromal cells correlates tumor invasiveness and tumor progression in breast cancer
    • Jung E.J., Moon H.G., Cho B.I., Jeong C.Y., Joo Y.T., Lee Y.J., et al. Galectin-1 expression in cancer-associated stromal cells correlates tumor invasiveness and tumor progression in breast cancer. Int J Cancer 2007, 120:2331-2338.
    • (2007) Int J Cancer , vol.120 , pp. 2331-2338
    • Jung, E.J.1    Moon, H.G.2    Cho, B.I.3    Jeong, C.Y.4    Joo, Y.T.5    Lee, Y.J.6
  • 46
    • 84862880544 scopus 로고
    • Galectin-1 and galectin-3 expression profiles in classically and alternatively activated human macrophages
    • Novak R., Dabelic S., Dumic J. Galectin-1 and galectin-3 expression profiles in classically and alternatively activated human macrophages. Biochim Biophys Acta 1820, 2012:1383-1390.
    • (1820) Biochim Biophys Acta , vol.2012 , pp. 1383-1390
    • Novak, R.1    Dabelic, S.2    Dumic, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.