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Volumn , Issue , 2013, Pages

Quantifying changes in the cellular thiol-disulfide status during differentiation of B cells into antibody-secreting plasma cells

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; IMMUNOGLOBULIN M; THIOL;

EID: 84885457296     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2013/898563     Document Type: Article
Times cited : (5)

References (36)
  • 1
    • 3543095148 scopus 로고    scopus 로고
    • Monitoring disulfide bond formation in the eukaryotic cytosol
    • DOI 10.1083/jcb.200402120
    • Østergaard H., Tachibana C., Winther J. R., Monitoring disulfide bond formation in the eukaryotic cytosol. Journal of Cell Biology 2004 166 3 337 345 2-s2.0-3543095148 10.1083/jcb.200402120 (Pubitemid 39031237)
    • (2004) Journal of Cell Biology , vol.166 , Issue.3 , pp. 337-345
    • Ostergaard, H.1    Tachibana, C.2    Winther, J.R.3
  • 2
    • 2542455473 scopus 로고    scopus 로고
    • Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators
    • DOI 10.1074/jbc.M312847200
    • Dooley C. T., Dore T. M., Hanson G. T., Jackson W. C., Remington S. J., Tsien R. Y., Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators. The Journal of Biological Chemistry 2004 279 21 22284 22293 2-s2.0-2542455473 10.1074/jbc.M312847200 (Pubitemid 38679425)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22284-22293
    • Dooley, C.T.1    Dore, T.M.2    Hanson, G.T.3    Jackson, W.C.4    Remington, S.J.5    Tsien, R.Y.6
  • 4
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • 2-s2.0-0026698060
    • Hwang C., Sinskey A. J., Lodish H. F., Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992 257 5076 1496 1502 2-s2.0-0026698060
    • (1992) Science , vol.257 , Issue.5076 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 5
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • 2-s2.0-0026508087 10.1038/356260a0
    • Braakman I., Helenius J., Helenius A., Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 1992 356 6366 260 262 2-s2.0-0026508087 10.1038/356260a0
    • (1992) Nature , vol.356 , Issue.6366 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 6
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • 2-s2.0-0026563680 10.1083/jcb.117.3.505
    • Marquardt T., Helenius A., Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. Journal of Cell Biology 1992 117 3 505 513 2-s2.0-0026563680 10.1083/jcb.117.3.505
    • (1992) Journal of Cell Biology , vol.117 , Issue.3 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 7
    • 36148967364 scopus 로고    scopus 로고
    • In vivo reduction-oxidation state of protein disulfide isomerase: The two active sites independently occur in the reduced and oxidized forms
    • DOI 10.1089/ars.2007.1837
    • Appenzeller-Herzog C., Ellgaard L., In vivo reduction-oxidation state of protein disulfide isomerase: the two active sites independently occur in the reduced and oxidized forms. Antioxidants and Redox Signaling 2008 10 1 55 64 2-s2.0-36148967364 10.1089/ars.2007.1837 (Pubitemid 350115985)
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.1 , pp. 55-64
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 8
    • 0023720121 scopus 로고
    • Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes
    • 2-s2.0-0023720121
    • Bulleid N. J., Freedman R. B., Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature 1988 335 6191 649 651 2-s2.0-0023720121
    • (1988) Nature , vol.335 , Issue.6191 , pp. 649-651
    • Bulleid, N.J.1    Freedman, R.B.2
  • 10
    • 80052372197 scopus 로고    scopus 로고
    • Multiple ways to make disulfides
    • 2-s2.0-80052372197 10.1016/j.tibs.2011.05.004
    • Bulleid N. J., Ellgaard L., Multiple ways to make disulfides. Trends in Biochemical Sciences 2011 36 9 485 492 2-s2.0-80052372197 10.1016/j.tibs.2011. 05.004
    • (2011) Trends in Biochemical Sciences , vol.36 , Issue.9 , pp. 485-492
    • Bulleid, N.J.1    Ellgaard, L.2
  • 11
    • 84875470472 scopus 로고    scopus 로고
    • Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
    • 10.1098/rstb.2011.0403, ARTICLE 0403
    • Benham A. M., van Lith M., Sitia R., Braakman I., Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum. Philosophical Transactions of the Royal Society B 2013 368 1617, article 0403 10.1098/rstb.2011.0403
    • (2013) Philosophical Transactions of the Royal Society B , vol.368 , pp. 1617
    • Benham, A.M.1    Van Lith, M.2    Sitia, R.3    Braakman, I.4
  • 12
    • 0025291580 scopus 로고
    • Membrane biogenesis during B cell differentiation: Most endoplasmic reticulum proteins are expressed coordinately
    • DOI 10.1083/jcb.110.5.1501
    • Wiest D. L., Burkhardt J. K., Hester S., Hortsch M., Meyer D. I., Argon Y., Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately. Journal of Cell Biology 1990 110 5 1501 1511 2-s2.0-0025291580 10.1083/jcb.110.5.1501 (Pubitemid 20169486)
    • (1990) Journal of Cell Biology , vol.110 , Issue.5 , pp. 1501-1511
    • Wiest, D.L.1    Burkhardt, J.K.2    Hester, S.3    Hortsch, M.4    Meyer, D.I.5    Argon, Y.6
  • 13
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • DOI 10.1016/S1074-7613(03)00024-4
    • van Anken E., Romijn E. P., Maggioni C., Mezghrani A., Sitia R., Braakman I., Heck A. J. R., Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 2003 18 2 243 253 2-s2.0-0037332128 10.1016/S1074-7613(03)00024-4 (Pubitemid 36262999)
    • (2003) Immunity , vol.18 , Issue.2 , pp. 243-253
    • Van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.R.7
  • 14
    • 26844511378 scopus 로고    scopus 로고
    • Expression clustering reveals detailed co-expression patterns of functionally related proteins during B cell differentiation: A proteomic study using a combination of one-dimensional gel electrophoresis, LC-MS/MS, and stable isotope labeling by amino acids in cell culture (SILAC)
    • DOI 10.1074/mcp.M500123-MCP200
    • Romijn E. P., Christis C., Wieffer M., Gouw J. W., Fullaondo A., van der Sluijs P., Braakman I., Heck A. J. R., Expression clustering reveals detailed co-expression patterns of functionally related proteins during B cell differentiation: a proteomic study using a combination of one-dimensional gel electrophoresis, LC-MS/MS, and stable isotope labeling by amino acids in cell culture (SILAC). Molecular and Cellular Proteomics 2005 4 9 1297 1310 2-s2.0-26844511378 10.1074/mcp.M500123-MCP200 (Pubitemid 41448717)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1297-1310
    • Romijn, E.P.1    Christis, C.2    Wieffer, M.3    Gouw, J.W.4    Fullaondo, A.5    Van Der Sluijs, P.6    Braakman, I.7    Heck, A.J.R.8
  • 15
    • 0028200169 scopus 로고
    • Mechanism and subcellular localization of secretory IgM polymer assembly
    • Brewer J. W., Randall T. D., Parkhouse R. M. E., Corley R. B., Mechanism and subcellular localization of secretory IgM polymer assembly. The Journal of Biological Chemistry 1994 269 25 17338 17348 2-s2.0-0028200169 (Pubitemid 24204062)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.25 , pp. 17338-17348
    • Brewer, J.W.1    Randall, T.D.2    Parkhouse, R.M.E.3    Corley, R.B.4
  • 17
    • 69949093360 scopus 로고    scopus 로고
    • An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations
    • 2-s2.0-69949093360 10.1016/j.ab.2009.07.051
    • Hansen R. E., Winther J. R., An introduction to methods for analyzing thiols and disulfides: reactions, reagents, and practical considerations. Analytical Biochemistry 2009 394 2 147 158 2-s2.0-69949093360 10.1016/j.ab.2009.07.051
    • (2009) Analytical Biochemistry , vol.394 , Issue.2 , pp. 147-158
    • Hansen, R.E.1    Winther, J.R.2
  • 18
    • 33847405272 scopus 로고    scopus 로고
    • Quantification of protein thiols and dithiols in the picomolar range using sodium borohydride and 4,4′-dithiodipyridine
    • DOI 10.1016/j.ab.2007.01.002, PII S0003269707000061
    • Hansen R. E., Østergaard H., Nørgaard P., Winther J. R., Quantification of protein thiols and dithiols in the picomolar range using sodium borohydride and 4,4′-dithiodipyridine. Analytical Biochemistry 2007 363 1 77 82 2-s2.0-33847405272 10.1016/j.ab.2007.01.002 (Pubitemid 46348975)
    • (2007) Analytical Biochemistry , vol.363 , Issue.1 , pp. 77-82
    • Hansen, R.E.1    Ostergaard, H.2    Norgaard, P.3    Winther, J.R.4
  • 19
    • 0023268505 scopus 로고
    • + clones may be induced by lipopolysaccharide to both IgM secretion and isotype switching
    • DOI 10.1002/eji.1830170419
    • + clones may be induced by lipopolysaccharide to both IgM secretion and isotype switching. European Journal of Immunology 1987 17 4 555 562 2-s2.0-0023268505 (Pubitemid 17094156)
    • (1987) European Journal of Immunology , vol.17 , Issue.4 , pp. 555-562
    • Alberini, C.1    Biassoni, R.2    DeAmbrosis, S.3
  • 22
    • 41449111412 scopus 로고    scopus 로고
    • Building and operating an antibody factory: Redox control during B to plasma cell terminal differentiation
    • 2-s2.0-41449111412 10.1016/j.bbamcr.2008.01.003
    • Masciarelli S., Sitia R., Building and operating an antibody factory: redox control during B to plasma cell terminal differentiation. Biochimica et Biophysica Acta 2008 1783 4 578 588 2-s2.0-41449111412 10.1016/j.bbamcr.2008.01. 003
    • (2008) Biochimica et Biophysica Acta , vol.1783 , Issue.4 , pp. 578-588
    • Masciarelli, S.1    Sitia, R.2
  • 23
    • 31344438651 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the making of a professional secretory cell
    • DOI 10.1080/10409230500315352
    • van Anken E., Braakman I., Endoplasmic reticulum stress and the making of a professional secretory cell. Critical Reviews in Biochemistry and Molecular Biology 2005 40 5 269 283 2-s2.0-31344438651 10.1080/10409230500315352 (Pubitemid 43142394)
    • (2005) Critical Reviews in Biochemistry and Molecular Biology , vol.40 , Issue.5 , pp. 269-283
    • Van Anken, E.1    Braakman, I.2
  • 24
    • 77953153048 scopus 로고    scopus 로고
    • Regulation of basal cellular physiology by the homeostatic unfolded protein response
    • 2-s2.0-77953153048 10.1083/jcb.201003138
    • Rutkowski D. T., Hegde R. S., Regulation of basal cellular physiology by the homeostatic unfolded protein response. Journal of Cell Biology 2010 189 5 783 794 2-s2.0-77953153048 10.1083/jcb.201003138
    • (2010) Journal of Cell Biology , vol.189 , Issue.5 , pp. 783-794
    • Rutkowski, D.T.1    Hegde, R.S.2
  • 25
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • 2-s2.0-82255173966 10.1126/science.1209038
    • Walter P., Ron D., The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011 334 6059 1081 1086 2-s2.0-82255173966 10.1126/science.1209038
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 26
    • 0037385313 scopus 로고    scopus 로고
    • Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-I
    • DOI 10.1038/ni907
    • Iwakoshi N. N., Lee A.-H., Vallabhajosyula P., Otipoby K. L., Rajewsky K., Glimcher L. H., Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-I. Nature Immunology 2003 4 4 321 329 2-s2.0-0037385313 10.1038/ni907 (Pubitemid 36432313)
    • (2003) Nature Immunology , vol.4 , Issue.4 , pp. 321-329
    • Iwakoshi, N.N.1    Lee, A.-H.2    Vallabhajosyula, P.3    Otipoby, K.L.4    Rajewsky, K.5    Glimcher, L.H.6
  • 28
    • 33645784167 scopus 로고    scopus 로고
    • The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress
    • 2-s2.0-33645784167 10.1038/sj.embor.7400645
    • Chakravarthi S., Jessop C. E., Bulleid N. J., The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress. EMBO Reports 2006 7 3 271 275 2-s2.0-33645784167 10.1038/sj.embor.7400645
    • (2006) EMBO Reports , vol.7 , Issue.3 , pp. 271-275
    • Chakravarthi, S.1    Jessop, C.E.2    Bulleid, N.J.3
  • 29
    • 11244319355 scopus 로고    scopus 로고
    • Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells
    • DOI 10.1074/jbc.M411409200
    • Jessop C. E., Bulleid N. J., Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. The Journal of Biological Chemistry 2004 279 53 55341 55347 2-s2.0-11244319355 10.1074/jbc.M411409200 (Pubitemid 40066532)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55341-55347
    • Jessop, C.E.1    Bulleid, N.J.2
  • 31
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • Cuozzo J. W., Kaiser C. A., Competition between glutathione and protein thiols for disulphide-bond formation. Nature Cell Biology 1999 1 3 130 135 2-s2.0-0033163758 (Pubitemid 129656016)
    • (1999) Nature Cell Biology , vol.1 , Issue.3 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 32
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of Cellular Disulfide-Bond Formation and the ER Redox Environment by Feedback Regulation of Ero1
    • DOI 10.1016/j.cell.2007.02.039, PII S009286740700325X
    • Sevier C. S., Qu H., Heldman N., Gross E., Fass D., Kaiser C. A., Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 2007 129 2 333 344 2-s2.0-34147126077 10.1016/j.cell.2007.02.039 (Pubitemid 46574965)
    • (2007) Cell , vol.129 , Issue.2 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6
  • 33
    • 1242294484 scopus 로고    scopus 로고
    • A Major Fraction of Endoplasmic Reticulum-located Glutathione Is Present as Mixed Disulfides with Protein
    • DOI 10.1074/jbc.M304951200
    • Bass R., Ruddock L. W., Klappa P., Freedman R. B., A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. The Journal of Biological Chemistry 2004 279 7 5257 5262 2-s2.0-1242294484 10.1074/jbc.M304951200 (Pubitemid 38220545)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4
  • 35
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • 2-s2.0-0029065402 10.1016/0076-6879(95)51107-5
    • Gilbert H. F., Thiol/disulfide exchange equilibria and disulfide bond stability. Methods in Enzymology 1995 251 8 28 2-s2.0-0029065402 10.1016/0076-6879(95)51107-5
    • (1995) Methods in Enzymology , vol.251 , pp. 8-28
    • Gilbert, H.F.1


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