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Volumn 33, Issue 1, 1996, Pages 15-24

IgM polymerization inhibits the Golgi-mediated processing of the μ-chain carboxy-terminal glycans

Author keywords

Glycosylation; IgM; Intracellular transport; Oligomerization; Processing; Reducing agents; Secretion

Indexed keywords

GLYCAN; IMMUNOGLOBULIN M; MANNOSE;

EID: 0029986845     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/0161-5890(95)00132-8     Document Type: Article
Times cited : (42)

References (46)
  • 1
    • 0025146994 scopus 로고
    • Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents
    • Alberini C. M., Bet P., Milstein C. and Sitia R. (1990) Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents. Nature 347, 485-487.
    • (1990) Nature , vol.347 , pp. 485-487
    • Alberini, C.M.1    Bet, P.2    Milstein, C.3    Sitia, R.4
  • 2
    • 0026644841 scopus 로고
    • Degradation of secretory immunoglobulin M in B lymphocytes occurs in a postendoplasmic reticulum compartment and is mediated by a cysteine protease
    • Amitay R., Shachar I., Rabinovich E., Haimovich J. and Bar-Nun S. (1992) Degradation of secretory immunoglobulin M in B lymphocytes occurs in a postendoplasmic reticulum compartment and is mediated by a cysteine protease. J. Biol. Chem. 267, 20694-20700.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20694-20700
    • Amitay, R.1    Shachar, I.2    Rabinovich, E.3    Haimovich, J.4    Bar-Nun, S.5
  • 4
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors on the liver
    • Ashwell G. and Harford J. (1982) Carbohydrate-specific receptors on the liver. A. Rev. Biochem. 51, 531-554.
    • (1982) A. Rev. Biochem. , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 6
    • 0019196213 scopus 로고
    • Structure of the oligosaccharides of mouse immunoglobulin M secreted by the MOPC 104E plasmacytoma
    • Brenckle R. and Kornfeld R. (1980) Structure of the oligosaccharides of mouse immunoglobulin M secreted by the MOPC 104E plasmacytoma. Arch. Biochem. Biophys. 201, 160-173.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 160-173
    • Brenckle, R.1    Kornfeld, R.2
  • 7
    • 0028200169 scopus 로고
    • Mechanism and subcellular localization of secretory IgM polymer assembly
    • Brewer J. W., Randall T. D., Parkhouse R. M. E. and Corley R. B. (1994) Mechanism and subcellular localization of secretory IgM polymer assembly. J. Biol. Chem. 269, 17338-17348.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17338-17348
    • Brewer, J.W.1    Randall, T.D.2    Parkhouse, R.M.E.3    Corley, R.B.4
  • 8
    • 0026688551 scopus 로고
    • Cell-free synthesis of enzymatically active tissue-type plasminogen activator. Protein folding determines the extent of N-linked glycosylation
    • Bulleid N. J., Bassel-Duby R. S., Freedman R. B., Sambrook J. F. and Gething M.-J. H. (1992) Cell-free synthesis of enzymatically active tissue-type plasminogen activator. Protein folding determines the extent of N-linked glycosylation. Biochem. J. 286, 275-280.
    • (1992) Biochem. J. , vol.286 , pp. 275-280
    • Bulleid, N.J.1    Bassel-Duby, R.S.2    Freedman, R.B.3    Sambrook, J.F.4    Gething, M.-J.H.5
  • 9
    • 0023403373 scopus 로고
    • Polymeric immunoglobulin M is secreted by transfectants of non-lymphoid cells in the absence of immunoglobulin J chain
    • Cattaneo A. and Neuberger M. S. (1987) Polymeric immunoglobulin M is secreted by transfectants of non-lymphoid cells in the absence of immunoglobulin J chain. EMBO J. 6, 2753-2758.
    • (1987) EMBO J. , vol.6 , pp. 2753-2758
    • Cattaneo, A.1    Neuberger, M.S.2
  • 10
    • 0018757886 scopus 로고
    • Structure of the high mannose oligosaccharides of a human IgM myeloma protein. I. The major oligosaccharides of the two high mannose glycopeptides
    • Chapman A. and Kornfeld R. (1979a) Structure of the high mannose oligosaccharides of a human IgM myeloma protein. I. The major oligosaccharides of the two high mannose glycopeptides. J. Biol. Chem. 254, 816-823.
    • (1979) J. Biol. Chem. , vol.254 , pp. 816-823
    • Chapman, A.1    Kornfeld, R.2
  • 11
    • 0018395656 scopus 로고
    • Structure of the high mannose oligosaccharides of a human IgM myeloma protein. II. The minor oligosaccharides of high mannose glycopeptide I
    • Chapman A. and Kornfeld R. (1979b) Structure of the high mannose oligosaccharides of a human IgM myeloma protein. II. The minor oligosaccharides of high mannose glycopeptide I. J. Biol. Chem. 254, 824-828.
    • (1979) J. Biol. Chem. , vol.254 , pp. 824-828
    • Chapman, A.1    Kornfeld, R.2
  • 12
    • 0025316165 scopus 로고
    • Differences in glycoprotein complexes associated with IgM and IgD on normal murine B cells potentially enable transduction of different signals
    • Chen J., Stall A. M., Herzenberg L. A. and Herzenberg L. A. (1990) Differences in glycoprotein complexes associated with IgM and IgD on normal murine B cells potentially enable transduction of different signals. EMBO J. 9, 2117-2124.
    • (1990) EMBO J. , vol.9 , pp. 2117-2124
    • Chen, J.1    Stall, A.M.2    Herzenberg, L.A.3    Herzenberg, L.A.4
  • 13
  • 14
    • 0022898398 scopus 로고
    • Influence of the quaternary structure on glycosylation
    • Dahms N. M. and Hart G. W. (1986) Influence of the quaternary structure on glycosylation. J. Biol. Chem. 261, 3186-3196.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3186-3196
    • Dahms, N.M.1    Hart, G.W.2
  • 15
    • 0024436948 scopus 로고
    • Intermolecular disulfide bonding in IgM: Effects of replacing cysteine residues in the μ heavy chain
    • Davis A. C., Roux K. H., Pursey J. and Shulman M. J. (1989a) Intermolecular disulfide bonding in IgM: effects of replacing cysteine residues in the μ heavy chain. EMBO J. 8, 2519-2526.
    • (1989) EMBO J. , vol.8 , pp. 2519-2526
    • Davis, A.C.1    Roux, K.H.2    Pursey, J.3    Shulman, M.J.4
  • 16
    • 0024505096 scopus 로고
    • Differential glycosylation of polymeric and monomeric IgM
    • Davis A. C., Collins C. and Shulman M. J. (1989b) Differential glycosylation of polymeric and monomeric IgM. Mol. Immun. 26, 147-152.
    • (1989) Mol. Immun. , vol.26 , pp. 147-152
    • Davis, A.C.1    Collins, C.2    Shulman, M.J.3
  • 17
    • 0015851495 scopus 로고
    • Biosynthesis of immunoglobulin A (IgA) and immunoglobulin M (IgM) Requirement for J chain and a disulphide exchange enzyme for polymerization
    • Della Corte E. and Parkhouse R. M. E. (1973) Biosynthesis of immunoglobulin A (IgA) and immunoglobulin M (IgM) Requirement for J chain and a disulphide exchange enzyme for polymerization. Biochem. J. 136, 597-606.
    • (1973) Biochem. J. , vol.136 , pp. 597-606
    • Della Corte, E.1    Parkhouse, R.M.E.2
  • 18
    • 0022533179 scopus 로고
    • The position of the oligosaccharide side-chains of phytohemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Golgi
    • Faye L., Sturm A., Bollini R., Vitale A. and Chrispeels M. J. (1986) The position of the oligosaccharide side-chains of phytohemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Golgi. Eur. J. Biochem. 158, 655-661.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 655-661
    • Faye, L.1    Sturm, A.2    Bollini, R.3    Vitale, A.4    Chrispeels, M.J.5
  • 20
    • 0022869333 scopus 로고
    • Immunoglobulin flexibility and complement activation
    • Feinstein A., Richardson N. and Taussig M. J. (1986) Immunoglobulin flexibility and complement activation. Immun. Today 7, 169-174.
    • (1986) Immun. Today , vol.7 , pp. 169-174
    • Feinstein, A.1    Richardson, N.2    Taussig, M.J.3
  • 21
    • 0027440769 scopus 로고
    • Quality control of ER synthesized proteins: An exposed thiol group as a three-way switch mediating assembly, retention and degradation
    • Fra A. M., Fagioli C., Finazzi D., Sitia R. and Alberini C. (1993) Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation. EMBO J. 12, 4755-4761.
    • (1993) EMBO J. , vol.12 , pp. 4755-4761
    • Fra, A.M.1    Fagioli, C.2    Finazzi, D.3    Sitia, R.4    Alberini, C.5
  • 22
    • 0027721032 scopus 로고
    • The endoplasmic reticulum as a site of protein degradation
    • Endoplasmic Reticulum (Edited by Borgese N. and Harris J. R.). Plenum Press, New York
    • Fra A. M. and Sitia R. (1993) The endoplasmic reticulum as a site of protein degradation. In Endoplasmic Reticulum (Edited by Borgese N. and Harris J. R.). Subcell. Biochem. 21, 143-168. Plenum Press, New York.
    • (1993) Subcell. Biochem. , vol.21 , pp. 143-168
    • Fra, A.M.1    Sitia, R.2
  • 23
    • 0017874586 scopus 로고
    • Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a, 6a-diphenylglycorulyl
    • Fraker P. J. and Speck J. C. Jr (1978) Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a, 6a-diphenylglycorulyl. Biochem. Biophys. Res. Commun. 80, 849-857.
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 849-857
    • Fraker, P.J.1    Speck J.C., Jr.2
  • 24
    • 0028168233 scopus 로고
    • The efficiency of cysteine-mediated intracellular retention determines the differential fate of secretory IgA and IgM in B and plasma cells
    • Guenzi S., Fra A. M., Sparvoli A., Bet P., Rocco M. and Sitia R. (1994) The efficiency of cysteine-mediated intracellular retention determines the differential fate of secretory IgA and IgM in B and plasma cells. Eur. J. Immun. 24, 2477-2482.
    • (1994) Eur. J. Immun. , vol.24 , pp. 2477-2482
    • Guenzi, S.1    Fra, A.M.2    Sparvoli, A.3    Bet, P.4    Rocco, M.5    Sitia, R.6
  • 25
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond C. and Helenius A. (1994) Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126, 41-52.
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 26
    • 0020534870 scopus 로고
    • Selective cleavage by endo-β-N-acetylglucosaminidase H at individual glycosylation sites of Sindbis virion envelope glycoproteins
    • Hsieh P., Rosner M. R. and Robbins P. W. (1983) Selective cleavage by endo-β-N-acetylglucosaminidase H at individual glycosylation sites of Sindbis virion envelope glycoproteins. J. Biol. Chem. 258, 2555-2561.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2555-2561
    • Hsieh, P.1    Rosner, M.R.2    Robbins, P.W.3
  • 27
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R. and Kornfeld S. (1985) Assembly of asparagine-linked oligosaccharides. A. Rev. Biochem. 54, 631-664.
    • (1985) A. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 29
    • 0021092716 scopus 로고
    • Expression and regulation of immunoglobulin heavy chain gene transfected into lymphoid cells
    • Neuberger M. S. (1983) Expression and regulation of immunoglobulin heavy chain gene transfected into lymphoid cells. EMBO J. 2, 1373-1378.
    • (1983) EMBO J. , vol.2 , pp. 1373-1378
    • Neuberger, M.S.1
  • 30
    • 0027472941 scopus 로고
    • Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells
    • Nilsson T., Pypaert M., Hoe M. H., Slusarewicz P., Berger E. G. and Warren G. (1993) Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells. J. Cell Biol. 120, 5-13.
    • (1993) J. Cell Biol. , vol.120 , pp. 5-13
    • Nilsson, T.1    Pypaert, M.2    Hoe, M.H.3    Slusarewicz, P.4    Berger, E.G.5    Warren, G.6
  • 31
    • 0022908968 scopus 로고
    • Computer models of the human immunoglobulins. Shape and segmental flexibility
    • Pumphrey R. (1986) Computer models of the human immunoglobulins. Shape and segmental flexibility. Immun. Today 7, 174-178.
    • (1986) Immun. Today , vol.7 , pp. 174-178
    • Pumphrey, R.1
  • 32
    • 0026597551 scopus 로고
    • J chain synthesis and secretion of hexameric IgM is differentially regulated by lipopolysaccharide and interleukin 5
    • Randall T. D., Parkhouse R. M. E. and Corley R. B. (1992) J chain synthesis and secretion of hexameric IgM is differentially regulated by lipopolysaccharide and interleukin 5. Proc. natn. Acad. Sci. USA 89, 962-966.
    • (1992) Proc. Natn. Acad. Sci. USA , vol.89 , pp. 962-966
    • Randall, T.D.1    Parkhouse, R.M.E.2    Corley, R.B.3
  • 33
    • 0020037889 scopus 로고
    • Immunocytochemical localization of galactosyl-transferase in HeLa cells: Codistribution with thiamine pyrophosphatase in trans-Golgi cysternae
    • Roth J. and Berger E. G. (1982) Immunocytochemical localization of galactosyl-transferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cysternae. J. Cell Biol. 92, 223-229.
    • (1982) J. Cell Biol. , vol.92 , pp. 223-229
    • Roth, J.1    Berger, E.G.2
  • 34
    • 0026713211 scopus 로고
    • The spectrum of incomplete N-linked oligosaccharides synthesized by endothelial cells in the presence of brefeldin A
    • Sampath D., Varki A. and Freeze H. H. (1992) The spectrum of incomplete N-linked oligosaccharides synthesized by endothelial cells in the presence of brefeldin A. J. Biol. Chem. 267, 4440-4455.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4440-4455
    • Sampath, D.1    Varki, A.2    Freeze, H.H.3
  • 35
    • 0026486823 scopus 로고
    • Polymerization of secretory IgM in B lymphocytes is prevented by a prior targeting to a degradation pathway
    • Shachar I., Amitay R., Rabinovich E., Haimovich J. and Bar-Nun S. (1992) Polymerization of secretory IgM in B lymphocytes is prevented by a prior targeting to a degradation pathway. J. Biol. Chem. 267, 24241-24247.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24241-24247
    • Shachar, I.1    Amitay, R.2    Rabinovich, E.3    Haimovich, J.4    Bar-Nun, S.5
  • 36
    • 0028104975 scopus 로고
    • Thiol-reducing agents and calcium perturbants alter intracellular sorting of immunoglobulin M
    • Shachar I., Rabinovich E., Kerem A. and Bar-Nun S. (1994) Thiol-reducing agents and calcium perturbants alter intracellular sorting of immunoglobulin M. J. Biol. Chem. 269, 27,344-27,350.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27344-27350
    • Shachar, I.1    Rabinovich, E.2    Kerem, A.3    Bar-Nun, S.4
  • 37
    • 85030193733 scopus 로고
    • Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb
    • Shibuya N., Goldstein I. J., VanDamme E. J. M. and Peumans W. J. (1988) Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb. J. Biol. Chem. 262, 1596-1601.
    • (1988) J. Biol. Chem. , vol.262 , pp. 1596-1601
    • Shibuya, N.1    Goldstein, I.J.2    VanDamme, E.J.M.3    Peumans, W.J.4
  • 38
    • 0023661332 scopus 로고
    • Regulation of membrane IgM expression in secretory B cells: Translational and post-translational events
    • Sitia R., Neuberger M. S. and Milstein C. (1987) Regulation of membrane IgM expression in secretory B cells: translational and post-translational events. EMBO J. 6, 3969-3977.
    • (1987) EMBO J. , vol.6 , pp. 3969-3977
    • Sitia, R.1    Neuberger, M.S.2    Milstein, C.3
  • 40
    • 0026091730 scopus 로고
    • Substitution of asparagine for serine-406 of the immunoglobulin μ heavy chains alters glycosylation at asparagine-402
    • Sun W., Xiong J. and Shulman M. J. (1991) Substitution of asparagine for serine-406 of the immunoglobulin μ heavy chains alters glycosylation at asparagine-402. Biochem. Biophys. Res. Commun. 179, 1627-1634.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1627-1634
    • Sun, W.1    Xiong, J.2    Shulman, M.J.3
  • 41
    • 85030190623 scopus 로고
    • Plasma cell immunoglobulin M molecules. Their biosynthesis, assembly, and intracellular transport
    • Tartakoff A. and Vassalli P. (1979) Plasma cell immunoglobulin M molecules. Their biosynthesis, assembly, and intracellular transport. J. Cell Biol. 115, 1225-1236.
    • (1979) J. Cell Biol. , vol.115 , pp. 1225-1236
    • Tartakoff, A.1    Vassalli, P.2
  • 42
    • 0020522151 scopus 로고
    • Glycoprotein biosynthesis in yeast. Protein conformation affects processing of high mannose oligosaccharides on carboxypeptidase Y and invertase
    • Trimble R. B., Maley F. and Chu F. K. (1983) Glycoprotein biosynthesis in yeast. Protein conformation affects processing of high mannose oligosaccharides on carboxypeptidase Y and invertase. J. Biol. Chem. 258, 2562-2567.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2562-2567
    • Trimble, R.B.1    Maley, F.2    Chu, F.K.3
  • 43
    • 0026347810 scopus 로고
    • Russell bodies: A general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum
    • Valetti C., Grossi C. E., Milstein C. and Sitia R. (1991) Russell Bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum. J. Cell Biol. 115, 983-994.
    • (1991) J. Cell Biol. , vol.115 , pp. 983-994
    • Valetti, C.1    Grossi, C.E.2    Milstein, C.3    Sitia, R.4
  • 44
    • 85030195812 scopus 로고
    • The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated intracellular retention does not take place in or beyond the Golgi
    • Valetti C. and Sitia R. (1994) The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated intracellular retention does not take place in or beyond the Golgi. J. Cell Biol. 115, 983-994.
    • (1994) J. Cell Biol. , vol.115 , pp. 983-994
    • Valetti, C.1    Sitia, R.2
  • 45
    • 0025916889 scopus 로고
    • The B-cell antigen receptor of the five immunoglobulin classes
    • Venkitaraman A. R., Williams G. T., Dariavach P. and Neuberger M. S. (1991) The B-cell antigen receptor of the five immunoglobulin classes. Nature 352, 777-781.
    • (1991) Nature , vol.352 , pp. 777-781
    • Venkitaraman, A.R.1    Williams, G.T.2    Dariavach, P.3    Neuberger, M.S.4


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