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Volumn 137, Issue 4, 1996, Pages 1370-1377

Carbohydrate and protein determinants are involved in thyroglobulin recognition by FRTL 5 cells

Author keywords

[No Author keywords available]

Indexed keywords

N ACETYLGLUCOSAMINE; THYROGLOBULIN; THYROTROPIN;

EID: 0029915210     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.137.4.8625913     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0019579702 scopus 로고
    • Structure of carbohydrate unit A of porcine thyroglobulin
    • Tsuji T, Yamamoto K, Irimura T, Osawa T 1981 Structure of carbohydrate unit A of porcine thyroglobulin. Biochem J 195:691-699
    • (1981) Biochem J , vol.195 , pp. 691-699
    • Tsuji, T.1    Yamamoto, K.2    Irimura, T.3    Osawa, T.4
  • 2
    • 0019580819 scopus 로고
    • The structure of the unit B of porcine thyroglobulin
    • Yamamoto K, Tsuji T, Irimura T, Osawa T 1981 The structure of the unit B of porcine thyroglobulin. Biochem J 195:701-713
    • (1981) Biochem J , vol.195 , pp. 701-713
    • Yamamoto, K.1    Tsuji, T.2    Irimura, T.3    Osawa, T.4
  • 3
    • 0027936075 scopus 로고
    • Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation
    • Kuznetsov G, Chen LB, Nigam SK 1994 Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation. J Biol Chem 269:22990-22995
    • (1994) J Biol Chem , vol.269 , pp. 22990-22995
    • Kuznetsov, G.1    Chen, L.B.2    Nigam, S.K.3
  • 4
    • 0028801931 scopus 로고
    • Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
    • Kim PS, Arvan P 1995 Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J Cell Biol 128:29-38
    • (1995) J Cell Biol , vol.128 , pp. 29-38
    • Kim, P.S.1    Arvan, P.2
  • 5
    • 0024574164 scopus 로고
    • Characterisation of a thyroid sulfotransferase responsible for the 3-O-sulfatation of terminal β-D-galactosyl residues in the N-linked carbohydrate units
    • Kato Y, Spiro RG 1989 Characterisation of a thyroid sulfotransferase responsible for the 3-O-sulfatation of terminal β-D-galactosyl residues in the N-linked carbohydrate units. J Biol Chem 264:3364-3371
    • (1989) J Biol Chem , vol.264 , pp. 3364-3371
    • Kato, Y.1    Spiro, R.G.2
  • 6
    • 0026515190 scopus 로고
    • Modulation of carbohydrate moiety of thyroglobulin by thyrotropin and calcium in Fisher rat thyroid line-5 cells
    • Di Jeso B, Liguoro D, Ferranti P, Marinaccio M, Acquaviva R, Fonnisano S, Consiglio E 1992 Modulation of carbohydrate moiety of thyroglobulin by thyrotropin and calcium in Fisher rat thyroid line-5 cells. J Biol Chem 267:1938-1944
    • (1992) J Biol Chem , vol.267 , pp. 1938-1944
    • Di Jeso, B.1    Liguoro, D.2    Ferranti, P.3    Marinaccio, M.4    Acquaviva, R.5    Fonnisano, S.6    Consiglio, E.7
  • 7
    • 0003038734 scopus 로고
    • Biochemistry of thyroid hormone formation and scretion
    • Greer MA (ed) Raven Press, NY
    • Bjorkman U, Ekholm R 1990 Biochemistry of thyroid hormone formation and scretion. In: Greer MA (ed) The Thyroid Gland. Raven Press, NY, pp 83-125
    • (1990) The Thyroid Gland , pp. 83-125
    • Bjorkman, U.1    Ekholm, R.2
  • 8
    • 0023898857 scopus 로고
    • Monoiodotyrosine formation during thyroglobulin processig in Golgi vesicles
    • Bastiani P, Rognoni JB 1988 Monoiodotyrosine formation during thyroglobulin processig in Golgi vesicles. Cell Biochem Funct 6:149-153
    • (1988) Cell Biochem Funct , vol.6 , pp. 149-153
    • Bastiani, P.1    Rognoni, J.B.2
  • 9
    • 0016815607 scopus 로고
    • Site of iodination in the rat thyroid gland deduced from electron microscopic autoradiographs
    • Ekholm R, Wollman SH 1975 Site of iodination in the rat thyroid gland deduced from electron microscopic autoradiographs. Endocrinology 97:1432-1444
    • (1975) Endocrinology , vol.97 , pp. 1432-1444
    • Ekholm, R.1    Wollman, S.H.2
  • 10
    • 0023645759 scopus 로고
    • The N-acetylglucosamine-specific receptor of the thyroid. Binding characteristics, partial characterization and potential role
    • Miquelis R, Alquier C, Monsigny M 1987 The N-acetylglucosamine-specific receptor of the thyroid. Binding characteristics, partial characterization and potential role. J Biol Chem 262:15291-15298
    • (1987) J Biol Chem , vol.262 , pp. 15291-15298
    • Miquelis, R.1    Alquier, C.2    Monsigny, M.3
  • 11
    • 0019780284 scopus 로고
    • Thyroglobulin interactions with thyroid membranes. Relationship between receptor recognition of N-acetylglucosamine residues and the iodine content of the thyroglobulin preparations
    • Consiglio E, Shifrin S, Yavin Z, Ambesi-Impombato FS, Rail J E, Salvatore G, Kohn LD 1981 Thyroglobulin interactions with thyroid membranes. Relationship between receptor recognition of N-acetylglucosamine residues and the iodine content of the thyroglobulin preparations. J Biol Chem 256:10592-10599
    • (1981) J Biol Chem , vol.256 , pp. 10592-10599
    • Consiglio, E.1    Shifrin, S.2    Yavin, Z.3    Ambesi-Impombato, F.S.4    Rail, J.E.5    Salvatore, G.6    Kohn, L.D.7
  • 12
    • 0029162607 scopus 로고
    • On the relationship between the completion of N-acetyllactosamine units and the iodination of thyroglobulin: A reinvestigation
    • Bastiani P, Papandreou MJ, Blanck O, Fenouillet E, Thibault V, Miquelis R 1995 On the relationship between the completion of N-acetyllactosamine units and the iodination of thyroglobulin: a reinvestigation. Endocrinology 136:4204-4209
    • (1995) Endocrinology , vol.136 , pp. 4204-4209
    • Bastiani, P.1    Papandreou, M.J.2    Blanck, O.3    Fenouillet, E.4    Thibault, V.5    Miquelis, R.6
  • 13
    • 0027395745 scopus 로고
    • The N-acetylglucosamine specific receptor of the thyroid: Purification, further characterization, and expression patterns on normal and pathological glands
    • Thibault V, Blanck O, Courageot J, Pachetti C, Perrin C, de Mascarel A, Miquelis R 1993 The N-acetylglucosamine specific receptor of the thyroid: purification, further characterization, and expression patterns on normal and pathological glands. Endocrinology 132: 468-476
    • (1993) Endocrinology , vol.132 , pp. 468-476
    • Thibault, V.1    Blanck, O.2    Courageot, J.3    Pachetti, C.4    Perrin, C.5    De Mascarel, A.6    Miquelis, R.7
  • 14
    • 0026697878 scopus 로고
    • Endocytosis of thyroglobulin is not mediated by mannose-6-phosphate receptors in thyrocytes. Evidence for low-affinity binding site operating in the uptake of thyroglobulin
    • Lemansky P, Herzog V 1992 Endocytosis of thyroglobulin is not mediated by mannose-6-phosphate receptors in thyrocytes. Evidence for low-affinity binding site operating in the uptake of thyroglobulin. Eur J Biochem 209:111-119
    • (1992) Eur J Biochem , vol.209 , pp. 111-119
    • Lemansky, P.1    Herzog, V.2
  • 15
    • 0027142645 scopus 로고
    • Intracellular routing of GlcNAc-bearing molecules in thyrocytes: Selective recycling through the Golgi apparatus
    • Miquelis R, Courageot J, Jacq A, Blanck O, Perrin C, Bastiani P 1993 Intracellular routing of GlcNAc-bearing molecules in thyrocytes: selective recycling through the Golgi apparatus. J Cell Biol 123:1695-1706
    • (1993) J Cell Biol , vol.123 , pp. 1695-1706
    • Miquelis, R.1    Courageot, J.2    Jacq, A.3    Blanck, O.4    Perrin, C.5    Bastiani, P.6
  • 16
    • 0022977050 scopus 로고
    • Immunochemical evidence for a role of complex carbohydrate chains in thyroglobulin antigenicity
    • Fenouillet E, Fayet G, Hovsepian S, Bahraoui EM, Ronin C 1986 Immunochemical evidence for a role of complex carbohydrate chains in thyroglobulin antigenicity. J Biol Chem 261:15153-15158
    • (1986) J Biol Chem , vol.261 , pp. 15153-15158
    • Fenouillet, E.1    Fayet, G.2    Hovsepian, S.3    Bahraoui, E.M.4    Ronin, C.5
  • 18
    • 0020985674 scopus 로고
    • Specificity of monoclonal antibodies against human thyroglobulin: A comparison with autoimmune antibodies
    • Ruf J, Carayon P, Sarles-Philip N, Kourlisky F, Lissitzky S 1983 Specificity of monoclonal antibodies against human thyroglobulin: a comparison with autoimmune antibodies. EMBO J 2:1821-1826
    • (1983) EMBO J , vol.2 , pp. 1821-1826
    • Ruf, J.1    Carayon, P.2    Sarles-Philip, N.3    Kourlisky, F.4    Lissitzky, S.5
  • 20
    • 0021273667 scopus 로고
    • Iodide transport in a continuous line of cultured cells from rat thyroid
    • Weiss SJ, Philp NJ, Grollman EF 1984 Iodide transport in a continuous line of cultured cells from rat thyroid. Endocrinology 114: 1090-1098
    • (1984) Endocrinology , vol.114 , pp. 1090-1098
    • Weiss, S.J.1    Philp, N.J.2    Grollman, E.F.3
  • 21
    • 0026607261 scopus 로고
    • Hydrogen peroxide generation and its Sregulation in FRTL-5 and porcine thyroid cells
    • Bjorkman U, Ekholm R 1992 Hydrogen peroxide generation and its Sregulation in FRTL-5 and porcine thyroid cells. Endocrinology 130:393-399
    • (1992) Endocrinology , vol.130 , pp. 393-399
    • Bjorkman, U.1    Ekholm, R.2
  • 23
    • 0027093721 scopus 로고
    • TSH-induced galactose incorporation at the NH2 terminus of thyroglobulin secreted by FRTL 5 cells
    • Di Jeso B, Gentile F 1992 TSH-induced galactose incorporation at the NH2 terminus of thyroglobulin secreted by FRTL 5 cells. Biochem Biophys Res Commun 189:1624-1630
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1624-1630
    • Di Jeso, B.1    Gentile, F.2
  • 24
    • 0027537479 scopus 로고
    • Thyrotropin regulation of sialic acid expression in rat thyroid cells
    • Grollman EF, Saji M, Shimura Y, Lau JTY, Ashwell G 1993 Thyrotropin regulation of sialic acid expression in rat thyroid cells. J Biol Chem 268:3604-3609
    • (1993) J Biol Chem , vol.268 , pp. 3604-3609
    • Grollman, E.F.1    Saji, M.2    Shimura, Y.3    Lau, J.T.Y.4    Ashwell, G.5
  • 25
    • 0025187298 scopus 로고
    • A human homologue of the yeast HDEL receptor
    • Lewis MJ, Pelham HRB 1990 A human homologue of the yeast HDEL receptor. Nature 348:162-163
    • (1990) Nature , vol.348 , pp. 162-163
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 26
    • 0027513285 scopus 로고
    • pH-dependent binding of KDEL receptor in vitro
    • Wilson DW, Lewis MJ, Pelham HRB 1993 pH-dependent binding of KDEL receptor in vitro. J Biol Chem 268:7465-7468
    • (1993) J Biol Chem , vol.268 , pp. 7465-7468
    • Wilson, D.W.1    Lewis, M.J.2    Pelham, H.R.B.3
  • 27
    • 0027326627 scopus 로고
    • Mutational analysis of the human KDEL receptor: Distinct structural requirements for Golgi retention, ligand binding and retrograde transport
    • Townsley FM, Wilson DW, Pelham HRB 1993 Mutational analysis of the human KDEL receptor: distinct structural requirements for Golgi retention, ligand binding and retrograde transport. EMBO J 12:2821-2829
    • (1993) EMBO J , vol.12 , pp. 2821-2829
    • Townsley, F.M.1    Wilson, D.W.2    Pelham, H.R.B.3
  • 28
    • 0027439583 scopus 로고
    • Molecular cloning, characterization, subcellular localisation and dynamics of p23, the mammalian KDEL receptor
    • Tang BL, Wong SH, Qi XL, Low SH, Hong W 1993 Molecular cloning, characterization, subcellular localisation and dynamics of p23, the mammalian KDEL receptor. J Cell Biol 120:325-338
    • (1993) J Cell Biol , vol.120 , pp. 325-338
    • Tang, B.L.1    Wong, S.H.2    Qi, X.L.3    Low, S.H.4    Hong, W.5
  • 29
    • 0023237474 scopus 로고
    • Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA
    • Malthiery Y, Lissitzky S 1987 Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA. Eur J Biochem 165:491-498
    • (1987) Eur J Biochem , vol.165 , pp. 491-498
    • Malthiery, Y.1    Lissitzky, S.2
  • 30
    • 0019771513 scopus 로고
    • Binding of thyroglobulin to bovine thyroid membranes. Role of specific amino acids in receptor recognition
    • Shifrin S, Kohn LD 1981 Binding of thyroglobulin to bovine thyroid membranes. Role of specific amino acids in receptor recognition. J Biol Chem 256:10600-10605
    • (1981) J Biol Chem , vol.256 , pp. 10600-10605
    • Shifrin, S.1    Kohn, L.D.2


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