메뉴 건너뛰기




Volumn 138, Issue 1, 1997, Pages 92-100

Expression of biologically active human thyrotropin (hTSH) in a baculovirus system: Effect of insect cell glycosylation on hTSH activity in vitro and in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; CYCLIC AMP; GLYCOPROTEIN; THYROTROPIN; THYROTROPIN RECEPTOR;

EID: 0031014551     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.138.1.4897     Document Type: Article
Times cited : (50)

References (49)
  • 1
    • 0019729482 scopus 로고
    • Glycoprotein hormones: Structure and function
    • Pierce JG, Parsons TF 1981 Glycoprotein hormones: structure and function. Annu Rev Biochem 50:465-495
    • (1981) Annu Rev Biochem , vol.50 , pp. 465-495
    • Pierce, J.G.1    Parsons, T.F.2
  • 3
    • 0002764888 scopus 로고
    • Biosynthesis, cell biology, and bioactivity of thyroid stimulating hormone
    • Magner JA 1994 Biosynthesis, cell biology, and bioactivity of thyroid stimulating hormone. Endocr Rev Monographs 3:55-60
    • (1994) Endocr Rev Monographs , vol.3 , pp. 55-60
    • Magner, J.A.1
  • 4
    • 0026743033 scopus 로고
    • The thyrotropin receptor and the regulation of thyrocyte function and growth
    • Vassart G, Dumont JE 1992 The thyrotropin receptor and the regulation of thyrocyte function and growth. Endocr Rev 13:596-611
    • (1992) Endocr Rev , vol.13 , pp. 596-611
    • Vassart, G.1    Dumont, J.E.2
  • 5
    • 0027158153 scopus 로고
    • The Lutropin/Choriogonadotropin receptor . . . 4 years later
    • Segaloff DL, Ascoli M 1993 The Lutropin/Choriogonadotropin receptor . . . 4 years later. Endocr Rev 14:324-347
    • (1993) Endocr Rev , vol.14 , pp. 324-347
    • Segaloff, D.L.1    Ascoli, M.2
  • 8
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA 1994 Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein. Structure 2:545-558
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 10
    • 0030272080 scopus 로고    scopus 로고
    • Structure-function studies of human TSH: New advances in the design of glycoprotein hormone analogs
    • Szkudlinski MW, Grossmann M, Weintraub BD Structure-function studies of human TSH: new advances in the design of glycoprotein hormone analogs. Trends Endocrinol Metab 7:277-286
    • Trends Endocrinol Metab , vol.7 , pp. 277-286
    • Szkudlinski, M.W.1    Grossmann, M.2    Weintraub, B.D.3
  • 11
    • 0001641561 scopus 로고
    • The glycoprotein hormone family: Structure and function of the carbohydrate chains
    • Montreuil J, Vliegenhart JFG, Schachter H (eds) Elsevier Science BV, Amsterdam, The Netherlands
    • Bielinska M, Boime I 1995 The glycoprotein hormone family: structure and function of the carbohydrate chains. In: Montreuil J, Vliegenhart JFG, Schachter H (eds) Glycoproteins. Elsevier Science BV, Amsterdam, The Netherlands, pp 167-174
    • (1995) Glycoproteins , pp. 167-174
    • Bielinska, M.1    Boime, I.2
  • 12
    • 0028890259 scopus 로고
    • Glycoprotein hormones: Glycobiology of gonadotropins, thyrotropin and free a subunit
    • Thotakura NR, Blithe DL 1995 Glycoprotein hormones: glycobiology of gonadotropins, thyrotropin and free a subunit. Glycobiology 5:3-10
    • (1995) Glycobiology , vol.5 , pp. 3-10
    • Thotakura, N.R.1    Blithe, D.L.2
  • 13
    • 0029977263 scopus 로고    scopus 로고
    • Oligosaccharides containing 1,4-linked N- acetylgalactosamine, a paradigm for protein-specific glycosylation
    • Manzella SM, Hooper LV, Baenziger JU 1996 Oligosaccharides containing 1,4-linked N- acetylgalactosamine, a paradigm for protein-specific glycosylation. J Biol Chem 271:12117-12120
    • (1996) J Biol Chem , vol.271 , pp. 12117-12120
    • Manzella, S.M.1    Hooper, L.V.2    Baenziger, J.U.3
  • 14
    • 0013684298 scopus 로고
    • Biological and molecular approaches to modify oligosaccharides: Analysis of glycosylation function in human choriogonadotropin
    • Roberts DD, Mechan RP (eds) Academic Press, San Diego
    • Bahl OP, Thotakura NR, Chen WY 1993 Biological and molecular approaches to modify oligosaccharides: analysis of glycosylation function in human choriogonadotropin. In: Roberts DD, Mechan RP (eds) Cell surface and extracellular glycoconjugates. Academic Press, San Diego, pp 245-271
    • (1993) Cell Surface and Extracellular Glycoconjugates , pp. 245-271
    • Bahl, O.P.1    Thotakura, N.R.2    Chen, W.Y.3
  • 15
    • 0025909605 scopus 로고
    • Carbohydrate variant of the recombinant β-subunit of human choriogonadotropin expressed in baculovirus expression system
    • Chen W, Shen QY, Bahl OP 1991 Carbohydrate variant of the recombinant β-subunit of human choriogonadotropin expressed in baculovirus expression system. J Biol Chem 266:4081-4087
    • (1991) J Biol Chem , vol.266 , pp. 4081-4087
    • Chen, W.1    Shen, Q.Y.2    Bahl, O.P.3
  • 16
    • 0025832629 scopus 로고
    • Recombinant carbohydrate variant of human choriogonadotropin β subunit des C-terminal (115-145)
    • Chen W, Bahl OP 1991 Recombinant carbohydrate variant of human choriogonadotropin β subunit des C-terminal (115-145). J Biol Chem 266:6246-6251
    • (1991) J Biol Chem , vol.266 , pp. 6246-6251
    • Chen, W.1    Bahl, O.P.2
  • 18
    • 0028882196 scopus 로고
    • Functional expression of yoked human chorionic gonadotropin in baculovirus-infected insect cells
    • Narayan P, Wu C, Puett D 1995 Functional expression of yoked human chorionic gonadotropin in baculovirus-infected insect cells. Mol Endocrinol 9:1720-1726
    • (1995) Mol Endocrinol , vol.9 , pp. 1720-1726
    • Narayan, P.1    Wu, C.2    Puett, D.3
  • 20
    • 0026776964 scopus 로고
    • Mutations of the human thyrotropin-β subunit glycosylation site reduce thyrotropin synthesis independent of changes in glycosylation status
    • Lash RW, Desai RK, Zimmermann CA, Flack MR, Yoshida T, Wondisford FE, Weintraub BD 1992 Mutations of the human thyrotropin-β subunit glycosylation site reduce thyrotropin synthesis independent of changes in glycosylation status. J Endocrinol Invest 15:225-263
    • (1992) J Endocrinol Invest , vol.15 , pp. 225-263
    • Lash, R.W.1    Desai, R.K.2    Zimmermann, C.A.3    Flack, M.R.4    Yoshida, T.5    Wondisford, F.E.6    Weintraub, B.D.7
  • 21
    • 0029166316 scopus 로고
    • Recombinant TSH containing a β-subunit chimera with the human CG-β carboxy- terminus is biologically active, with a prolonged halt-life: Role of carbohydrate in bioactivity and metabolic clearance
    • Joshi L, Murata Y, Wondisford FE, Szkudlinski MW, Desai R, Weintraub BD 1995 Recombinant TSH containing a β-subunit chimera with the human CG-β carboxy- terminus is biologically active, with a prolonged halt-life: role of carbohydrate in bioactivity and metabolic clearance. Endocrinology 136:3839-3848
    • (1995) Endocrinology , vol.136 , pp. 3839-3848
    • Joshi, L.1    Murata, Y.2    Wondisford, F.E.3    Szkudlinski, M.W.4    Desai, R.5    Weintraub, B.D.6
  • 22
    • 0028805384 scopus 로고
    • Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites: Characterization of a novel role tor the oligosaccharides in the in vitro and in vivo bioactivity
    • Grossmann M, Szkudlinski MW, Tropea JE, Bishop LA, Thotakura NR, Schofield PR Weintraub BD 1995 Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites: characterization of a novel role tor the oligosaccharides in the in vitro and in vivo bioactivity. J Biol Chem 270:29378-29385
    • (1995) J Biol Chem , vol.270 , pp. 29378-29385
    • Grossmann, M.1    Szkudlinski, M.W.2    Tropea, J.E.3    Bishop, L.A.4    Thotakura, N.R.5    Schofield, P.R.6    Weintraub, B.D.7
  • 23
    • 0027378859 scopus 로고
    • Baculovirus system for the expression of human gene products
    • Luckow VA 1993 Baculovirus system for the expression of human gene products. Curr Opin Biotechnol 4:564-572
    • (1993) Curr Opin Biotechnol , vol.4 , pp. 564-572
    • Luckow, V.A.1
  • 24
    • 0027651179 scopus 로고
    • The use of baculoviruses as expression vectors
    • Kidd M, Emery VC 1993 The use of baculoviruses as expression vectors. Appl Biochem Biotech 42:137-155
    • (1993) Appl Biochem Biotech , vol.42 , pp. 137-155
    • Kidd, M.1    Emery, V.C.2
  • 25
    • 0000383273 scopus 로고
    • Protein glycosylation in insect cells
    • Montreuil J, Vliegenhart JFG Schachter H (eds) Elsevier Science BV, Amsterdam, The Netherlands
    • Maerz L, Altmann F, Staudacher E, Kubelka V 1995 Protein glycosylation in insect cells. In: Montreuil J, Vliegenhart JFG Schachter H (eds) Glycoproteins. Elsevier Science BV, Amsterdam, The Netherlands pp 543-563
    • (1995) Glycoproteins , pp. 543-563
    • Maerz, L.1    Altmann, F.2    Staudacher, E.3    Kubelka, V.4
  • 28
    • 0027517557 scopus 로고
    • Purification and characterization of recombinant human thyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: The role of sialylation and sulfation in TSH bioactivity
    • Szkudlinski MW, Thotakura NR, Bucci I, Joshi LR, Tsai A, East-Palmer J, Shiloach J, Weintraub BD 1993 Purification and characterization of recombinant human thyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: the role of sialylation and sulfation in TSH bioactivity. Endocrinology 133:1490-1503
    • (1993) Endocrinology , vol.133 , pp. 1490-1503
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Bucci, I.3    Joshi, L.R.4    Tsai, A.5    East-Palmer, J.6    Shiloach, J.7    Weintraub, B.D.8
  • 29
    • 0029135420 scopus 로고
    • Role of the carboxy-terminal residues of the α-subunit in the expression and bioactivity of human thyroid-stimulating hormone
    • Grossmann M, Szkudlinski MW, Zeng H, Kraiem Z, Ji I, Tropea JE, Ji HT, Weintraub BD 1995 Role of the carboxy-terminal residues of the α-subunit in the expression and bioactivity of human thyroid-stimulating hormone. Mol Endocrinol 9:948-958
    • (1995) Mol Endocrinol , vol.9 , pp. 948-958
    • Grossmann, M.1    Szkudlinski, M.W.2    Zeng, H.3    Kraiem, Z.4    Ji, I.5    Tropea, J.E.6    Ji, H.T.7    Weintraub, B.D.8
  • 31
    • 0004954085 scopus 로고
    • Culture of hormone-dependent functional epithelial cells from rat thyroids
    • Ambesi-Impiombato FS, Parks LAM, Coon HG 1980 Culture of hormone-dependent functional epithelial cells from rat thyroids. Proc Natl Acad Sci USA 77:3455-3459
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 3455-3459
    • Ambesi-Impiombato, F.S.1    Parks, L.A.M.2    Coon, H.G.3
  • 32
    • 0030013815 scopus 로고    scopus 로고
    • Site-directed mutagenesis of amino acids 33-44 of the common α-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cAMP production and growth promotion are potentially dissociable functions of hTSH
    • Grossmann M, Szkudlinski MW, Dias JA, Xia H, Wong R, Puett D, Weintraub BD 1996 Site-directed mutagenesis of amino acids 33-44 of the common α-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cAMP production and growth promotion are potentially dissociable functions of hTSH. Mol Endocrinol 10:769-779
    • (1996) Mol Endocrinol , vol.10 , pp. 769-779
    • Grossmann, M.1    Szkudlinski, M.W.2    Dias, J.A.3    Xia, H.4    Wong, R.5    Puett, D.6    Weintraub, B.D.7
  • 34
    • 0026317511 scopus 로고
    • Glycosidase inhibitors: Inhibitors of N-linked oligosaccharide processing
    • Elbein AD 1991 Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. FASEB J 5:3055-3063
    • (1991) FASEB J , vol.5 , pp. 3055-3063
    • Elbein, A.D.1
  • 35
    • 0016819546 scopus 로고
    • Role of the carbohydrate of human chorionic gonadotropin in the mechanism of hormone action
    • Moyle WR, Bahl OP, Maerz L 1974 Role of the carbohydrate of human chorionic gonadotropin in the mechanism of hormone action. J Biol Chem 250:9163-9169
    • (1974) J Biol Chem , vol.250 , pp. 9163-9169
    • Moyle, W.R.1    Bahl, O.P.2    Maerz, L.3
  • 36
    • 0028041190 scopus 로고
    • Structure-function studies of oligosaccharides of recombinant human thyrotropin by sequential deglycosylation and resialylation
    • Thotakura NR, Szkudlinski MW, Weintraub BD 1994 Structure-function studies of oligosaccharides of recombinant human thyrotropin by sequential deglycosylation and resialylation. Glycobiology 4:525-533
    • (1994) Glycobiology , vol.4 , pp. 525-533
    • Thotakura, N.R.1    Szkudlinski, M.W.2    Weintraub, B.D.3
  • 37
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors in the liver
    • Ashwell G, Harford J 1982 Carbohydrate-specific receptors in the liver. Annu Rev Biochem 51:531-554
    • (1982) Annu Rev Biochem , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 39
    • 0001581868 scopus 로고
    • Glycosylation and glycoprotein hormone function
    • Lustbander JW, Puett D, Ruddon RW (eds) Springer-Verlag, New York
    • Baenziger JU 1994 Glycosylation and glycoprotein hormone function. In: Lustbander JW, Puett D, Ruddon RW (eds) Glycoprotein hormones. Springer-Verlag, New York, pp 167-174
    • (1994) Glycoprotein Hormones , pp. 167-174
    • Baenziger, J.U.1
  • 40
    • 0028936425 scopus 로고
    • Expression of the extracellular domain of the thyrotropin receptor in the baculovirus system using a promoter active earlier than the polyhedrin promoter
    • Chazenbalk GD, Rapoport B 1995 Expression of the extracellular domain of the thyrotropin receptor in the baculovirus system using a promoter active earlier than the polyhedrin promoter. J Biol Chem 270:1543-1549
    • (1995) J Biol Chem , vol.270 , pp. 1543-1549
    • Chazenbalk, G.D.1    Rapoport, B.2
  • 41
    • 0025974324 scopus 로고
    • Biological activity and metabolic clearance of a recombinant human thyrotropin produced in Chinese hamster ovary cells
    • Thotakura NR, Desai RK, Bates LG, Cole ES, Pratt BM, Weintraub BD 1991 Biological activity and metabolic clearance of a recombinant human thyrotropin produced in Chinese hamster ovary cells. Endocrinology 128:341-348
    • (1991) Endocrinology , vol.128 , pp. 341-348
    • Thotakura, N.R.1    Desai, R.K.2    Bates, L.G.3    Cole, E.S.4    Pratt, B.M.5    Weintraub, B.D.6
  • 42
    • 0024840150 scopus 로고
    • Expression of recombinant chorionic gonadotropin in Chinese hamster ovary glycosylation mutants
    • Keene JL, Matzuk MM, Boime I 1989 Expression of recombinant chorionic gonadotropin in Chinese hamster ovary glycosylation mutants. Mol Endocrinol 3:2011-2017
    • (1989) Mol Endocrinol , vol.3 , pp. 2011-2017
    • Keene, J.L.1    Matzuk, M.M.2    Boime, I.3
  • 43
    • 0025291299 scopus 로고
    • In vitro and in vivo bioactivity of human follicle-stimulating hormone and partially deglycosylated variants secreted by transfected eukaryotic cell lines
    • Galway AB, Hsueh AJW, Keene JL, Yamoto M, Fauser BCJM, Boime I 1990 In vitro and in vivo bioactivity of human follicle-stimulating hormone and partially deglycosylated variants secreted by transfected eukaryotic cell lines. Endocrinology 127:93-100
    • (1990) Endocrinology , vol.127 , pp. 93-100
    • Galway, A.B.1    Hsueh, A.J.W.2    Keene, J.L.3    Yamoto, M.4    Fauser, B.C.J.M.5    Boime, I.6
  • 44
    • 0025176933 scopus 로고
    • The sialylated oligosaccharides of recombinant bovine lutropin modulate hormone bioactivity
    • Smith PL, Kaetzel D, Nilson J, Baenziger JU 1990 The sialylated oligosaccharides of recombinant bovine lutropin modulate hormone bioactivity. J Biol Chem 265:874-881
    • (1990) J Biol Chem , vol.265 , pp. 874-881
    • Smith, P.L.1    Kaetzel, D.2    Nilson, J.3    Baenziger, J.U.4
  • 45
    • 0025374906 scopus 로고
    • Differential interactions of human choriogonadotropin and its aglycosylated analog with their receptor
    • Ji I, Ji TH 1990 Differential interactions of human choriogonadotropin and its aglycosylated analog with their receptor. Proc Natl Acad Sci USA 87:4396-4400
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4396-4400
    • Ji, I.1    Ji, T.H.2
  • 46
    • 0029112363 scopus 로고
    • Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropins (TSH)
    • Szkudlinski MW, Thotakura NR, Tropea JE, Grossmann M, Weintraub BD 1995 Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropins (TSH). Endocrinology 136:3325-3330
    • (1995) Endocrinology , vol.136 , pp. 3325-3330
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Tropea, J.E.3    Grossmann, M.4    Weintraub, B.D.5
  • 48
    • 0027261228 scopus 로고
    • Variable carbohydrate structures of circulating thyrotropin as studied by lectin affinity chromatography in different clinical conditions
    • Papandreou MJ, Persani L, Asteria C, Ronin C, Beck-Peccoz P 1993 Variable carbohydrate structures of circulating thyrotropin as studied by lectin affinity chromatography in different clinical conditions. J Clin Endocrinol Metab 77:393-398
    • (1993) J Clin Endocrinol Metab , vol.77 , pp. 393-398
    • Papandreou, M.J.1    Persani, L.2    Asteria, C.3    Ronin, C.4    Beck-Peccoz, P.5
  • 49


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.