메뉴 건너뛰기




Volumn 137, Issue 10, 1996, Pages 4196-4200

Disulfide bonds 7-31 and 59-87 of the α-subunit play a different role in assembly of human chorionic gonadotropin and lutropin

Author keywords

[No Author keywords available]

Indexed keywords

CHORIONIC GONADOTROPIN; LUTEINIZING HORMONE;

EID: 0029768832     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.137.10.8828477     Document Type: Article
Times cited : (18)

References (35)
  • 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
  • 4
    • 0028116115 scopus 로고
    • Mutagenesis of Cysteine residues in the human gonadotropin α subunit. Roles of individual disulfide bonds in secretion, assembly, and biologic activity
    • Furuhashi M, Ando H, Bielinska M, Pixley MR, Shikone T, Hsueh AJW, Boime I 1994 Mutagenesis of Cysteine residues in the human gonadotropin α subunit. Roles of individual disulfide bonds in secretion, assembly, and biologic activity. J Biol Chem 269:25543-25548
    • (1994) J Biol Chem , vol.269 , pp. 25543-25548
    • Furuhashi, M.1    Ando, H.2    Bielinska, M.3    Pixley, M.R.4    Shikone, T.5    Hsueh, A.J.W.6    Boime, I.7
  • 5
    • 0023941649 scopus 로고
    • The role of the aspargine-linked oligosaccharides of the α subunit in the secretion and assembly of human chorionic gonadotropin
    • Matzuk MM, Boime I 1988 The role of the aspargine-linked oligosaccharides of the α subunit in the secretion and assembly of human chorionic gonadotropin. J Cell Biol 106:1049-1059
    • (1988) J Cell Biol , vol.106 , pp. 1049-1059
    • Matzuk, M.M.1    Boime, I.2
  • 7
    • 0024454312 scopus 로고
    • Mutagenesis and chimeric genes define determinants in the β subunits of human chorionic gonadotropin and lutropin for secretion and assembly
    • Matzuk MM, Spangler MM, Camel M, Suganuma N, Boime I 1989 Mutagenesis and chimeric genes define determinants in the β subunits of human chorionic gonadotropin and lutropin for secretion and assembly. J Cell Biol 109:1429-1438
    • (1989) J Cell Biol , vol.109 , pp. 1429-1438
    • Matzuk, M.M.1    Spangler, M.M.2    Camel, M.3    Suganuma, N.4    Boime, I.5
  • 9
    • 0028936554 scopus 로고
    • Role of the Pro-LeuArg motif in glycosylation of human gonadotropin α-subunit
    • Furuhashi M, Suzuki S, Tomoda Y, Suganuma N 1995 Role of the Pro-LeuArg motif in glycosylation of human gonadotropin α-subunit. Endocrinology 136:2270-2275
    • (1995) Endocrinology , vol.136 , pp. 2270-2275
    • Furuhashi, M.1    Suzuki, S.2    Tomoda, Y.3    Suganuma, N.4
  • 10
    • 0008519414 scopus 로고
    • Effects of preventing O-glycosylation on the secretion of human chorionic gonadotropin in Chinese hamster ovary cells
    • Matzuk MM, Krieger M, Corless CL, Boime I 1987 Effects of preventing O-glycosylation on the secretion of human chorionic gonadotropin in Chinese hamster ovary cells. Proc Natl Acad Sci USA 84:6354-6358
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6354-6358
    • Matzuk, M.M.1    Krieger, M.2    Corless, C.L.3    Boime, I.4
  • 11
    • 0023277697 scopus 로고
    • Gonadotropin beta subunits determine the rate of assembly and the oligosaccharide processing of hormone dimer in transfected cells
    • Corless CL, Matzuk MM, Ramabhadran TV, Krichevsky A, Boime I 1987 Gonadotropin beta subunits determine the rate of assembly and the oligosaccharide processing of hormone dimer in transfected cells. J Cell Biol 104:1173-1181
    • (1987) J Cell Biol , vol.104 , pp. 1173-1181
    • Corless, C.L.1    Matzuk, M.M.2    Ramabhadran, T.V.3    Krichevsky, A.4    Boime, I.5
  • 13
    • 0023835289 scopus 로고
    • The glycoprotein α-subunit is critical for secretion and stability of the human thyrotropin β-subunit
    • Matzuk MM, Kornmeier CM, Whitfield GK, Kourides IA, Boime I 1988 The glycoprotein α-subunit is critical for secretion and stability of the human thyrotropin β-subunit. Mol Endocrinol 2:95-100
    • (1988) Mol Endocrinol , vol.2 , pp. 95-100
    • Matzuk, M.M.1    Kornmeier, C.M.2    Whitfield, G.K.3    Kourides, I.A.4    Boime, I.5
  • 14
    • 0014245352 scopus 로고
    • Establishment of clonal strains of rat pituitary tumor cells that secrete growth hormone
    • Tashjian AH, Yasumura Y, Levine L, Sato GH, Parker ML 1968 Establishment of clonal strains of rat pituitary tumor cells that secrete growth hormone. Endocrinology 82:342-352
    • (1968) Endocrinology , vol.82 , pp. 342-352
    • Tashjian, A.H.1    Yasumura, Y.2    Levine, L.3    Sato, G.H.4    Parker, M.L.5
  • 15
    • 0024813415 scopus 로고
    • Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin β subunit
    • Suganuma N, Matzuk MM, Boime I 1989 Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin β subunit. J Biol Chem 264:19302-19307
    • (1989) J Biol Chem , vol.264 , pp. 19302-19307
    • Suganuma, N.1    Matzuk, M.M.2    Boime, I.3
  • 16
    • 0026800851 scopus 로고
    • Intracellular folding pathway of human chorionic gonadotropin β subunit
    • Huth JR, Mountjoy K, Perini F, Ruddon RW 1992 Intracellular folding pathway of human chorionic gonadotropin β subunit. J Biol Chem 267:8870-8879
    • (1992) J Biol Chem , vol.267 , pp. 8870-8879
    • Huth, J.R.1    Mountjoy, K.2    Perini, F.3    Ruddon, R.W.4
  • 17
    • 0025231706 scopus 로고
    • Identification of a follicle-stimulating hormone receptor-binding region in hFSH-β-(81-95) using synthetic peptides
    • Santa-Coloma TA, Reichert Jr LE 1990 Identification of a follicle-stimulating hormone receptor-binding region in hFSH-β-(81-95) using synthetic peptides. J Biol Chem 265:5037-5042
    • (1990) J Biol Chem , vol.265 , pp. 5037-5042
    • Santa-Coloma, T.A.1    Reichert Jr., L.E.2
  • 18
    • 0025174829 scopus 로고
    • Peptide mapping of intersubunit and receptor interactions of human choriogonadotropin
    • Salesse R, Bidart JM, Troalen F, Bellet D, Garnier J 1990 Peptide mapping of intersubunit and receptor interactions of human choriogonadotropin. Mol Cell Endocrinol 68:113-119
    • (1990) Mol Cell Endocrinol , vol.68 , pp. 113-119
    • Salesse, R.1    Bidart, J.M.2    Troalen, F.3    Bellet, D.4    Garnier, J.5
  • 19
    • 0025872893 scopus 로고
    • Identification of subunit contact sites on the α-subunit of lutropin
    • Krystek Jr SR, Dias JA, Andersen TT 1991 Identification of subunit contact sites on the α-subunit of lutropin. Biochemistry 30:1858-1864
    • (1991) Biochemistry , vol.30 , pp. 1858-1864
    • Krystek Jr., S.R.1    Dias, J.A.2    Andersen, T.T.3
  • 20
    • 0024991449 scopus 로고
    • Topographic analysis of the α-subunit of human follicle-stimulating hormone using site-specific antipeptide antisera
    • Weiner RS, Andersen TT, Dias JA 1990 Topographic analysis of the α-subunit of human follicle-stimulating hormone using site-specific antipeptide antisera. Endocrinology 127:573-579
    • (1990) Endocrinology , vol.127 , pp. 573-579
    • Weiner, R.S.1    Andersen, T.T.2    Dias, J.A.3
  • 21
    • 0017072980 scopus 로고
    • The reaction of tetranitromethane with human chorionic gonadotropin
    • Carlsen RB, Bahl OMP 1976 The reaction of tetranitromethane with human chorionic gonadotropin. Arch Biochem Biophys 175:209-220
    • (1976) Arch Biochem Biophys , vol.175 , pp. 209-220
    • Carlsen, R.B.1    Bahl, O.M.P.2
  • 22
    • 0020696020 scopus 로고
    • Purification of an alternate form of the α subunit of the glycoprotein hormones from bovine pituitaries and identification of its O-linked oligosaceharide
    • Parsons TF, Bloomfield GA, Pierce JG 1983 Purification of an alternate form of the α subunit of the glycoprotein hormones from bovine pituitaries and identification of its O-linked oligosaceharide. J Biol Chem 258:240-244
    • (1983) J Biol Chem , vol.258 , pp. 240-244
    • Parsons, T.F.1    Bloomfield, G.A.2    Pierce, J.G.3
  • 23
    • 0021765514 scopus 로고
    • An oligosaccharide of the O-linked type distinguishes the free from the combined form of hCG α subunit
    • Cole LA, Perini F, Birken S, Ruddon RW 1984 An oligosaccharide of the O-linked type distinguishes the free from the combined form of hCG α subunit. Biochem Biophys Res Commun 122:1260-1267
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1260-1267
    • Cole, L.A.1    Perini, F.2    Birken, S.3    Ruddon, R.W.4
  • 24
    • 0018584123 scopus 로고
    • Studies with carbodiimide-cross-linked derivatives of bovine lutropin. II. Location of the cross-link and implication for interaction with the receptors in testes
    • Weare JA, Reichert Jr LE 1979 Studies with carbodiimide-cross-linked derivatives of bovine lutropin. II. Location of the cross-link and implication for interaction with the receptors in testes. J Biol Chem 254:6972-6979
    • (1979) J Biol Chem , vol.254 , pp. 6972-6979
    • Weare, J.A.1    Reichert Jr., L.E.2
  • 25
    • 0027513329 scopus 로고
    • A subunit interaction site in human luteinizing hormone: Identification by photoaffinity cross-linking
    • Keutmann HT, Rubin DA 1993 A subunit interaction site in human luteinizing hormone: identification by photoaffinity cross-linking. Endocrinology 132:1305-1312
    • (1993) Endocrinology , vol.132 , pp. 1305-1312
    • Keutmann, H.T.1    Rubin, D.A.2
  • 26
    • 0026535920 scopus 로고
    • Site-directed mutagenesis defines a domain in the gonadotropin α-subunit required for assembly with the chorionic gonadotropin β-subunit
    • Bielinska M, Boime I 1992 Site-directed mutagenesis defines a domain in the gonadotropin α-subunit required for assembly with the chorionic gonadotropin β-subunit. Mol Endocrinol 6:267-271
    • (1992) Mol Endocrinol , vol.6 , pp. 267-271
    • Bielinska, M.1    Boime, I.2
  • 27
    • 0028218007 scopus 로고
    • A region in the human glycoprotein hormone α-subunit important in holoprotein formation and receptor binding
    • Xia H, Chen F, Puett D 1994 A region in the human glycoprotein hormone α-subunit important in holoprotein formation and receptor binding. Endocrinology 134:1768-1770
    • (1994) Endocrinology , vol.134 , pp. 1768-1770
    • Xia, H.1    Chen, F.2    Puett, D.3
  • 28
    • 0021836550 scopus 로고
    • Analysis of computer-generated hydropathy profiles for human glycoprotein and lactogenic hormones
    • Krystek Jr SR, Reichert Jr LE, Andersen TT 1985 Analysis of computer-generated hydropathy profiles for human glycoprotein and lactogenic hormones. Endocrinology 117:1110-1124
    • (1985) Endocrinology , vol.117 , pp. 1110-1124
    • Krystek Jr., S.R.1    Reichert Jr., L.E.2    Andersen, T.T.3
  • 29
    • 0026786419 scopus 로고
    • Kinetics of folding and assembly of the human chorionic gonadotropin β subunit in transfected Chinese hamster ovary cells
    • Bedows E, Huth JR, Ruddon RW 1992 Kinetics of folding and assembly of the human chorionic gonadotropin β subunit in transfected Chinese hamster ovary cells. J Biol Chem 267:8880-8886
    • (1992) J Biol Chem , vol.267 , pp. 8880-8886
    • Bedows, E.1    Huth, J.R.2    Ruddon, R.W.3
  • 30
    • 0018679846 scopus 로고
    • Formation of an intrachain disulfide bond on nascent immunoglobulin light chains
    • Bergman LW, Kuehl WM 1979 Formation of an intrachain disulfide bond on nascent immunoglobulin light chains. J Biol Chem 254:8869-8876
    • (1979) J Biol Chem , vol.254 , pp. 8869-8876
    • Bergman, L.W.1    Kuehl, W.M.2
  • 31
    • 0020479440 scopus 로고
    • The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds
    • Peters Jr T, Davidson LK 1982 The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds. J Biol Chem 257:8847-8853
    • (1982) J Biol Chem , vol.257 , pp. 8847-8853
    • Peters Jr., T.1    Davidson, L.K.2
  • 32
    • 0023720121 scopus 로고
    • Defective co-translational formation of disulphide bonds in protein disulphide-isomernse-deficient microsomes
    • Bulleid NJ, Freedman RB 1988 Defective co-translational formation of disulphide bonds in protein disulphide-isomernse-deficient microsomes. Nature 335:649-651
    • (1988) Nature , vol.335 , pp. 649-651
    • Bulleid, N.J.1    Freedman, R.B.2
  • 33
    • 0023236959 scopus 로고
    • Catalysis of protein folding by prolyl isomerase
    • Lang K, Schmid FX, Fischer G 1987 Catalysis of protein folding by prolyl isomerase. Nature 329:268-270
    • (1987) Nature , vol.329 , pp. 268-270
    • Lang, K.1    Schmid, F.X.2    Fischer, G.3
  • 35
    • 0027182764 scopus 로고
    • Protein folding and assembly in vitro parallel intracellular folding and assembly. Catalysis of folding and assembly of the human chorionic gonadotropin α β dimer by protein disulfide isomerase
    • Huth JR, Perini F, Lockridge O, Bedows E, Ruddon RW 1993 Protein folding and assembly in vitro parallel intracellular folding and assembly. Catalysis of folding and assembly of the human chorionic gonadotropin α β dimer by protein disulfide isomerase. J Biol Chem 268:16472-16482
    • (1993) J Biol Chem , vol.268 , pp. 16472-16482
    • Huth, J.R.1    Perini, F.2    Lockridge, O.3    Bedows, E.4    Ruddon, R.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.