메뉴 건너뛰기




Volumn 242, Issue 3, 1996, Pages 608-618

Structural characterisation of human recombinant glycohormones follitropin, lutropin and choriogonadotropin expressed in Chinese hamster ovary cells

Author keywords

Gonadotropin; Mass spectrometry; Oligosaccharide; Recombinant glycoprotein; Structural characterisation

Indexed keywords

CHORIONIC GONADOTROPIN; FOLLITROPIN; GLYCOPROTEIN; LUTEINIZING HORMONE; RECOMBINANT PROTEIN;

EID: 0030438018     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0608r.x     Document Type: Article
Times cited : (49)

References (31)
  • 1
    • 0019729482 scopus 로고
    • Glycoprotein hormones: Structure and function
    • Pierce, J. G. & Parson, T. F. (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    Parson, T.F.2
  • 2
    • 0026485387 scopus 로고
    • Molecular structures of glycoprotein hormones and functions of their carbohydrate components
    • Stockell Hartree, A. & Renwick, A. G. C. (1992) Molecular structures of glycoprotein hormones and functions of their carbohydrate components, Biochem. J. 287, 665-679.
    • (1992) Biochem. J. , vol.287 , pp. 665-679
    • Stockell Hartree, A.1    Renwick, A.G.C.2
  • 3
    • 0004526403 scopus 로고
    • Chin, W. W. & Boime, I., eds Serono Symposia, Norwell MA
    • Childs, G. V., Ellison, D. G. & Unabia, G. (1990) in Glycoprotein hormones (Chin, W. W. & Boime, I., eds) pp. 1-10, Serono Symposia, Norwell MA.
    • (1990) Glycoprotein Hormones , pp. 1-10
    • Childs, G.V.1    Ellison, D.G.2    Unabia, G.3
  • 4
    • 0016221603 scopus 로고
    • Studies on the disulphide bonds of glycoprotein hormones
    • Cornell, J. S. & Pierce, J. G. (1974) Studies on the disulphide bonds of glycoprotein hormones, J. Biol. Chem. 249, 4166-4174.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4166-4174
    • Cornell, J.S.1    Pierce, J.G.2
  • 5
    • 0027156984 scopus 로고
    • Disulphide bond mutations affect the folding of the human chorionic gonadotrophin β subunit in transfected Chinese hamster ovary cells
    • Bedows, E., Huth, J. R., Suganuma, N., Bartels, C., Boime, I. & Ruddon, R. W. (1993) Disulphide bond mutations affect the folding of the human chorionic gonadotrophin β subunit in transfected Chinese hamster ovary cells, J. Biol. Chem. 268, 11655-11662.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11655-11662
    • Bedows, E.1    Huth, J.R.2    Suganuma, N.3    Bartels, C.4    Boime, I.5    Ruddon, R.W.6
  • 7
    • 0028890259 scopus 로고
    • Glycoprotein hormones: Glycobiology of gonadotrophins, thyrotrophin and free α subunit
    • Thotakura, K. & Blithe, D. (1995) Glycoprotein hormones: glycobiology of gonadotrophins, thyrotrophin and free α subunit, Glycobiology 5, 3-10.
    • (1995) Glycobiology , vol.5 , pp. 3-10
    • Thotakura, K.1    Blithe, D.2
  • 8
    • 0028289785 scopus 로고
    • Specific roles for the asparagines-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal trasduction
    • Bishop, L. A., Robertson, D. M., Cahir, N. & Schofield, P. R. (1994) Specific roles for the asparagines-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal trasduction, Mol. Endocrinol. 8, 722-731.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 722-731
    • Bishop, L.A.1    Robertson, D.M.2    Cahir, N.3    Schofield, P.R.4
  • 9
    • 0026344397 scopus 로고
    • Changes in binding activity of lutenizing hormone receptors by site directed mutagenesis of potential glycosylation sites
    • Zhang, R., Tsai-Morris, C. H., Kitamura, M., Buczko, E. & Dufau, M. L. (1991) Changes in binding activity of lutenizing hormone receptors by site directed mutagenesis of potential glycosylation sites, Biochem. Biophys. Res. Commun. 181, 804-808.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 804-808
    • Zhang, R.1    Tsai-Morris, C.H.2    Kitamura, M.3    Buczko, E.4    Dufau, M.L.5
  • 10
    • 0024282581 scopus 로고
    • Pituitary glycoprotein hormone oligosaccharides: Structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin
    • Baenzíger, J. U. & Green, E. D. (1988) Pituitary glycoprotein hormone oligosaccharides: structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin, Biochem. Biophys. Acta 947, 287-306.
    • (1988) Biochem. Biophys. Acta , vol.947 , pp. 287-306
    • Baenzíger, J.U.1    Green, E.D.2
  • 11
    • 0025981417 scopus 로고
    • Glycosylation of recombinant protein therapeutics: Control and functional implication
    • Cummings, D. A. (1991) Glycosylation of recombinant protein therapeutics: control and functional implication, Glycobiology 1, 115-130.
    • (1991) Glycobiology , vol.1 , pp. 115-130
    • Cummings, D.A.1
  • 12
    • 0028924455 scopus 로고
    • Amino acid sequence and disulphide bridge pattern of three γ-thionins from Sorghum bicolor
    • Nitti, G., Orru, S., Bloch, C., Mohry, L., Marino, G. & Pucci, P. (1995) Amino acid sequence and disulphide bridge pattern of three γ-thionins from Sorghum bicolor, Eur. J. Biochem. 228, 250-256.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 250-256
    • Nitti, G.1    Orru, S.2    Bloch, C.3    Mohry, L.4    Marino, G.5    Pucci, P.6
  • 13
    • 0014408452 scopus 로고
    • Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucin
    • Carlson, D. M. (1968) Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucin, J. Biol. Chem. 243, 616-626.
    • (1968) J. Biol. Chem. , vol.243 , pp. 616-626
    • Carlson, D.M.1
  • 15
    • 0025615601 scopus 로고
    • Preparation and desorption mass spectrometry of permethyl and peracetyl derivatives of oligosaccharides
    • Dell, A. (1990) Preparation and desorption mass spectrometry of permethyl and peracetyl derivatives of oligosaccharides, Methods Enzimol. 193, 647-660.
    • (1990) Methods Enzimol. , vol.193 , pp. 647-660
    • Dell, A.1
  • 16
    • 0023691052 scopus 로고
    • Computer program for post-translational modification site assignment in proteins using fast atom bombardment mass spectral data
    • Pucci, P. & Sepe, C. (1988) Computer program for post-translational modification site assignment in proteins using fast atom bombardment mass spectral data, Biomed. Environ. Mass Spectrum. 17, 287-291.
    • (1988) Biomed. Environ. Mass Spectrum. , vol.17 , pp. 287-291
    • Pucci, P.1    Sepe, C.2
  • 18
    • 0022551007 scopus 로고
    • Carbohydrate mapping by mass spectrometry: A novel method for identifying attachment sites of Asn-linked sugars in glycoproteins
    • Carr, S. A. & Roberts, G. L. (1986) Carbohydrate mapping by mass spectrometry: a novel method for identifying attachment sites of Asn-linked sugars in glycoproteins, Anal. Biochem. 157, 396-402.
    • (1986) Anal. Biochem. , vol.157 , pp. 396-402
    • Carr, S.A.1    Roberts, G.L.2
  • 19
    • 33845374920 scopus 로고
    • An approach toward the complete FAB analysis of enzymic digests of peptides and proteins
    • Naylor, S., Findeis, A., Gibson, G. W. & Williams, D. H. (1986) An approach toward the complete FAB analysis of enzymic digests of peptides and proteins, J. Am. Chem. Soc. 108, 6359-6363.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6359-6363
    • Naylor, S.1    Findeis, A.2    Gibson, G.W.3    Williams, D.H.4
  • 20
    • 0023474057 scopus 로고
    • FAB mass spectrometry of carbohydrates
    • Dell, A. (1987) FAB mass spectrometry of carbohydrates, Adv. Carbohydr. Chem. Biochem. 45, 19-72.
    • (1987) Adv. Carbohydr. Chem. Biochem. , vol.45 , pp. 19-72
    • Dell, A.1
  • 21
    • 0025723984 scopus 로고
    • Chemistry of the inactivation of 4-aminobutyrate aminotransferase by the antiepilectic drug vigabatrin
    • Debiase, D., Barra, D., Bossa, F., Pucci, P. & John, R. A. (1991) Chemistry of the inactivation of 4-aminobutyrate aminotransferase by the antiepilectic drug vigabatrin, J. Biol. Chem. 266, 20056-20061.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20056-20061
    • Debiase, D.1    Barra, D.2    Bossa, F.3    Pucci, P.4    John, R.A.5
  • 22
    • 0002711923 scopus 로고
    • Li, C. H., ed. Academic Press, New York
    • Sairam, M. R. (1983) in Hormonal protein and peptides (Li, C. H., ed.) vol. 11, pp. 1-79, Academic Press, New York.
    • (1983) Hormonal Protein and Peptides , vol.11 , pp. 1-79
    • Sairam, M.R.1
  • 23
    • 0004207109 scopus 로고
    • Academic Press, Orlando FL
    • Norman, A. W. & Litwack, G. (1987) Hormones, pp. 171-220, Academic Press, Orlando FL.
    • (1987) Hormones , pp. 171-220
    • Norman, A.W.1    Litwack, G.2
  • 24
    • 0025280694 scopus 로고
    • Carbohydrate composition of the α-subunit of human choriogonadotropin (hCGα) and the free H molecules produced in pregnancy: Most free α and some combined hCG-α molecules are fucosylated
    • Blithe, D. L. (1990) Carbohydrate composition of the α-subunit of human choriogonadotropin (hCGα) and the free H molecules produced in pregnancy: most free α and some combined hCG-α molecules are fucosylated, Endocrinology 126, 2788-2799.
    • (1990) Endocrinology , vol.126 , pp. 2788-2799
    • Blithe, D.L.1
  • 26
    • 0019277548 scopus 로고
    • Different asparagine-linked sugar chains on the two polypeptide chains of human chorionic gonadotropin
    • Mizuochi, T. & Kobata, A. (1980) Different asparagine-linked sugar chains on the two polypeptide chains of human chorionic gonadotropin, Biochem. Biophys. Res. Commun. 97, 772-778.
    • (1980) Biochem. Biophys. Res. Commun. , vol.97 , pp. 772-778
    • Mizuochi, T.1    Kobata, A.2
  • 28
    • 0022884332 scopus 로고
    • Biosynthesis of sulphated asparagine-linked oligosaccharides on bovine lutropin
    • Green, E. D., Boíme, I. & Baenziger, J. U. (1986) Biosynthesis of sulphated asparagine-linked oligosaccharides on bovine lutropin, J. Biol. Chem. 261, 16309-16316.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16309-16316
    • Green, E.D.1    Boíme, I.2    Baenziger, J.U.3
  • 29
    • 0026665176 scopus 로고
    • Human liver and human placenta both contain CMP-NeuAc: Gal β1→4GlcNAc-R α2→3- As well as α2→6-sialyltransferase activity
    • Nemansky, M., Schiphorst, W. E., Kolleman, C. A. & Van den Eijnden, D. H. (1992) Human liver and human placenta both contain CMP-NeuAc: Gal β1→4GlcNAc-R α2→3- as well as α2→6-sialyltransferase activity, FEBS Lett. 312, 31-36.
    • (1992) FEBS Lett. , vol.312 , pp. 31-36
    • Nemansky, M.1    Schiphorst, W.E.2    Kolleman, C.A.3    Van Den Eijnden, D.H.4
  • 31
    • 0026585325 scopus 로고
    • Circulatory half-life but not interaction with the lutropin/chorionic gonadotropin receptor is modulated hy sulfation of bovine lutropin oligosaccharides
    • Baenziger, J. U., Kumar, S., Brodbeck, R. M., Smith, P. L. & Beranek, M. C. (1992) Circulatory half-life but not interaction with the lutropin/chorionic gonadotropin receptor is modulated hy sulfation of bovine lutropin oligosaccharides, Proc. Natl Acad. Sci. USA 89, 334-338.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 334-338
    • Baenziger, J.U.1    Kumar, S.2    Brodbeck, R.M.3    Smith, P.L.4    Beranek, M.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.