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Volumn 154, Issue 3, 2013, Pages 1373-1383

Carbohydrate-mediated polyethylene glycol conjugation of TSH improves its pharmacological properties

Author keywords

[No Author keywords available]

Indexed keywords

GALACTOSE; MACROGOL; RADIOACTIVE IODINE; RECOMBINANT THYROTROPIN; SIALIC ACID; THYROGLOBULIN; THYROTROPIN RECEPTOR;

EID: 84874601289     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2012-2010     Document Type: Article
Times cited : (15)

References (31)
  • 1
    • 70449370231 scopus 로고    scopus 로고
    • Revised American thyroid association management guidelines for patients with thyroid nodules and differentiated thyroid cancer
    • Cooper DS, Doherty GM, Haugen BR, et al. Revised American Thyroid Association management guidelines for patients with thyroid nodules and differentiated thyroid cancer. Thyroid. 2009;19:1167-1214.
    • (2009) Thyroid. , vol.19 , pp. 1167-1214
    • Cooper, D.S.1    Doherty, G.M.2    Haugen, B.R.3
  • 2
    • 84874643791 scopus 로고    scopus 로고
    • Thyrogen (thyrotropin alfa for injection
    • Cambridge, MA. Genzyme Corp
    • Thyrogen (thyrotropin alfa for injection) Package Insert. 2008. Cambridge, MA. Genzyme Corp.
    • (2008) Package Insert.
  • 3
    • 0028890259 scopus 로고
    • Glycoprotein hormones: Glycobiology of gonadotrophins, thyrotrophin and free β subunit
    • Thotakura NR, Blithe DL. Glycoprotein hormones: Glycobiology of gonadotrophins, thyrotrophin and free β subunit. Glycobiology. 1995;5:3-10.
    • (1995) Glycobiology. , vol.5 , pp. 3-10
    • Thotakura, N.R.1    Blithe, D.L.2
  • 4
    • 0024282581 scopus 로고
    • Pituitary glycoprotein hormone oligosaccharides: Structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin
    • Baenziger JU, Green ED. Pituitary glycoprotein hormone oligosaccharides: Structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin. Biochim Biophys Acta. 1988;947:287-306.
    • (1988) Biochim Biophys Acta. , vol.947 , pp. 287-306
    • Baenziger, J.U.1    Green, E.D.2
  • 5
    • 0347993695 scopus 로고    scopus 로고
    • The effect of posttranslational modifications on the in vitro activity of recombinanthumanthyroidstimulating hormone
    • Sendak RA, Ganesa C, Lee KL, et al. The effect of posttranslational modifications on the in vitro activity of recombinanthumanthyroidstimulating hormone. Thyroid. 2003;13:1091-1101.
    • (2003) Thyroid. , vol.13 , pp. 1091-1101
    • Sendak, R.A.1    Ganesa, C.2    Lee, K.L.3
  • 6
    • 0027177562 scopus 로고
    • Recombinant human thyroid stimulating hormone: Development of a biotechnology product for detection of metastatic lesions of thyroid carcinoma
    • Cole ES, Lee K, Lauziere K, et al. Recombinant human thyroid stimulating hormone: Development of a biotechnology product for detection of metastatic lesions of thyroid carcinoma. Biotechnology. 1993;11:1014-1024.
    • (1993) Biotechnology. , vol.11 , pp. 1014-1024
    • Cole, E.S.1    Lee, K.2    Lauziere, K.3
  • 7
    • 0027517557 scopus 로고
    • Purification and characterization of recombinanthumanthyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: The role of sialylation and sulfation in TSH bioactivity
    • Szkudlinski MW, Thotakura NR, Bucci I, et al. Purification and characterization of recombinanthumanthyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: The role of sialylation and sulfation in TSH bioactivity. Endocrinology. 1993;133:1490-1503.
    • (1993) Endocrinology. , vol.133 , pp. 1490-1503
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Bucci, I.3
  • 8
    • 0029079758 scopus 로고
    • Subunit-specific functions of N-linked oligosaccharides in human thyrotropin: Role of terminal residues of α-and α-subunit oligosaccharides in metabolic clearance and bioactivity
    • Szkudlinski MW, Thotakura NR, Weintraub BD. Subunit-specific functions of N-linked oligosaccharides in human thyrotropin: Role of terminal residues of α-and α-subunit oligosaccharides in metabolic clearance and bioactivity. Proc Natl Acad Sci U S A. 1995;92: 9062-9066.
    • (1995) Proc Natl Acad Sci U S A. , vol.92 , pp. 9062-9066
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Weintraub, B.D.3
  • 9
    • 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 for the oligosaccharides in the in vitro and in vivo bioactivity
    • Grossmann M, Szkudlinski MW, Tropea JE, et al. Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites. Characterization of a novel role for the oligosaccharides in the in vitro and in vivo bioactivity. J Biol Chem. 1995;270:29378-29385.
    • (1995) J Biol Chem. , vol.270 , pp. 29378-29385
    • Grossmann, M.1    Szkudlinski, M.W.2    Tropea, J.E.3
  • 10
    • 0030025347 scopus 로고    scopus 로고
    • Modification of the sialic acid residues of choriogonadotropin affects signal transduction
    • Reddy BV, Bartoszewicz Z, Rebois RV. Modification of the sialic acid residues of choriogonadotropin affects signal transduction. Cell Signal. 1996;8:35-41.
    • (1996) Cell Signal. , vol.8 , pp. 35-41
    • Reddy, B.V.1    Bartoszewicz, Z.2    Rebois, R.V.3
  • 12
    • 0029112363 scopus 로고
    • Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropin
    • SzkudlinskiMW,Thotakura NR, Tropea JE, Grossmann M, Weintraub BD. Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropin. Endocrinology. 1995;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
  • 13
    • 0033569567 scopus 로고    scopus 로고
    • Multiple interactions between pituitary hormones and the mannose receptor
    • Simpson DZ, Hitchen PG, Elmhirst EL, Taylor ME. Multiple interactions between pituitary hormones and the mannose receptor. Biochem J. 1999;343(2):403-411.
    • (1999) Biochem J. , vol.343 , Issue.2 , pp. 403-411
    • Simpson, D.Z.1    Hitchen, P.G.2    Elmhirst, E.L.3    Taylor, M.E.4
  • 14
    • 55749111387 scopus 로고    scopus 로고
    • The pharmacology of PEGylation: Balancing PD with PK to generate novel therapeutics
    • Fishburn CS. The pharmacology of PEGylation: Balancing PD with PK to generate novel therapeutics. J Pharm Sci. 2008;97:4167-4183.
    • (2008) J Pharm Sci. , vol.97 , pp. 4167-4183
    • Fishburn, C.S.1
  • 17
    • 17044429357 scopus 로고    scopus 로고
    • Carbohydrate-specifically polyethylene glycol-modified ricin A-chain with improved therapeutic potential
    • Youn YS, Na DH, Yoo SD, Song SC, Lee KC. Carbohydrate-specifically polyethylene glycol-modified ricin A-chain with improved therapeutic potential. Int J Biochem Cell Biol. 2005;37:1525-1533.
    • (2005) Int J Biochem Cell Biol. , vol.37 , pp. 1525-1533
    • Youn, Y.S.1    Na, D.H.2    Yoo, S.D.3    Song, S.C.4    Lee, K.C.5
  • 18
  • 19
    • 12744280744 scopus 로고    scopus 로고
    • Structure of human follicle-stimulating hormone in complex with its receptor
    • Fan QR, Hendrickson WA. Structure of human follicle-stimulating hormone in complex with its receptor. Nature. 2005;433:269-277.
    • (2005) Nature. , vol.433 , pp. 269-277
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 20
    • 0035086519 scopus 로고    scopus 로고
    • Rational design of a potent, long-lasting form of interferon: A 40 kDa branched polyethylene glycol-conjugated interferon α-2a for the treatment of hepatitis C
    • Bailon P, Palleroni A, Schaffer CA, et al. Rational design of a potent, long-lasting form of interferon: A 40 kDa branched polyethylene glycol-conjugated interferon α-2a for the treatment of hepatitis C. Bioconjug Chem. 2001;12:195-202.
    • (2001) Bioconjug Chem. , vol.12 , pp. 195-202
    • Bailon, P.1    Palleroni, A.2    Schaffer, C.A.3
  • 21
    • 0026536995 scopus 로고
    • Detection and molecular weight determination of polyethylene glycol-modified hirudin by staining after sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Kurfurst MM. Detection and molecular weight determination of polyethylene glycol-modified hirudin by staining after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal Biochem. 1992;200:244-248.
    • (1992) Anal Biochem. , vol.200 , pp. 244-248
    • Kurfurst, M.M.1
  • 22
    • 0028041190 scopus 로고
    • Structure-function studies of oligosaccharides of recombinanthumanthyrotrophin by sequential deglycosylation and resialylation
    • Thotakura NR, Szkudlinski MW, Weintraub BD. Structure-function studies of oligosaccharides of recombinanthumanthyrotrophin by sequential deglycosylation and resialylation. Glycobiology. 1994;4:525-533.
    • (1994) Glycobiology. , vol.4 , pp. 525-533
    • Thotakura, N.R.1    Szkudlinski, M.W.2    Weintraub, B.D.3
  • 23
    • 0036083401 scopus 로고    scopus 로고
    • Thyroidstimulating hormone and thyroid-stimulating hormone receptor structure-function relationships
    • Szkudlinski MW, Fremont V, Ronin C, Weintraub BD. Thyroidstimulating hormone and thyroid-stimulating hormone receptor structure-function relationships. Physiol Rev. 2002;82:473-502.
    • (2002) Physiol Rev. , vol.82 , pp. 473-502
    • Szkudlinski, M.W.1    Fremont, V.2    Ronin, C.3    Weintraub, B.D.4
  • 24
    • 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, et al. Biological activity and metabolic clearance of a recombinant human thyrotropin produced in Chinese hamster ovary cells. Endocrinology. 1991;128:341-348.
    • (1991) Endocrinology. , vol.128 , pp. 341-348
    • Thotakura, N.R.1    Desai, R.K.2    Bates, L.G.3
  • 26
    • 55749106015 scopus 로고    scopus 로고
    • FSH and TSH binding to their respective receptors: Similarities, differences and implication for glycoprotein hormone specificity
    • Nunez Miguel R, Sanders J, Chirgadze DY, Blundell TL, Furmaniak J, Rees Smith B. FSH and TSH binding to their respective receptors: Similarities, differences and implication for glycoprotein hormone specificity. J Mol Endocrinol. 2008;41:145-164.
    • (2008) J Mol Endocrinol. , vol.41 , pp. 145-164
    • Nunez Miguel, R.1    Sanders, J.2    Chirgadze, D.Y.3    Blundell, T.L.4    Furmaniak, J.5    Rees Smith, B.6
  • 27
    • 39749120684 scopus 로고    scopus 로고
    • Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity, stability, and biological activity
    • Banks DD, Gadgil HS, Pipes GD, et al. Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity, stability, and biological activity. J Pharm Sci. 2008;97:775-790.
    • (2008) J Pharm Sci. , vol.97 , pp. 775-790
    • Banks, D.D.1    Gadgil, H.S.2    Pipes, G.D.3
  • 28
    • 33746273552 scopus 로고    scopus 로고
    • Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis
    • Gadgil HS, Bondarenko PV, Pipes GD, et al. Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis. Anal Biochem. 2006;355:165-174.
    • (2006) Anal Biochem. , vol.355 , pp. 165-174
    • Gadgil, H.S.1    Bondarenko, P.V.2    Pipes, G.D.3
  • 29
    • 54749084565 scopus 로고    scopus 로고
    • Hydrolytic stability of hydrazones and oximes
    • Kalia J, Raines RT. Hydrolytic stability of hydrazones and oximes. Angew Chem Int Ed Engl. 2008;47:7523-7526.
    • (2008) Angew Chem Int Ed Engl. , vol.47 , pp. 7523-7526
    • Kalia, J.1    Raines, R.T.2
  • 30
    • 79955047963 scopus 로고    scopus 로고
    • CQ. Strategies for Neoglycan conjugation to human acid α-glucosidase
    • Zhou Q, Stefano JE, Harrahy J, et al.CQ. Strategies for Neoglycan conjugation to human acid α-glucosidase. Bioconjug Chem. 2011; 22:741-751.
    • (2011) Bioconjug Chem. , vol.22 , pp. 741-751
    • Zhou, Q.1    Stefano, J.E.2    Harrahy, J.3


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