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Chapter 44: Discovery of a Growth Hormone Antagonist Using a Structure–Function Approach—References

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Abosch A., Tyrrell J.B., Lamborn K.R., Hannegan L.T., Applebury C.B., and Wilson C.B. 1998. Transsphenoidal microsurgery for growth hormone-secreting pituitary adenomas: Initial outcome and long-term results. J. Clin. Endocrinol. Metab. 83: 3411–3418.

Alexander L., Appleton D., Hall R., Ross W.M., and Wilkinson R. 1980. Epidemiology of acromegaly in the Newcastle region. Clin. Endocrinol. 12: 71–79.

Ballesteros M., Leung K.C., Ross R.J., Iismaa T.P., and Ho K.K. 2000. Distribution and abundance of messenger ribonucleic acid for growth hormone receptor isoforms in human tissues. J. Clin. Endocrinol. Metab. 85: 2865–2871.

Bass S.H., Mulkerrin M.G., and Wells J.A. 1991. A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor. Proc. Natl. Acad. Sci. 88: 4498–4502.

Bates A.S., Van't Hoff W., Jones J.M., and Clayton R.N. 1993. An audit of outcome of treatment in acromegaly. Q. J. Med. 86: 293–299.

Baumann G. 2001. Growth hormone binding protein 2001. J. Pediatr. Endocrinol. Metab. 14: 355–375.

Baumann G. 2002. Growth hormone binding protein. The soluble growth hormone receptor. Minerva Endocrinol. 27: 265–276.

Baumbach W.R., Horner D.L., and Logan J.S. 1989. The growth hormone-binding protein in rat serum is an alternatively spliced form of the rat growth hormone receptor. Genes Dev. 3: 1199–1205.

Baumgartner J.W., Wells C.A., Chen C.M., and Waters M.J. 1994. The role of the WSXWS equivalent motif in growth hormone receptor function. J. Biol. Chem. 269: 29094–29101.

Bazan J.F. 1990. Haemopoietic receptors and helical cytokines. Immunol. Today 11: 350–354.

Chen W.Y., White M.E., Wagner T.E., and Kopchick J.J. 1991a. Functional antagonism between endogenous mouse growth hormone (GH) and a GH analog results in dwarf transgenic mice. Endocrinology 129: 1402–1408.

Chen W.Y., Wight D.C., Wagner T.E., and Kopchick J.J. 1990. Expression of a mutated bovine growth hormone gene suppresses growth of transgenic mice. Proc. Natl. Acad. Sci. 87: 5061–5065.

Chen W.Y., Chen N., Yun J., Wagner T.E., and Kopchick J.J. 1994. In vitro and in vivo studies of the antagonistic effects of human growth hormone analogs. J. Biol. Chem. 269: 15892–15897.

Chen W.Y., Wight D.C., Mehta B.V., Wagner T.E., and Kopchick J.J. 1991b. Glycine 119 of bovine growth hormone is critical for growth-promoting activity. Mol. Endocrinol. 5: 1845–1852.

Chen W.Y., Wight D.C., Chen N.Y., Coleman T.A., Wagner T.E., and Kopchick J.J. 1991c. Mutations in the third alpha-helix of bovine growth hormone dramatically affect its intracellular distribution in vitro and growth enhancement in transgenic mice. J. Biol. Chem. 266: 2252–2258.

Chen X.Z., Shafer A.W., Yun J.S., Li Y.S., Wagner T.E., and Kopchick J.J. 1992. Conversion of bovine growth hormone cysteine residues to serine affects secretion by cultured cells and growth rates in transgenic mice. Mol. Endocrinol. 6: 598–606.

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Clackson T., Ultsch M.H., Wells J.A., and de Vos A.M. 1998. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol. 277: 1111–1128.

Clark R., Olson K., Fuh G., Marian M., Mortensen D., Teshima G., Chang S., Chu H., Mukku V., Canova-Davis E., Somers T., Cronin M., Winkler M., and Wells J.A. 1996. Long-acting growth hormones produced by conjugation with polyethylene glycol. J. Biol. Chem. 271: 21969–21977.

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Cowan J., Wang X., Guan R., He K., Jiang J., Baumann G., Black R.A., Wolfe M.S., and Frank S.J. 2005. GH receptor is a target for presinilin-dependent γ-secretase cleavage. J. Biol. Chem. 280: 19331–19342.

Cunningham B.C. and Wells J.A. 1989. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244: 1081–1085.

Cunningham B.C. and Wells J.A. 1991. Rational design of receptor-specific variants of human growth hormone. Proc. Natl. Acad. Sci. 88: 3407–3411.

Cunningham B.C., Jhurani P., Ng P., and Wells J.A. 1989. Receptor and antibody epitopes in human growth hormone identified by homolog-scanning mutagenesis. Science 243: 1330–1336.

Cunningham B.C., Ultsch M., De Vos A.M., Mulkerrin M.G., Clauser K.R., and Wells J.A. 1991. Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254: 821–825.

Davidson M.B. 1987. Effect of growth hormone on carbohydrate and lipid metabolism. Endocr. Rev. 8: 115–131.

Davidson M.B., Shen D.C., Venkatesan N., and Sladen G. 1987. In vivo insulin antagonism but evanescent in vitro tissue effect in rats with growth hormone-secreting tumors. J. Endocrinol. Investig. 10: 569–574.

de Vos A.M., Ultsch M., and Kossiakoff A.A. 1992. Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science 255: 306–312.

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Freda P.U. 2003. How effective are current therapies for acromegaly? Growth Horm. IGF Res. (suppl. A) 13: S144–151.

Fuh G., Cunningham B.C., Fukunaga R., Nagata S., Goeddel D.V., and Wells J.A. 1992. Rational design of potent antagonists to the human growth hormone receptor. Science 256: 1677–1680.

Gent J., van Kerkhof P., Roza M., Bu G., and Strous G.J. 2002. Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis. Proc. Natl. Acad. Sci. 99: 9858–9863.

Goodman H.M. 1968. Multiple effects of growth hormone on lipolysis. Endocrinology 83: 300–308.

Green H., Morikawa M., and Nixon T. 1985. A dual effector theory of growth-hormone action. Differentiation 29: 195–198.

Hara K., Hsu Chen C.J., and Sonenberg M. 1978. Recombination of the biologically active peptides from a tryptic digest of bovine growth hormone. Biochemistry 17: 550–556.

Harding P.A., Wang X., Okada S., Chen W.Y., Wan W., and Kopchick J.J. 1996. Growth hormone (GH) and a GH antagonist promote GH receptor dimerization and internalization. J. Biol. Chem. 271: 6708–6712.

Hill D.J., Riley S.C., Bassett N.S., and Waters M.J. 1992. Localization of the growth hormone receptor, identified by immunocytochemistry, in second trimester human fetal tissues and in placenta throughout gestation. J. Clin. Endocrinol. Metab. 75: 646–650.

Holdaway I.M., Rajasoorya R.C., and Gamble G.D. 2004. Factors influencing mortality in acromegaly. J. Clin. Endocrinol. Metab. 89: 667–674.

Holl R.W., Thorner M.O., and Leong D.A. 1988. Intracellular calcium concentration and growth hormone secretion in individual somatotropes: Effects of growth hormone-releasing factor and somatostatin. Endocrinology 122: 2927–2932.

Jenkins P.J. 1999. Growth hormone and exercise. Clin. Endocrinol. 50: 683–689.

Kopchick J.J. and Andry J.M. 2000. Growth hormone (GH), GH receptor, and signal transduction. Mol. Genet. Metab. 71: 293–314.

Kopchick J.J., Parkinson C., Stevens E.C., and Trainer P.J. 2002. Growth hormone receptor antagonists: Discovery, development, and use in patients with acromegaly. Endocr. Rev. 23: 623–646.

Lange K.H., Isaksson F., Juul A., Rasmussen M.H., Bulow J., and Kjaer M. 2000. Growth hormone enhances effects of endurance training on oxidative muscle metabolism in elderly women. Am. J. Physiol. Endocrinol. Metab. 279: E989–996.

Lange K.H., Lorentsen J., Isaksson F., Juul A., Rasmussen M.H., Christensen N.J., Bulow J., and Kjaer M. 2001. Endurance training and GH administration in elderly women: Effects on abdominal adipose tissue lipolysis. Am. J. Physiol. Endocrinol. Metab. 280: E886–897.

Lee P.A., Kendig J.W., and Kerrigan J.R. 2003. Persistent short stature, other potential outcomes, and the effect of growth hormone treatment in children who are born small for gestational age. Pediatrics 112: 150–162.

Leung D.W., Spencer S.A., Cachianes G., Hammonds R.G., Collins C., Henzel W.J., Barnard R., Waters M.J., and Wood W.I. 1987. Growth hormone receptor and serum binding protein: Purification, cloning and expression. Nature 330: 537–543.

Li C.H., Evans H.M., and Simpson M.E. 1945. Isolation and properties of the anterior hypophysical growth hormone. J. Biol. Chem. 159: 353–366.

Maison P., Balkau B., Simon D., Chanson P., Rosselin G., and Eschwege E. 1998. Growth hormone as a risk for premature mortality in healthy subjects: Data from the Paris prospective study. BMJ 316: 1132–1133.

Mercado M., DaVila N., McLeod J.F., and Baumann G. 1994. Distribution of growth hormone receptor messenger ribonucleic acid containing and lacking exon 3 in human tissues. J. Clin. Endocrinol. Metab. 78: 731–735.

Mertani H.C. and Morel G. 1995. In situ gene expression of growth hormone (GH) receptor and GH binding protein in adult male rat tissues. Mol. Cell. Endocrinol. 109: 47–61.

Miller W.L. and Eberhardt N.L. 1983. Structure and evolution of the growth hormone gene family. Endocr. Rev. 4: 97–130.

Muller A.F., Kopchick J.J., Flyvbjerg A., and van der Lely A.J. 2004. Clinical review 166: Growth hormone receptor antagonists. J. Clin. Endocrinol. Metab. 89: 1503–1511.

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Rapaport R., Sills I.N., Green L., Barrett P., Labus J., Skuza K.A., Chartoff A., Goode L., Stene M., and Petersen B.H. 1995. Detection of human growth hormone receptors on IM-9 cells and peripheral blood mononuclear cell subsets by flow cytometry: Correlation with growth hormone-binding protein levels. J. Clin. Endocrinol. Metab. 80: 2612–2619.

Ross R.J., Leung K.C., Maamra M., Bennett W., Doyle N., Waters M.J., and Ho K.K. 2001. Binding and functional studies with the growth hormone receptor antagonist, B2036-PEG (pegvisomant), reveal effects of pegylation and evidence that it binds to a receptor dimer. J. Clin. Endocrinol. Metab. 86: 1716–1723.

Rudman D., Feller A.G., Nagraj H.S., Gergans G.A., Lalitha P.Y., Goldberg A.F., Schlenker R.A., Cohn L., Rudman I.W., and Mattson D.E. 1990. Effects of human growth hormone in men over 60 years old. N. Engl. J. Med. 323: 1–6.

Smith W.C., Kuniyoshi J., and Talamantes F. 1989. Mouse serum growth hormone (GH) binding protein has GH receptor extracellular and substituted transmembrane domains. Mol. Endocrinol. 3: 984–990.

Trainer P.J., Drake W.M., Katznelson L., Freda P.U., Herman-Bonert V., van der Lely A.J., Dimaraki E.V., Stewart P.M., Friend K.E., Vance M.L., et al. 2000. Treatment of acromegaly with the growth hormone-receptor antagonist pegvisomant. N. Engl. J. Med. 342: 1171–1177.

Ultsch M., de Vos A.M., and Kossiakoff A.A. 1991. Crystals of the complex between human growth hormone and the extracellular domain of its receptor. J. Mol. Biol. 222: 865–868.

van der Lely A.J., Hutson R.K., Trainer P.J., Besser G.M., Barkan A.L., Katznelson L., Klibanski A., Herman-Bonert V., Melmed S., Vance M.L., et al. 2001. Long-term treatment of acromegaly with pegvisomant, a growth hormone receptor antagonist. Lancet 358: 1754–1759.

Veldhuis J.D., Bidlingmaier M., Anderson S.M., Evans W.S., Wu Z., and Strasburger C.J. 2002. Impact of experimental blockade of peripheral growth hormone (GH) receptors on the kinetics of endogenous and exogenous GH removal in healthy women and men. J. Clin. Endocrinol. Metab. 87: 5737–5745.

Wanke C., Gerrior J., Kantaros J., Coakley E., and Albrecht M. 1999. Recombinant human growth hormone improves the fat redistribution syndrome (lipodystrophy) in patients with HIV. AIDS 13: 2099–2103.

Watahiki M., Yamamoto M., Yamakawa M., Tanaka M., and Nakashima K. 1989. Conserved and unique amino acid residues in the domains of the growth hormones. Flounder growth hormone deduced from the cDNA sequence has the minimal size in the growth hormone prolactin gene family. J. Biol. Chem. 264: 312–316.

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