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GH Binding Protein, GH Receptors, and Domains Involved in Signal Transduction

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Part of the book series: Serono Symposia USA ((SERONOSYMP))

Abstract

Growth hormone (GH) and prolactin (PRL), along with placental lacto-gen, form a family of hormones that has been shown to be derived by duplication of an ancestral gene (1). The major functions of GH include effects on the growth of skeletal and soft tissues and metabolic actions, while the best-known action of PRL is lactation.

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References

  1. Niall HD, Hogan ML, Sayer R, Rosenblum IY, Greenwood FC. Sequences of pituitary and placental lactogenic and growth hormones: evolution from a primordial peptide by gene duplication. Proc Natl Acad Sci USA 1971; 68:866–9.

    Article  PubMed  CAS  Google Scholar 

  2. Leung DW, Spencer SA, Cachianes G, et al. Growth hormone receptor and serum binding protein: purification, cloning and expression. Nature 1987;330:537–43.

    Article  PubMed  CAS  Google Scholar 

  3. Boutin JM, Jolicoeur C, Okamura H, et al. Cloning and expression of the rat PRL receptor, a member of the GH/PRL receptor gene family. Cell 1988;53:69–77.

    Article  PubMed  CAS  Google Scholar 

  4. Shirota M, Banville D, Ali S, et al. Expression of two forms of the prolactin receptor in rat ovary and liver. Mol Endocrinol 1990;4:1136–43.

    Article  PubMed  CAS  Google Scholar 

  5. Davis JA, Linzer DIH. Expression of multiple forms of the prolactin receptor in mouse liver. Mol Endocrinol 1989;3:674–80.

    Article  PubMed  CAS  Google Scholar 

  6. Smith WC, Kuniyoshi J, Talamantes F. Mouse serum growth hormone (GH) binding protein has GH receptor extracellular and substituted transmembrane domains. Mol Endocrinol 1989;3:984–90.

    Article  PubMed  CAS  Google Scholar 

  7. Baumbach WR, Homer DL, Logan JS. The growth hormone-binding protein in rat serum is an alternatively spliced form of the rat growth hormone receptor. Genes Dev 1989;3:1199–205.

    Article  PubMed  CAS  Google Scholar 

  8. Sotiropoulos A, Goujon L, Simonin G, Kelly PA, Postel-Vinay MC, Finidori J. Evidence for generation of the growth hormone-binding protein through proteolysis of the growth hormone membrane receptor. Endocrinology 1993;132:1863–5.

    Article  PubMed  CAS  Google Scholar 

  9. Baumann G, Shaw MA, Winter RJ. Absence of the plasma growth hormone-binding protein in Laron-type dwarfism. J Clin Endocrinol Metab 1987; 65:814–6.

    Article  PubMed  CAS  Google Scholar 

  10. Baumann G, Amburn K, Shaw M. The circulating growth hormone-binding protein complex: a major constituent of plasma GH in man. Endocrinology 1988;122:976–84.

    Article  PubMed  CAS  Google Scholar 

  11. Tar A, Hocquette JF, Souberbielle JC, Clot JP, Brauner R, Postel-Vinay MC. Evaluation of the growth hormone-binding proteins in human plasma using HPLC-gel filtration. J Clin Endocrinol Metab 1990;71:1202–7.

    Article  PubMed  CAS  Google Scholar 

  12. Hocquette JF, Postel-Vinay MC, Djiane J, Tar A, Kelly PA. Human liver growth hormone receptor and plasma binding protein: characterization and partial purification. Endocrinology 1990;127:1665–72.

    Article  PubMed  CAS  Google Scholar 

  13. Amit T, Barkey RJ, Youdim MBH, Hochberg Z. A new and convenient assay of growth hormone-binding protein activity in human serum. J Clin Endocrinol Metab 1990;71:474–9.

    Article  PubMed  CAS  Google Scholar 

  14. Carlsson LMS, Rowland AM, Clark RG, Gesundheit N, Wong WLT. Ligand-mediated immunofunctional assay for quantitation of growth hormone-binding protein in human blood. J Clin Endocrinol Metab 1991;73:1216–23.

    Article  CAS  Google Scholar 

  15. Fairhall KM, Carmignac DF, Robinson ICAF. Growth hormone (GH) binding protein and GH interactions in vivo in the guinea pig. Endocrinology 1992;131:1963–9.

    Article  PubMed  CAS  Google Scholar 

  16. Cosman D. The hematopoietin receptor superfamily. Cytokine 1993;5: 95–106.

    Article  PubMed  CAS  Google Scholar 

  17. Cunningham BC, Wells JA. Rational design of receptor-specific variants of human growth hormone. Proc Natl Acad Sci USA 1991;88:3407–11.

    Article  PubMed  CAS  Google Scholar 

  18. Bass SH, Mulkerrin MG, Wells JA. A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor. Proc Natl Acad Sci USA 1991;88:4498–502.

    Article  PubMed  CAS  Google Scholar 

  19. de Vos AM, Ultsch M, Kossiakoff AA. Human growth hormone and extra-cellular domain of its receptor: crystal structure of the complex. Science 1992;255:257–372.

    Google Scholar 

  20. Chen WY, Wight DC, Mehta BV, Wagner TE, Kopchick JJ. Glycine 119 of bovine growth hormone is critical for growth-promoting activity. Mol Endocrinol 1991;5:1845–52.

    Article  PubMed  CAS  Google Scholar 

  21. Cunningham BC, Ultsch M, de Vos AM, Mulkerrin MG, Clauser KR, Wells JA. Dimerization of the eXtracellular domain of the human growth hormone receptor by a single hormone molecule. Science 1991;254:821–5.

    Article  PubMed  CAS  Google Scholar 

  22. Fuh G, Cunningham BC, Fukunaga R, Nagata S, Goeddel DV, Wells JA. Rational design of potent antagonists to the human growth hormone receptor. Science 1992;256:1677–80.

    Article  PubMed  CAS  Google Scholar 

  23. Elberg G, Kelly PA, Djiane J, Binder L, Gertler A. J Biol Chem 1990; 265:14770–6.

    PubMed  CAS  Google Scholar 

  24. Lesueur L, Edery M, Ali S, Paly J, Kelly PA, Djiane J. Comparison of long and short form of the prolactin receptor on prolactin-induced milk protein gene transcription. Proc Natl Acad Sci USA 1991;88:824–8.

    Article  PubMed  CAS  Google Scholar 

  25. Goujon L, Allevato G, Simonin G, et al. Cytoplasmic domains of the growth hormone receptor necessary for signal transduction. Proc Natl Acad Sci USA 1993.

    Google Scholar 

  26. Colosi P, Wong K, Leong SR, Wood WI. Mutational analysis of the intracellular domain of the human growth hormone receptor. J Biol Chem 1993;268:12617–23.

    PubMed  CAS  Google Scholar 

  27. Carter-Su C, Stubbart JR, Wang X, Stred SE, Argetsinger LS, Shafer JA. Phosphorylation of highly purified growth hormone receptors by a growth hormone receptor-associated tyrosine kinase. J Biol Chem 1989;264: 18654–61.

    PubMed  CAS  Google Scholar 

  28. Wang X, Möller C, Norstedt G, Carter-Su C. Growth hormone-promoted tyrosyl phosphorylation of a 121-kDa growth hormone receptor-associated protein. J Biol Chem 1993;268:3573–9.

    PubMed  CAS  Google Scholar 

  29. Rui H, Djeu JY, Evans GA, Kelly PA, Farrar WL. Prolactin receptor triggering: evidence for rapid tyrosine kinase activation. J Biol Chem 1992;267:24076–81.

    PubMed  CAS  Google Scholar 

  30. Rillema JA, Campbell GS, Lawson DM, Carter-Su C. Evidence for a rapid stimulation of tyrosine kinase activity by prolactin in Nb2 rat lymphoma cells. Endocrinology 1992;131:973–5.

    Article  PubMed  CAS  Google Scholar 

  31. Firmbach-Kraft I, Byers M, Shows T, Dalla-Favera R, Krolewski JJ. Tyk2, prototype of a novel class of non-receptor tyrosine kinase genes. Oncogene 1990;5:1329–36.

    PubMed  CAS  Google Scholar 

  32. Wilks AF, Harpur AG, Kurban RR, Ralph SJ, Zurcher G, Ziemiecki A. Two novel protein-tyrosine kinases, each with a second phosphotransferaserelated catalytic domain, define a new class of protein kinase. Mol Cell Biol 1991;11:2057–65.

    PubMed  CAS  Google Scholar 

  33. Harpur AG, Andres AC, Ziemiecki A, Aston RR, Wilks AF. JAK2, a third member of the JAK family of protein tyrosine kinases. Oncogene 1992;7:1347–53.

    PubMed  CAS  Google Scholar 

  34. Argetsinger LS, Campbell GS, Yang X, et al. Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell 1993;74:237–44.

    Article  PubMed  CAS  Google Scholar 

  35. Witthuhn BA, Quelle FW, Silvennoinen O, et al. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell 1993;74:227–36.

    Article  PubMed  CAS  Google Scholar 

  36. Silvennoinen O, Zitthuhn BA, Quelle FW, Cleveland JL, Yi T, Ihle JA. Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction. PNAS 1993;90:8429–33.

    Article  PubMed  CAS  Google Scholar 

  37. Lamer AC, David M, Feldman GM, et al. Tyrosine phosphorylation of DNA binding protein by multiple cytokines. Science 1993;261:1730–3.

    Article  Google Scholar 

  38. Ruff-Jamison S, Chen K, Cohen S. Induction by EGF and interferon-y of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei. Science 1993;261:1733–6.

    Article  PubMed  CAS  Google Scholar 

  39. Silvennoinen O, Schindler C, Schlessinger J, Levy DE. Ras-independent growth factor signaling by transcription factor tyrosine phosphorylation. Science 1993;261:1736–9.

    Article  PubMed  CAS  Google Scholar 

  40. Sadowski HB, Shuai K, Darnell JE Jr, Gilman MZ. A common nuclear signal transduction pathway activated by growth factor and cytokine receptors. Science 1993;261:1739–44.

    Article  PubMed  CAS  Google Scholar 

  41. Shuai K, Stark GR, Kerr IM, Darnell JE Jr. A single phosphotyrosine residue of stat 91 required for gene activation by interferon-γ. Science 1993;261:1744–6.

    Article  PubMed  CAS  Google Scholar 

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© 1995 Springer Science+Business Media New York

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Kelly, P.A. et al. (1995). GH Binding Protein, GH Receptors, and Domains Involved in Signal Transduction. In: Blackman, M.R., Roth, J., Harman, S.M., Shapiro, J.R. (eds) GHRH, GH, and IGF-I. Serono Symposia USA. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-0807-5_4

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  • DOI: https://doi.org/10.1007/978-1-4612-0807-5_4

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-6908-3

  • Online ISBN: 978-1-4612-0807-5

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