Functional domains of human growth hormone necessary for the adipogenic activity of hGH/hPL chimeric molecules

Journal of Cell Science

Volumn 112, Issue 18, 1999, Pages 3127-3135

  Juárez Aguilar, Enrique ^a   Castro Muñozledo, Federico ^a   Guerra Rodríguez, Norma E ^b   Reséndez Pérez, Diana ^b   Martínez Rodríguez, Herminia G ^b   Barrera Saldaña, Hugo A ^b   Kuri Harcuch, Walid ^a  

^a Ctro de Investigacion y de E   (Mexico)

^b Medicina UANL   (Mexico)

Author keywords

3T3 preadipocyte; Adipogenic activity; Adipose conversion; Growth hormone; hGH binding sites; Homologous mutagenesis; Placental lactogen

Indexed keywords

CHIMERIC PROTEIN; HUMAN GROWTH HORMONE; PLACENTA LACTOGEN; PLASMID DNA;

ADIPOCYTE; ANIMAL CELL; ARTICLE; BINDING SITE; CELL DIFFERENTIATION; CELL STRAIN 3T3; CONTROLLED STUDY; DNA TRANSFECTION; HORMONE RELEASE; HORMONE STRUCTURE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION;

3T3 CELLS; ADIPOSE TISSUE; ANIMALS; BINDING SITES; CELL DIFFERENTIATION; HUMAN GROWTH HORMONE; HUMANS; MICE; MODELS, MOLECULAR; MUTAGENESIS; PLACENTAL LACTOGEN; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; TRANSFECTION;

ANIMALIA; MAMMALIA;

EID: 0032828338     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (65)

1. Aloj, S. and Edelhoch, H. (1971). The molecular properties of human chorionic somatomammotropin. J. Biol. Chem. 247, 1146-1152.
2. Aubert, M. L., Bewley, T. A., Grumbach, M. M., Kaplan, S. L. and Li, C. H. (1986). Structure-function studies on human growth hormone. Evidence that tertiary structure is essential for biological activity. Int. J. Pept. Protein Res. 28, 45-57.
3. Barrera-Saldaña, H. A., Seeburg, P. H. and Saunders, G. F. (1983). Two structurally different genes produce the same secreted human placental lactogen hormone. J. Biol. Chem. 258, 3787-3793.
4. Behncken, S. N., Rowlinson, S. W., Rowland, J. E., Conway-Campbell, B. L., Monks, T. A. and Waters, M. J. (1997). Aspartate 171 is the major primate-specific determinant of human growth hormone. Engineering porcine growth hormone to activate the human receptor. J. Biol. Chem. 272, 27077-27083.
5. Bewley, T. A., Dixon, J. S. and Li, C. H. (1972). Sequence comparison of human pituitary growth hormone, human chorionic somatomammotropin and ovine pituitary growth and lactogenic hormones. Int. J. Pept. Protein Res. 4, 281-287.
6. Castro-Muñozledo, F., Marsch-Moreno, M., Beltrán-Langarica, A. and Kuri-Harcuch, W. ( 1987). Commitment of adipocyte differentiation in 3T3 cells is inhibit by retinoic acid and the expression of lipogenic enzymes is modulated through cytoskeleton stabilization. Differentiation 36, 211-219.
7. Chawla, R. J., Parks, J. S. and Rudman, D. (1983). Structural variants of human growth hormone: biochemical, genetic and clinic aspects. Annu. Rev. Med. 34, 519-547.
8. Chen, W.-Y., Chen. N., Yun, J., Wagner, T. E. and Kopchick, J. (1994). In vitro and in vivo studies of antagonistic effects of human growth hormone analogs. J. Biol. Chem. 269, 15892-15897.
9. Clarkson, R. W. E., Chen, C. M., Harrison, S., Wells, C., Muscat, G. E. O. and Waters, M. J. (1995). Early responses of trans-activating factors to growth hormone in preadipocytes: differential regulation of CCAAT enhancer-binding protein-ß (C/EBPß) and C/EBPδ. Mol. Endocrinol. 9, 108-120.
10. Clewell, D. B. and Helsinki, D. R. (1969). Supercoiled circular DNA-protein complex in Escherichia coli: purification and induced conversion to an open circular DNA form. Proc. Nat. Acad. Sci. USA 62, 1159-1166.
11. Cooke, N. E., Coit, D., Shine, J., Daxter, J. D. and Martial, J. A. (1981). Human prolactin cDNA: Structural analysis and evolutionary comparisons. J. Biol. Chem. 256, 4007-4016.
12. 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.
13. Cunningham, B. C., Ultsch, M., DeVos, 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.
14. Cunningham, B. C. and Wells, J. A. (1993). Comparison of a structural and a functional epitope. J. Mol. Biol. 234, 554-563.
15. Dattani, M. T., Hinmarsh, P. C., Brook, C. G. D., Robinson, I., Kopchick, J. J. and Marshall, N. J. (1995). G120R, a human growth hormone antagonist, shows zinc-dependent agonist and antagonist activity on Nb2 cells. J. Biol. Chem. 270, 9222-9226.
16. 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.
17. Fuh, G., Cunningham, B. C., Fukunaga, R., Nagata, S., Goeddel, D. V. and Wells, J. A. (1992). Rational design of potent antagonist to the human growth hormone receptor. Science 256, 1677-1680.
18. Fuh, G., Colosi, P., Wood, W. I. and Wells, J. A. (1993). Mechanism-based design of prolactin receptor antagonist. J. Biol. Chem. 268, 5376-5381.
19. Gertler, A., Grosclaude, J., Strasburger, C. J., Nir, S. and Djiane, J. (1996). Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization. J. Biol. Chem. 271, 24482-24491.
20. Gráf, L. and Li, C. H. (1981). Human somatotropin: covalent reconstitution of two polypeptide contiguous fragments with thrombin. Proc. Nat. Acad. Sci. USA 78, 6135-6138.
21. Green, H., Morikawa, M. and Nixon, T. (1985). A dual effector theory of growth-hormone action. Differentiation 29, 195-198.
22. Harding, P. A., Wang, X., Okada, S., Chen, W. Y., Wam, W. and Kopchick, J. J. (1996). Growth hormone (GH) and GH antagonist promote GH receptor dimerization and internalization. J. Biol. Chem. 271, 6708-6712.
23. Helman, D., Staten, N. R., Byatt, J., Grosclaude, J., McKinnie, R. E., Djiane, J. and Gertler, A. (1997). Site-directed mutagenesis of recombinant bovine placental lactogen at lysine-73 leads to selective attenuation of its somatogenic activity. Endocrinology 138, 4069-4080.
24. Hu, E., Tontonoz, P. and Spiegelman, B. M. (1995). Transdifferentiation of myoblasts by the adipogenic transcription factors PPARγ2 and C/EBPα. Proc. Nat. Acad. Sci. USA 92, 9856-9860.
25. Ilondo, M., Damholt, A., Cunningham, B. C., Wells, J., De Meyts, P. and Shymko, R. ( 1994). Receptor dimerization determines the effects of growth hormone in primary rat adipocytes and cultured human IM-9 lymphocytes. Endocrinology 134, 2397-2403.
26. Kostyo, J. L. and Wilhelmi, A. E. (1976). Conference on the structure-function relationship of pituitary growth hormone: a report. Metabolism 25, 105-124.
27. Kuri-Harcuch, W. and Green, H. (1977). Increasing activity of enzymes on pathway of triacylglycerol synthesis during adipose conversion of 3T3 cells. J. Biol. Chem. 252, 2158-2160.
28. Kuri-Harcuch W. and Green, H. (1978). Adipose conversion of 3T3 cells depends on a serum factor. Proc. Nat. Acad. Sci. USA 75, 6107-6109.
29. Kuri-Harcuch, W., Wise, L. S. and Green, H. (1978) Interruption of the adipose conversion of 3T3 cells by biotin deficiency: differentiation without triglyceride accumulation. Cell 14, 53-59.
30. Lewis, U. J., Lewis, L. J., Salem, M. A. M., Staten. N. R., Galosy, S. S., Krivi, G. G. (1991). A recombinant DNA-derived modification of human growth hormone (hGH 44-191) with enhanced diabetogenic activity. Mol. Cell. Endocrinol. 78, 45-54.
31. Li, C. H. and Graf, L. (1974). Human pituitary growth hormone: isolation and properties of two biologically active fragments from plasmin digests. Proc. Nat. Acad. Sci. USA 71,1197-1201.
32. Li, C. H. and Bewley, T. A. (1976). Human pituitary growth hormone: restoration of full biological activity by noncovalent interaction of two fragments of the hormone. Proc. Nat. Acad. Sci. USA 73, 1476-1479.
33. Lowman, H. B., Cunningham, B. C. and Wells, J. A. (1991). Mutational analysis and protein engineering of receptor-binding determinants in human placental lactogen. J. Biol. Chem. 266, 10982-10988.
34. G120RhGH does not antagonize GH in the rat, but has paradoxical agonist activity, probably via the prolactin receptor. Endocrinology 137, 447-454.
35. Mondon, C. E., Reaven, G. M., Ling, N., Lewis, U. J. and Frigeri, L. G. (1988). Amino-terminal peptide of growth hormone enhances insulin action in normal rats. Endocrinology 123, 827-833.
36. Morikawa, M., Nixon, T. and Green, H. (1982). Growth hormone and the adipose conversion of 3T3 cells. Cell 29, 783-789.
37. Morikawa, M., Green, H. and Lewis, U. J. (1984). Activity of human growth hormone and related polypeptides on the adipose conversion of 3T3 cells. Mol. Cell. Biol. 4, 228-231.
38. Ng, F. M. and Harcourt, J. A. (1986). Stimulation of 2-deoxyglucose uptake in rat adipocytes by a human growth hormone fragment (hGH 4-15). Diabetologia 29, 882-887.
39. Ng, F. M. and Rotstein, T. (1988). Pancreatic effect of a hypoglycaemic fragment of human growth hormone (hGH 6-13). Diabetes Res. 7, 103-108.
40. Nixon, T. and Green, H. (1983). Properties of growth hormone receptors in relation to the adipose conversion of 3T3 cells. J. Cell. Physiol. 115, 291-296.
41. Ohlsson, C., Nilsson, A., Isaksson, O. and Lindahl, A. (1992).Growth hormone induces multiplication of the slowly cycling germinal cells of the rat tibial growth plate. Proc. Nat. Acad. Sci. USA 89, 9826-9830.
42. Pairault, J. and Green, H. (1979). A study of the adipose conversion of suspended 3T3 cells by using glycerophosphate dehydrogenase as differentiation marker. Proc. Nat. Acad. Sci. USA 76, 5138-5142.
43. Palmiter, R. D., Behringer, R. R., Quaife, C. J., Maxwell, F., Maxwell, I. H., Brinster, R. L. (1987). Cell lineage ablation in transgenic mice by cell-specific expression of a toxin gene. Cell 50, 435-443.
44. Peña, C., Poskus, E. and Paladini, A. C. (1980). A relevant antigenic site in hGH localized in sequence 98-128. Mol. Immunol. 17, 1487-1491.
45. Ramírez-Solís, R., Reséndez-Pérez, D., Alvidrez-Quihui, L. E., Rincón-Limas, D. E., Varela-Martínez, R., Martínez-Rodríguez, H. G. and Barrera-Saldaña, H. A. (1990). New vectors for the efficient expression of mammalian genes in cultured cells. Gene 87, 291-294.
46. Ray, J., Okamura, H., Kelly, P. A., Liebhaber, S. A. and Cooke, N. E. (1990). Alteration in the receptor binding specificity of human growth hormone by genomic exon exchange. Mol. Endocrinol. 4, 101-107.
47. Reagan, C. R., Mills, J. B., Kostyo, J. L. and Wilhelmi, A. E. (1975). Isolation and biological characterization of fragments of human growth hormone produced by digestion with plasmin. Endocrinology 96, 625-636.
48. Résendez-Pérez, D. and Barrera-Saldaña, H. A. (1990). Expression studies of transfected multigene families by homologous DNA mutagenesis. Biotechniques 9, 281-286.
49. Reséndez-Pérez, D., Ramírez-Solís, T., Varela-Echavarría, A., Martínez-Rodríguez, H. G. and Barrera-Saldaña, H. A. (1990). Coding potential of transfected human placental lactogen genes. Nucl. Acids Res. 18, 4665-4670.
50. Salazar-Olivo, L. A., Castro-Muñozledo, F. and Kuri-Harcuch, W. (1995). A preadipose 3T3 cell variant highly sensitive to adipogenic factors and to human growth hormone. J. Cell Sci. 108, 2101-2107.
51. Salem, M. A. (1988). Effects of the amino-terminal portion of human growth hormone on glucose clearance and metabolism in normal, diabetic, hypophysectomized and diabetic-hypophysectomized rats. Endocrinology 123, 1565-1576.
52. Sambrook, J. M., Fritsch, E. F. and Maniatis, T. (1989). Molecular Cloning. A Laboratory Manual. 2nd edn. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY.
53. Schwartz, J. (1984). Growth hormone directly alters glucose metabolism in 3T3 adipocytes. Biochem. Biophys. Res. Commun. 125, 237-243.
54. Schwartz, J. and Carter-Su, C. (1988). Effects of growth hormone on glucose metabolism and glucose transport in 3T3-F442A cells: Dependence on cell differentiation. Endocrinology 122, 2247-2256.
55. Silva, C. M., Weber, M. J. and Thorner, M. O. (1993). Stimulation of tyrosine phosphorylalion in human cells by activation of the growth hormone receptor. Endocrinology 132, 101-108.
56. Singh, R. N. P., Seavey, B. K., Lewis, L. J. and Lewis, U. J. (1983). Human growth hormone peptide 1-43: isolation from pituitary glands. J. Protein Chem. 2, 425-436.
57. Sonenberg, M., Kikutani M., Free, C. A., Nadler, A. C. and Dellacha, J. M. (1968). Chemical and biological characterization of clinically active tryptic digests of bovine growth hormone. Ann. NY Acad. Sci. 148, 532-558.
58. Stevenson, R. W., Stebbing, N., Rudman, C. G., Williams, P. E. and Cherrington, A. D. (1987). The synthetic 32-46 fragment of human growth hormone increases insulin and glucagon levels in the conscious dog. Metabolism 36, 400-404.
59. Takahashi, Y., Shirono, H., Arisaka, O., Takahashi, K., Yagi, T., Koga, J., Kaji, H., Okimura, Y., Abe, H., Tanaka, T. and Chijara, K. (1997). Biologically inactive growth hormone caused by an amino acid substitution J. Clin. Invest. 100, 1159-1165.
60. Tontonoz, P., Hu, E., Graves, R. A., Budavari, A. I. and Spiegelman, B. M. (1994). mPPARγ2: tissue-specific regulator of an adipocyte enhancer. Genes Dev. 8, 1224-1234.
61. Uchida, E., Shimokawa, S., Nishida, Y., Takasu, H., Ikehara, M., Uesugi, S., Tomita, K., Morikawa, M., Hayakawa, T. and Nishikawa, S. (1990). An active site of growth hormone for eliciting the differentiation of preadipose 3T3-F442A cells to adipose cells. Biochem. Biophys. Res. Commun. 172, 357-363.
62. Vashdi-Elberg, D., Staten, N. R., Sakal, E., Krivi, G. G. and Gertler, A. (1995). N-Terminal-truncated recombinant analogs of bovine placental lactogen: Interaction with human and rat growth hormone receptors and insulin-like growth factor-I secretion mediated by somatogenic receptors in rat hepatocytes. Endocrinology 136, 1258-1266.
63. Wells, J. A. and de Vos, A. M. (1996). Hematopoietic receptor complexes. Annu. Rev. Biochem. 65, 609-634.
64. Wise, L. S. and Green, H. (1979). Participation of one isoenzyme of cytosolic glycerophosphate dehydrogenase in the adipose conversion of 3T3 cells. J. Biol. Chem. 254, 273-275.
65. Yamasaki, N., Kikitani, M. and Sonenberg, M. (1970). Peptides of a biologically active tryptic digest of bovine growth hormone. Biochemistry 9, 1107-1114.