DOI QR코드

DOI QR Code

Growth Hormone Signaling in the Regulation of Acid Labile Subunit

  • Kim, Jin Wook (Department of Animal Science, College of Agriculture and Life Sciences, Cornell University) ;
  • Boisclair, Yves R. (Division of Applied Life Sciences (Institute of Agriculture and Life Science), College of Agriculture and Life Sciences Gyeongsang National University)
  • 투고 : 2007.09.05
  • 심사 : 2007.11.12
  • 발행 : 2008.05.01

초록

The past decades have seen enormous advances in our understanding of how GH acts. GH is a pituitary-derived polypeptide hormone that has diverse physiological effects including the regulation of bone growth, carbohydrate and lipid metabolism. The effects of GH are mediated directly and indirectly through IGF-I. In addition, GH stimulates the hepatic production of ALS. In postnatal life, IGF-I and -II circulate as 150 kDa ternary complexes consisting of one molecule each of IGFBP-3 or IGFBP-5, IGF-I or IGF-II and ALS. It is now known that ALS increases significantly the half-lives of the IGFs, IGFBP-3 and -5, and therefore is responsible for maintaining a circulating reservoir for each of these proteins.

키워드

참고문헌

  1. Adams, T. E., J. A. Hansen, R. Starr, N. A. Nicola, D. J. Hilton and N. Billestrup. 1998. Growth hormone preferentially induces the rapid, transient expression of SOCS-3, a novel inhibitor of cytokine receptor signaling. J. Biol. Chem. 273:1285-1287. https://doi.org/10.1074/jbc.273.3.1285
  2. Agarwal, S. K., L. A. Cogburn and J. Burnside. 1994. Dysfunctional growth hormone receptor in a strain of sexlinked dwarf chicken: evidence for a mutation in the intracellular domain. J. Endocrinol. 142:427-434. https://doi.org/10.1677/joe.0.1420427
  3. Akers, R. M. 1985. Lactogenic hormones: binding sites, mammary growth, secretory cell differentiation, and milk biosynthesis in ruminants. J. Dairy Sci. 68:501-519. https://doi.org/10.3168/jds.S0022-0302(85)80849-3
  4. Argetsinger, L. S., G. W. Hsu, M. G. Myers Jr., N. Billestrup, M. F. White and C. Carter-Su. 1995. Growth hormone, interferon gamma, and leukemia inhibitory factor promoted tyrosyl phosphorylation of insulin receptor substrate-1. J. Biol. Chem. 270:14685-14692. https://doi.org/10.1074/jbc.270.24.14685
  5. Argetsinger, L. S., G. Norstedt, N. Billestrup, M. F. White and C. Carter-Su. 1996. Growth hormone, interferon-gamma, and leukemia inhibitory factor utilize insulin receptor substrate-2 in intracellular signaling. J. Biol. Chem. 271:29415-19421. https://doi.org/10.1074/jbc.271.46.29415
  6. Baker, J., J. P. Liu, E. J. Robertson and A. Efstratiadis. 1993. Role of insulin-like growth factors in embryonic and postnatal growth. Cell 75:73-82. https://doi.org/10.1016/S0092-8674(05)80085-6
  7. Barbano, D. M., J. M. Lynch, D. E. Bauman, G. F. Hartnell, R. L. Hintz and M. A. Nemeth. 1992. Effect of a prolonged-release formation of N-methionyl bovine somatotropin (sometribove) on milk composition. J. Dairy Sci. 75:1775-1793. https://doi.org/10.3168/jds.S0022-0302(92)77937-5
  8. Barreca, A., P. Ponzani, M. Arvigo, G. Giordano and F. Minuto. 1995. Effect of the acid-labile subunit on the binding of insulin-like growth factor (IGF)-binding protein-3 to [125I]IGF-I. J. Clin. Endocrinol. Metab. 80:1318-1324. https://doi.org/10.1210/jc.80.4.1318
  9. Bauman, D. E. 1999. Bovine somatotropin and lactation: from basic science to commercial application. Domest. Anim. Endocrinol. 17:101-116. https://doi.org/10.1016/S0739-7240(99)00028-4
  10. Bauman, D. E. and R. G. Vernon. 1993. Effects of exogenous bovine somatotropin on lactation. Annu. Rev. Nutr. 13:437-461. https://doi.org/10.1146/annurev.nu.13.070193.002253
  11. Baumbach, W. R., D. L. Horner and J. S. Logan. 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. https://doi.org/10.1101/gad.3.8.1199
  12. Baxter, R. C. 1988. Characterization of the acid-labile subunit of the growth hormone-dependent insulin-like growth factor binding protein complex. J. Clin. Endocrinol. Metab. 67:265-272. https://doi.org/10.1210/jcem-67-2-265
  13. Baxter, R. C. 1990. Circulating levels and molecular distribution of the acid-labile (alpha) subunit of the high molecular weight insulin-like growth factor- binding protein complex. J. Clin. Endocrinol. Metab. 70:1347-1353. https://doi.org/10.1210/jcem-70-5-1347
  14. Baxter, R. C. and W. H. Daughaday. 1991. Impaired formation of the ternary insulin-like growth factor-binding protein complex in patients with hypoglycemia due to nonislet cell tumors. J. Clin. Endocrinol. Metab. 73:696-702. https://doi.org/10.1210/jcem-73-4-696
  15. Baxter, R. C. and J. L. Martin. 1989. Structure of the Mr 140,000 growth hormone-dependent insulin-like growth factor binding protein complex: determination by reconstitution and affinitylabeling. Proc. Natl. Acad. Sci. USA 86:6898-6902. https://doi.org/10.1073/pnas.86.18.6898
  16. Baxter, R. C., J. L. Martin and V. A. Beniac. 1989. High molecular weight insulin-like growth factor binding protein complex. Purification and properties of the acid-labile subunit from human serum. J. Biol. Chem. 264:11843-11848.
  17. Bereket, A., T. A. Wilson, S. L. Blethen, Y. Sakurai, D. N. Herndon, R. R. Wolfe and C. H. Lang. 1996. Regulation of the acid-labile subunit of the insulin-like growth factor ternary complex in patients with insulin-dependent diabetes mellitus and severe burns. Clin. Endocrinol. (Oxf) 44:525-532. https://doi.org/10.1046/j.1365-2265.1996.726547.x
  18. Binoux, M. and P. Hossenlopp. 1988. Insulin-like growth factor (IGF) and IGF-binding proteins: comparison of human serum and lymph. J. Clin. Endocrinol. Metab. 67:509-514. https://doi.org/10.1210/jcem-67-3-509
  19. Boisclair, Y. R., D. E. Bauman, A. W. Bell, F. R. Dunshea and M. Harkins. 1994. Nutrient utilization and protein turnover in the hindlimb of cattle treated with bovine somatotropin. J. Nutr. 124:664-673. https://doi.org/10.1093/jn/124.5.664
  20. Boisclair, Y. R., D. Seto, S. Hsieh, K. R. Hurst and G. T. Ooi. 1996. Organization and chromosomal localization of the gene encoding the mouse acid labile subunit of the insulin-like growth factor binding complex. Proc. Natl. Acad. Sci. USA 93:10028-10033. https://doi.org/10.1073/pnas.93.19.10028
  21. Boisclair, Y. R., J. Wang, J. Shi, K. R. Hurst and G. T. Ooi. 2000. Role of the suppressor of cytokine signaling-3 in mediating the inhibitory effects of interleukin-1beta on the growth hormonedependent transcription of the acid-labile subunit gene in liver cells. J. Biol. Chem. 275:3841-3847. https://doi.org/10.1074/jbc.275.6.3841
  22. Bousquet, C., C. Susini and S. Melmed. 1999. Inhibitory roles for SHP-1 and SOCS-3 following pituitary proopiomelanocortin induction by leukemia inhibitory factor. J. Clin. Invest. 104:1277-1285. https://doi.org/10.1172/JCI7924
  23. Bruning, J. C., J. Winnay, B. Cheatham and C. R. Kahn. 1997. Differential signaling by insulin receptor substrate 1 (IRS-1) and IRS-2 in IRS-1-deficient cells. Mol. Cell. Biol. 17:1513-1521. https://doi.org/10.1128/MCB.17.3.1513
  24. Burrin, D. G., T. A. Davis, M. L. Fiorotto and P. J. Reeds. 1997. Role of milk-borne vs. endogenous insulin-like growth factor I in neonatal growth. J. Anim. Sci. 75:2739-2743. https://doi.org/10.2527/1997.75102739x
  25. Butler, J. H. and P. D. Gluckman. 1986. Circulating insulin-like growth factor-binding proteins in fetal, neonatal and adult sheep. J. Endocrinol. 109:333-338. https://doi.org/10.1677/joe.0.1090333
  26. Campbell, G. S., D. J. Meyer, R. Raz, D. E. Levy, J. Schwartz and C. Carter-Su. 1995. Activation of acute phase response factor (APRF)/Stat3 transcription factor by growth hormone. J. Biol. Chem. 270:3974-3979. https://doi.org/10.1074/jbc.270.8.3974
  27. Campbell, R. G., R. J. Johnson, M. R. Taverner and R. H. King. 1991. Interrelationships between exogenous porcine somatotropin (PST) administration and dietary protein and energy intake on protein deposition capacity and energy metabolism of pigs. J. Anim. Sci. 69:1522-1531. https://doi.org/10.2527/1991.6941522x
  28. Carter-Su, C., L. Rui and J. Herrington. 2000a. Role of the tyrosine kinase JAK2 in signal transduction by growth hormone. Pediatr. Nephrol. 14:550-557. https://doi.org/10.1007/s004670000366
  29. Carter-Su, C., L. Rui and M. R. Stofega. 2000b. SH2-B and SIRP: JAK2 binding proteins that modulate the actions of growth hormone. Recent. Prog. Horm. Res. 55:293-311.
  30. Chalupa, W. and D. T. Galligan. 1989. Nutritional implications of somatotropin for lactating cows. J. Dairy Sci. 72:2510-2524. https://doi.org/10.3168/jds.S0022-0302(89)79391-7
  31. Chin, E., J. Zhou, J. Dai, R. C. Baxter and C. A. Bondy. 1994. Cellular localization and regulation of gene expression for components of the insulin-like growth factor ternary binding protein complex. Endocrinol. 134:2498-2504. https://doi.org/10.1210/en.134.6.2498
  32. Chung, C. S., T. D. Etherton and J. P. Wiggins. 1985. Stimulation of swine growth by porcine growth hormone. J. Anim. Sci. 60:118-130. https://doi.org/10.2527/jas1985.601118x
  33. Cobb, M. H. 1999. MAP kinase pathways. Prog. Biophys. Mol. Biol. 71:479-500. https://doi.org/10.1016/S0079-6107(98)00056-X
  34. Cohick, W. S. 1998. Role of the insulin-like growth factors and their binding proteins in lactation. J. Dairy Sci. 81:1769-1777. https://doi.org/10.3168/jds.S0022-0302(98)75746-7
  35. Cramer, S. D. and F. Talamantes. 1993. The growth hormone receptor and growth hormone-binding protein:structure, functions, and regulation. New York.
  36. Dai, J. and R. C. Baxter. 1992. Molecular cloning of the acidlabile subunit of the rat insulin-like growth factor binding protein complex. Biochem. Biophys. Res. Commun. 188:304-309. https://doi.org/10.1016/0006-291X(92)92385-B
  37. Dai, J. and R. C. Baxter. 1994. Regulation in vivo of the acid-labile subunit of the rat serum insulin-like growth factor-binding protein complex. Endocrinology 135:2335-2341. https://doi.org/10.1210/en.135.6.2335
  38. Dai, J., C. D. Scott and R. C. Baxter. 1994. Regulation of the acidlabile subunit of the insulin-like growth factor complex in cultured rat hepatocytes. Endocrinol. 135:1066-1072. https://doi.org/10.1210/en.135.3.1066
  39. Daughaday, W. H., K. Hall, M. S. Raben, W. D. Salmon Jr., J. L. van den Brande and J. J. van Wyk. 1972. Somatomedin: proposed designation for sulphation factor. Nature 235:107. https://doi.org/10.1038/235107a0
  40. Daughaday, W. H. and P. Rotwein. 1989. Insulin-like growth factors I and II. Peptide, messenger ribonucleic acid and gene structures, serum, and tissue concentrations. Endocr. Rev. 10:68-91. https://doi.org/10.1210/edrv-10-1-68
  41. Davey, H. W., M. J. McLachlan, R. J. Wilkins, D. J. Hilton and T. E. Adams. 1999. STAT5b mediates the GH-induced expression of SOCS-2 and SOCS-3 mRNA in the liver. Mol. Cell. Endocrinol. 158:111-116. https://doi.org/10.1016/S0303-7207(99)00175-6
  42. Davey, H. W., T. Xie, M. J. McLachlan, R. J. Wilkins, D. J. Waxman and D. R. Grattan. 2001. STAT5b is required for GHinduced liver IGF-I gene expression. Endocrinology 142:3836-3841. https://doi.org/10.1210/en.142.9.3836
  43. Davis, T. A., M. L. Fiorotto, D. G. Burrin, W. G. Pond and H. V. Nguyen. 1997. Intrauterine growth restriction does not alter response of protein synthesis to feeding in newborn pigs. Am. J. Physiol. 272:E877-884.
  44. Delhanty, P. and R. C. Baxter. 1996. The cloning and expression of the baboon acid-labile subunit of the insulin-like growth factor binding protein complex. Biochem. Biophys. Res. Commun. 227:897-902. https://doi.org/10.1006/bbrc.1996.1602
  45. Delhanty, P. J. and R. C. Baxter. 1998. The regulation of acidlabile subunit gene expression and secretion by cyclic adenosine 3',5'-monophosphate. Endocrinol. 139:260-265. https://doi.org/10.1210/en.139.1.260
  46. Domene, H. M., M. S. Bengolia, A. S. Martinez, M. G. Ropelato, P. Pennisi, P. H. J. Scaglia and H. G. Jasper. 2004. Deficiency of the circulating insulin-like growth factor system associated with inactivation of the acid-labile subunit gene. The New England Journal of Medicine 350:570-577. https://doi.org/10.1056/NEJMoa013100
  47. Donaghy, A. J., P. J. Delhanty, K. K. Ho, R. Williams and R. C. Baxter. 2002. Regulation of the growth hormone receptor/binding protein, insulin-like growth factor ternary complex system in human cirrhosis. J. Hepatol. 36:751-758. https://doi.org/10.1016/S0168-8278(02)00049-1
  48. Doris, R., R. G. Vernon, M. D. Houslay and E. Kilgour. 1994. Growth hormone decreases the response to anti-lipolytic agonists and decreases the levels of Gi2 in rat adipocytes. Biochem. J. 297 ( Pt 1):41-45. https://doi.org/10.1042/bj2970041
  49. Doris, R. A., G. E. Thompson, E. Finley, E. Kilgour, M. D. Houslay and R. G. Vernon. 1996. Chronic effects of somatotropin treatment on response of subcutaneous adipose tissue lipolysis to acutely acting factors in vivo and in vitro. J. Anim. Sci. 74:562-568. https://doi.org/10.2527/1996.743562x
  50. Dunshea, F. R., D. M. Harris, D. E. Bauman, R. D. Boyd and A. W. Bell. 1992. Effect of porcine somatotropin on in vivo glucose kinetics and lipogenesis in growing pigs. J. Anim. Sci. 70:141-151. https://doi.org/10.2527/1992.701141x
  51. Edens, A. and F. Talamantes. 1998. Alternative processing of growth hormone receptor transcripts. Endocr. Rev. 19:559-582. https://doi.org/10.1210/er.19.5.559
  52. Eisemann, J. H., A. C. Hammond, D. E. Bauman, P. J. Reynolds, S. N. McCutcheon, H. F. Tyrrell and G. L. Haaland. 1986. Effect of bovine growth hormone administration on metabolism of growing Hereford heifers: protein and lipid metabolism and plasma concentrations of metabolites and hormones. J. Nutr. 116:2504-2515. https://doi.org/10.1093/jn/116.12.2504
  53. Eisemann, J. H., A. C. Hammond, T. S. Rumsey and D. E. Bauman. 1989. Nitrogen and protein metabolism and metabolites in plasma and urine of beef steers treated with somatotropin. J. Anim. Sci. 67:105-115. https://doi.org/10.2527/jas1989.671105x
  54. Etherton, T. D. and D. E. Bauman. 1998. Biology of somatotropin in growth and lactation of domestic animals. Physiol. Rev. 78:745-761. https://doi.org/10.1152/physrev.1998.78.3.745
  55. Etherton, T. D., I. Louveau, M. T. Sorensen and S. Chaudhuri. 1993. Mechanisms by which somatotropin decreases adipose tissue growth. Am. J. Clin. Nutr. 58:287S-295S. https://doi.org/10.1093/ajcn/58.2.287S
  56. Etherton, T. D., J. P. Wiggins, C. M. Evock, C. S. Chung, J. F. Rebhun, P. E. Walton and N. C. Steele. 1987. Stimulation of pig growth performance by porcine growth hormone: determination of the dose-response relationship. J. Anim. Sci. 64:433-443. https://doi.org/10.2527/jas1987.642433x
  57. Evock, C. M., T. D. Etherton, C. S. Chung and R. E. Ivy. 1988. Pituitary porcine growth hormone (pGH) and a recombinant pGH analog stimulate pig growth performance in a similar manner. J. Anim. Sci. 66:1928-1941. https://doi.org/10.2527/jas1988.6681928x
  58. Finidori, J. 2000. Regulators of growth hormone signaling. Vitam. Horm. 59:71-97. https://doi.org/10.1016/S0083-6729(00)59004-9
  59. Firth, S. M., U. Ganeshprasad and R. C. Baxter. 1998. Structural determinants of ligand and cell surface binding of insulin-like growth factor-binding protein-3. J. Biol. Chem. 273:2631-2638. https://doi.org/10.1074/jbc.273.5.2631
  60. Fowden, A. L. 1995. Endocrine regulation of fetal growth. Reprod. Fertil. Dev. 7:351-363. https://doi.org/10.1071/RD9950351
  61. Frystyk, J., P. J. Delhanty, C. Skjaerbaek and R. C. Baxter. 1999. Changes in the circulating IGF system during short-term fasting and refeeding in rats. Am. J. Physiol. 277:E245-252.
  62. Frystyk, J., H. Gronbaek, C. Skjaerbaek, A. Flyvbjerg, H. Orskov and R. C. Baxter. 1998. Developmental changes in serum levels of free and total insulin-like growth factor I (IGF-I), IGF-binding protein-1 and -3, and the acid-labile subunit in rats. Endocrinology 139:4286-4292. https://doi.org/10.1210/en.139.10.4286
  63. Fukuda, I., M. Hotta, N. Hizuka, K. Takano, Y. Ishikawa, K. Asakawa-Yasumoto, E. Tagami and H. Demura. 1999. Decreased serum levels of acid-labile subunit in patients with anorexia nervosa. J. Clin. Endocrinol. Metab. 84:2034-2036. https://doi.org/10.1210/jc.84.6.2034
  64. Gargosky, S. E., P. Tapanainen and R. G. Rosenfeld. 1994. Administration of growth hormone (GH), but not insulin-like growth factor-I (IGF-I), by continuous infusion can induce the formation of the 150-kilodalton IGF-binding protein-3 complex in GH-deficient rats. Endocrinol. 134:2267-2276. https://doi.org/10.1210/en.134.5.2267
  65. Gaur, S., H. Yamaguchi and H. M. Goodman 1996. Growth hormone increases calcium uptake in rat fat cells by a mechanism dependent on protein kinase C. Am. J. Physiol. 270:C1485-1492. https://doi.org/10.1152/ajpcell.1996.270.5.C1485
  66. Gertler, A., A. Ashkenazi and Z. Madar. 1984. Binding sites of human growth hormone and ovine and bovine prolactins in the mammary gland and the liver of lactating dairy cow. Mol. Cell. Endocrinol. 34:51-57. https://doi.org/10.1016/0303-7207(84)90158-8
  67. Glimm, D. R., V. E. Baracos and J. J. Kennelly. 1990. Molecular evidence for the presence of growth hormone receptors in the bovine mammary gland. J. Endocrinol. 126:R5-8. https://doi.org/10.1677/joe.0.126R005
  68. Glimm, D. R., V. E. Baracos and J. J. Kennelly. 1992. Northern and in situ hybridization analyses of the effects of somatotropin on bovine mammary gene expression. J. Dairy Sci. 75:2687-2705. https://doi.org/10.3168/jds.S0022-0302(92)78031-X
  69. Goodman, G. T., R. M. Akers, K. H. Friderici and H. A. Tucker. 1983. Hormonal regulation of alpha-lactalbumin secretion from bovine mammary tissue cultured in vitro. Endocrinol. 112:1324-1330. https://doi.org/10.1210/endo-112-4-1324
  70. Gopinath, R. and T. D. Etherton. 1989. Effects of porcine growth hormone on glucose metabolism of pigs: II. Glucose tolerance, peripheral tissue insulin sensitivity and glucose kinetics. J. Anim. Sci. 67:689-697. https://doi.org/10.2527/jas1989.673689x
  71. Gu, F., N. Dube, J. W. Kim, A. Cheng, J. Ibarra-Sanchez Mde, M. L.Tremblay and Y. R. Boisclair. 2003. Protein tyrosine phosphatase 1B attenuates growth hormone-mediated JAK2-STAT signaling. Mol. Cell. Biol. 23:3753-3762. https://doi.org/10.1128/MCB.23.11.3753-3762.2003
  72. Gurland, G., G. Ashcom, B. H. Cochran and J. Schwartz. 1990. Rapid events in growth hormone action. Induction of c-fos and c-jun transcription in 3T3-F442A preadipocytes. Endocrinol. 127:3187-3195. https://doi.org/10.1210/endo-127-6-3187
  73. Hackett, R. H., Y. D. Wang, S. Sweitzer, G. Feldman, W. I. Wood. and A. C. Larner. 1997. Mapping of a cytoplasmic domain of the human growth hormone receptor that regulates rates of inactivation of Jak2 and Stat proteins. J. Biol. Chem. 272:11128-11132. https://doi.org/10.1074/jbc.272.17.11128
  74. Haluzik, M., S. Yakar, O. Gavrilova, J. Setser, Y. Boisclair and D. LeRoith. 2003. Insulin resistance in the liver-specific IGF-1 gene-deleted mouse is abrogated by deletion of the acid-labile subunit of the IGF-binding protein-3 complex: relative roles of growth hormone and IGF-1 in insulin resistance. Diabetes 52:2483-2489. https://doi.org/10.2337/diabetes.52.10.2483
  75. Hammond, A. C., T. H. Elsasser and T. A. Olson. 1991. Endocrine characteristics of a miniature condition in Brahman cattle: circulating concentrations of some growth-related hormones. Proc. Soc. Exp. Biol. Med. 197:450-457.
  76. Harris, D. M., F. R. Dunshea, D. E. Bauman, R. D. Boyd, S. Y. Wang, P. A. Johnson and S. D. Clarke. 1993. Effect of in vivo somatotropin treatment of growing pigs on adipose tissue lipogenesis. J. Anim. Sci. 71:3293-300. https://doi.org/10.2527/1993.71123293x
  77. Hashimoto, R., M. Ono, H. Fujiwara, N. Higashihashi, M. Yoshida, T. Enjoh-Kimura and K. Sakano. 1997. Binding sites and binding properties of binary and ternary complexes of insulinlike growth factor-II (IGF-II), IGF-binding protein-3, and acidlabile subunit. J. Biol. Chem. 272:27936-27942. https://doi.org/10.1074/jbc.272.44.27936
  78. Hauser, S. D., M. F. McGrath, R. J. Collier and G. G. Krivi. 1990. Cloning and in vivo expression of bovine growth hormone receptor mRNA. Mol. Cell. Endocrinol. 72:187-200. https://doi.org/10.1016/0303-7207(90)90143-V
  79. Heap, D., R. J. Collier, C. K. Boyd and M. C. Lucy. 1996. Expression of alternate growth hormone receptor messenger RNA in ovary and uterus of cattle. Domest. Anim. Endocrinol. 13:421-430. https://doi.org/10.1016/0739-7240(96)00072-0
  80. Heap, D., M. C. Lucy, R. J. Collier, C. K. Boyd and W. C. Warren. 1995. Rapid communication: nucleotide sequence of the promoter and first exon of the somatotropin receptor gene in cattle. J. Anim. Sci. 73:1529. https://doi.org/10.2527/1995.7351529x
  81. Herrington, J. and C. Carter-Su. 2001. Signaling pathways activated by the growth hormone receptor. Trends Endocrinol. Metab. 12:252-257. https://doi.org/10.1016/S1043-2760(01)00423-4
  82. Herrington, J., L. S. Smit, J. Schwartz and C. Carter-Su. 2000. The role of STAT proteins in growth hormone signaling. Oncogene 19:2585-2597. https://doi.org/10.1038/sj.onc.1203526
  83. Hodge, C., J. Liao, M. Stofega, K. Guan, C. Carter-Su and J. Schwartz, J. 1998. Growth hormone stimulates phosphorylation and activation of elk-1 and expression of c-fos, egr-1, and junB through activation of extracellular signalregulated kinases 1 and 2. J. Biol. Chem. 273:31327-1336. https://doi.org/10.1074/jbc.273.47.31327
  84. Hodgkinson, S. C., L. Moore, J. R. Napier, S. R. Davis, J. J. Bass and P. D. Gluckman. 1989. Characterization of insulin-like growth factor binding proteins in ovine tissue fluids. J. Endocrinol. 120:429-438. https://doi.org/10.1677/joe.0.1200429
  85. Holland, M. D., K. L. Hossner, S. E. Williams, C. R. Wallace, G. D. Niswender and K. G. Odde. 1997. Serum concentrations of insulin-like growth factors and placental lactogen during gestation in cattle. I. Fetal profiles. Domest. Anim. Endocrinol. 14:231-239. https://doi.org/10.1016/S0739-7240(97)00023-4
  86. Horber, F. F. and M. W. Haymond. 1990. Human growth hormone prevents the protein catabolic side effects of prednisone in humans. J. Clin. Invest. 86:265-272. https://doi.org/10.1172/JCI114694
  87. Houseknecht, K. L., D. A. Dwyer, D. P. Lanna and D. E. Bauman. 1995. Effect of somatotropin on adipose tissue metabolism: ontogeny of the enhanced response to adrenergic challenge in the lactating cow. Domest. Anim. Endocrinol. 12:105-113. https://doi.org/10.1016/0739-7240(94)00013-Q
  88. Hughes, S. C., H. D. Mason, S. Franks and J. M. Holly. 1997. The insulin-like growth factors (IGFs) in follicular fluid are predominantly bound in the ternary complex. J. Endocrinol. 155:R1-4. https://doi.org/10.1677/joe.0.155R001
  89. Imada, K. and W. J. Leonard. 2000. The Jak-STAT pathway. Mol. Immunol. 37:1-11. https://doi.org/10.1016/S0161-5890(00)00018-3
  90. Ingvartsen, K. L. and J. B. Andersen. 2000. Integration of metabolism and intake regulation: a review focusing on periparturient animals. J. Dairy Sci. 83:1573-1597. https://doi.org/10.3168/jds.S0022-0302(00)75029-6
  91. Janosi, J. B., S. M. Firth, J. J. Bond, R. C. Baxter and P. J. Delhanty. 1999a. N-Linked glycosylation and sialylation of the acid-labile subunit. Role in complex formation with insulinlike growth factor (IGF)-binding protein-3 and the IGFs. J. Biol. Chem. 274:5292-5298. https://doi.org/10.1074/jbc.274.9.5292
  92. Janosi, J. B., P. A. Ramsland, M. R. Mott, S. M. Firth, R. C. Baxter and P. J. Delhanty. 1999b. The acid-labile subunit of the serum insulin-like growth factor-binding protein complexes. Structural determination by molecular modeling and electron microscopy. J. Biol. Chem. 274:23328-23332. https://doi.org/10.1074/jbc.274.33.23328
  93. Jiang, H. and M. C. Lucy. 2001a. Involvement of hepatocyte nuclear factor-4 in the expression of the growth hormone receptor 1A messenger ribonucleic acid in bovine liver. Mol. Endocrinol. 15:1023-1034. https://doi.org/10.1210/me.15.6.1023
  94. Jiang, H. and M. C. Lucy. 2001b. Variants of the 5'-untranslated region of the bovine growth hormone receptor mRNA: isolation, expression and effects on translational efficiency. Gene 265:45-53. https://doi.org/10.1016/S0378-1119(01)00356-0
  95. Jiang, H., C. S. Okamura, C. K. Boyd and M. C. Lucy. 2000. Identification of Sp1 as the transcription factor for the alternative promoter P2 of the bovine growth hormone receptor gene. J. Mol. Endocrinol. 24:203-214. https://doi.org/10.1677/jme.0.0240203
  96. Jiang, H., C. S. Okamura and M. C. Lucy. 1999. Isolation and characterization of a novel promoter for the bovine growth hormone receptor gene. J. Biol. Chem. 274:7893-7900. https://doi.org/10.1074/jbc.274.12.7893
  97. Jiang, H., Y. Wang, M. Wu, Z. Gu, S. J. Frank and R. Torres-Diaz. 2007. Growth hormone stimulates hepatic expression of bovine growth hormone receptor mRNA through STATactivation of a major growth hormone receptor gene promoter. Endocrinol. 148(7):3307-3315. https://doi.org/10.1210/en.2006-1738
  98. Katz, L. E., F. Liu, B. Baker, M. S. Agus, S. E. Nunn, R. L. Hintz and P. Cohen. 1996. The effect of growth hormone treatment on the insulin-like growth factor axis in a child with nonislet cell tumor hypoglycemia. J. Clin. Endocrinol. Metab. 81:1141-1146. https://doi.org/10.1210/jc.81.3.1141
  99. Keys, J. E. and J. Djiane. 1988. Prolactin and growth hormone binding in mammary and liver tissue of lactating cows. J. Recept. Res. 8:731-750. https://doi.org/10.3109/10799898809049022
  100. Khosravi, M. J., A. Diamandi, J. Mistry, R. G. Krishna and A. Khare. 1997. Acid-labile subunit of human insulin-like growth factor-binding protein complex: measurement, molecular, and clinical evaluation. J. Clin. Endocrinol. Metab. 82:3944-3951. https://doi.org/10.1210/jc.82.12.3944
  101. Kim, J. W., R. P. Rhoads, S. S. Block, T. R. Overton, S. J. Frank and Y. R. Boisclair. 2004. Dairy cows experience selective reduction of the hepatic growth hormone receptor during the periparturient period. J. Endocrinol. 181:281-290. https://doi.org/10.1677/joe.0.1810281
  102. Kim, J. W., R. P. Rhoads, N. Segoale, N. B. Kristensen, D. E. Bauman and Y. R. Boisclair. 2006. Isolation of the cDNA encoding the acid labile subunit (ALS) of the 150 kDa IGFbinding protein complex in cattle and ALS regulation during the transition from pregnancy to lactation. J. Endocrinol. 189:583-593. https://doi.org/10.1677/joe.1.06824
  103. Kitagawa, H., K. Kitoh, T. Ito, Y. Ohba, N. Nishii, K. Katoh, Y. Obara, Y. Motoi and Y. Sasaki. 2001. Serum growth hormone and insulin-like growth factor-1 concentrations in Japanese black cattle with growth retardation. J. Vet. Med. Sci. 63:167-170. https://doi.org/10.1292/jvms.63.167
  104. Knapp, J. R., H. C. Freetly, B. L. Reis, C. C. Calvert and R. L. Baldwin. 1992. Effects of somatotropin and substrates on patterns of liver metabolism in lactating dairy cattle. J. Dairy Sci. 75:1025-1035. https://doi.org/10.3168/jds.S0022-0302(92)77846-1
  105. Kobayashi, Y., C. K. Boyd, C. J. Bracken, W. R. Lamberson, D. H. Keisler and M. C. Lucy. 1999. Reduced growth hormone receptor (GHR) messenger ribonucleic acid in liver of periparturient cattle is caused by a specific down-regulation of GHR 1A that is associated with decreased insulin-like growth factor I. Endocrinol. 140:3947-3954. https://doi.org/10.1210/en.140.9.3947
  106. Kong, S. E., R. C. Baxter and P. J. Delhanty. 2002a. Agedependent regulation of the acid-labile subunit in response to fasting-refeeding in rats. Endocrinol. 143:4505-4512. https://doi.org/10.1210/en.2002-220527
  107. Kong, S. E., S. M. Firth, R. C. Baxter and P. J. Delhanty. 2002b. Regulation of the acid-labile subunit in sustained endotoxemia. Am. J. Physiol. Endocrinol. Metab. 283:E692-701. https://doi.org/10.1152/ajpendo.00148.2002
  108. Kopchick, J. J. and J. M. Andry. 2000. Growth hormone (GH), GH receptor, and signal transduction. Mol. Genet. Metab. 71:293-314. https://doi.org/10.1006/mgme.2000.3068
  109. Kopchick, J. J., L. L. Bellush and K. T. Coschigano. 1999. Transgenic models of growth hormone action. Annu. Rev. Nutr. 19:437-461. https://doi.org/10.1146/annurev.nutr.19.1.437
  110. Kostyo, J. L. 1968. Rapid effects of growth hormone on amino acid transport and protein synthesis. Ann. NY Acad. Sci. 148:389-407. https://doi.org/10.1111/j.1749-6632.1968.tb20365.x
  111. Krebs, D. L. and D. J. Hilton. 2000. SOCS: physiological suppressors of cytokine signaling. J. Cell Sci. 113:2813-2819.
  112. Krebs, D. L. and D. J. Hilton. 2001. SOCS proteins: negative regulators of cytokine signaling. Stem Cells 19:378-387. https://doi.org/10.1634/stemcells.19-5-378
  113. Labarta, J. I., S. E. Gargosky, D. M. Simpson, P. D. Lee, J. Argente, J. Guevara-Aguirre and R. G. Rosenfeld. 1997. Immunoblot studies of the acid-labile subunit (ALS) in biological fluids, normal human serum and in children with GH deficiency and GH receptor deficiency before and after long-term therapy with GH or IGF-I respectively. Clin. Endocrinol. (Oxf) 47:657-666. https://doi.org/10.1046/j.1365-2265.1997.2581078.x
  114. Lang, C. H., J. Fan, R. A. Frost, M. C. Gelato, Y. Sakurai, D. N. Herndon and R. R. Wolfe. 1996. Regulation of the insulin-like growth factor system by insulin in burn patients. J. Clin. Endocrinol. Metab. 81:2474-2480. https://doi.org/10.1210/jc.81.7.2474
  115. Lanna, D. P., K. L. Houseknecht, D. M. Harris and D. E. Bauman. 1995. Effect of somatotropin treatment on lipogenesis, lipolysis, and related cellular mechanisms in adipose tissue of lactating cows. J. Dairy Sci. 78:1703-1712. https://doi.org/10.3168/jds.S0022-0302(95)76795-9
  116. Laron, Z. 1993. An update on Laron syndrome. Arch. Dis. Child. 68:345-346. https://doi.org/10.1136/adc.68.3.345
  117. Le Marchand-Brustel, Y., J. F. Tanti, M. Cormont, J. M. Ricort, T. Gremeaux and S. Grillo. 1999. From insulin receptor signalling to Glut 4 translocation abnormalities in obesity and insulin resistance. J. Recept. Signal Transduct. Res. 19:217-228. https://doi.org/10.3109/10799899909036647
  118. Le Roith, D., C. Bondy, S. Yakar, J. L. Liu and A. Butler. 2001. The somatomedin hypothesis: 2001. Endocr. Rev. 22:53-74. https://doi.org/10.1210/er.22.1.53
  119. Lee, C. Y., I. Kwak, C. S. Chung, W. S. Choi, R. C. Simmen and F. A. Simmen. 2001 Molecular cloning of the porcine acid-labile subunit (ALS) of the insulin-like growth factor-binding protein complex and detection of ALS gene expression in hepatic and non-hepatic tissues. J. Mol. Endocrinol. 26:135-144. https://doi.org/10.1677/jme.0.0260135
  120. Lee, C. Y. and M. M. Rechler. 1995. Formation of 150-kDa binary complexes of insulin-like growth factor binding protein-3 and the acid-labile subunit in vitro and in vivo. Prog. Growth Factor Res. 6:241-251. https://doi.org/10.1016/0955-2235(95)00014-3
  121. Leevers, S. J., B. Vanhaesebroeck and M. D. Waterfield. 1999. Signalling through phosphoinositide 3-kinases: the lipids take centre stage. Curr. Opin. Cell Biol. 11:219-225. https://doi.org/10.1016/S0955-0674(99)80029-5
  122. Leong, S. R., R. C. Baxter, T. Camerato, J. Dai and W. I. Wood. 1992. Structure and functional expression of the acid-labile subunit of the insulin-like growth factor-binding protein complex. Mol. Endocrinol. 6:870-876. https://doi.org/10.1210/me.6.6.870
  123. LeRoith, D. 1996. Insulin-like growth factor receptors and binding proteins. Baillieres. Clin. Endocrinol. Metab. 10:49-73. https://doi.org/10.1016/S0950-351X(96)80298-9
  124. Leung, D. W., S. A. Spencer, G. Cachianes, R. G. Hammonds, C. Collins, W. J. Henzel, R. Barnard, M. J. Waters and W. I. Wood. 1987. Growth hormone receptor and serum binding protein: purification, cloning and expression. Nature 330:537-543. https://doi.org/10.1038/330537a0
  125. Lewis, T. S., P. S. Shapiro and N. G. Ahn. 1998. Signal transduction through MAP kinase cascades. Adv. Cancer. Res. 74:49-139. https://doi.org/10.1016/S0065-230X(08)60765-4
  126. Lewitt, M. S., F. P. Scott, N. M. Clarke and R. C. Baxter. 1995. Developmental regulation of circulating insulin-like growth factor-binding proteins in normal pregnancies and in preeclampsia. Prog. Growth Factor Res. 6:475-480. https://doi.org/10.1016/0955-2235(95)00030-5
  127. Liu, C. Y., A. L. Grant, K. H. Kim and S. E. Mills. 1994. Porcine somatotropin decreases acetyl-CoA carboxylase gene expression in porcine adipose tissue. Domest. Anim. Endocrinol. 11:125-132. https://doi.org/10.1016/0739-7240(94)90040-X
  128. Liu, J., C. K. Boyd, Y. Kobayashi, C. C. Chase Jr., A. C. Hammond, T. A. Olson, T. H. Elsasser and M. C. Lucy. 1999. A novel phenotype for Lardon dwarfism in miniature Bos indicus cattle suggests that the expression of growth hormone receptor 1A in liver is required for normal growth. Domest. Anim. Endocrinol. 17:421-437. https://doi.org/10.1016/S0739-7240(99)00051-X
  129. Liu, J. L. and D. LeRoith. 1999. Insulin-like growth factor I is essential for postnatal growth in response to growth hormone. Endocrinology 140:5178-5184. https://doi.org/10.1210/en.140.11.5178
  130. Liu, J. P., J. Baker, A. S. Perkins, E. J. Robertson and A. Efstratiadis. 1993. Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r). Cell 75:59-72.
  131. Liu, X., G. W. Robinson, K. U. Wagner, L. Garrett, A. Wynshaw-Boris and L. Hennighausen. 1997. Stat5a is mandatory for adult mammary gland development and lactogenesis. Genes Dev. 11:179-186. https://doi.org/10.1101/gad.11.2.179
  132. Lucy, M. C., H. Jiang and Y. Kobayashi. 2001. Changes in the somatotrophic axis associated with the initiation of lactation. J. Dairy Sci. 84(E. Suppl.):E113-E119 (The paper is available at http://www.adsa.org/jds/abs/2001/ jds_es113.htm). https://doi.org/10.3168/jds.S0022-0302(01)70205-6
  133. Lupu, F., J. D. Terwilliger, K. Lee, G. V. Segre and A. Efstratiadis. 2001. Roles of growth hormone and insulin-like growth factor 1 in mouse postnatal growth. Dev. Biol. 229:141-162. https://doi.org/10.1006/dbio.2000.9975
  134. Machlin, L. J. 1972. Effect of porcine growth hormone on growth and carcass composition of the pig. J. Anim. Sci. 35:794-800. https://doi.org/10.2527/jas1972.354794x
  135. Magri, K. A., M. Adamo, D. Leroith and T. D. Etherton. 1990. The inhibition of insulin action and glucose metabolism by porcine growth hormone in porcine adipocytes is not the result of any decrease in insulin binding or insulin receptor kinase activity. Biochem. J. 266:107-113. https://doi.org/10.1042/bj2660107
  136. Mathews, L. S., B. Enberg and G. Norstedt. 1989. Regulation of rat growth hormone receptor gene expression. J. Biol. Chem. 264:9905-9910.
  137. McCutcheon, S. N. and D. E. Bauman. 1986. Effect of chronic growth hormone treatment on responses to epinephrine and thyrotropin-releasing hormone in lactating cows. J. Dairy Sci. 69:44-51. https://doi.org/10.3168/jds.S0022-0302(86)80368-X
  138. Menon, R. K., D. A. Stephan, M. Singh, S. M. Morris Jr. and L. Zou. 1995. Cloning of the promoter-regulatory region of the murine growth hormone receptor gene. Identification of a developmentally regulated enhancer element. J. Biol. Chem. 270:8851-8859. https://doi.org/10.1074/jbc.270.15.8851
  139. Metcalf, D., Greenhalgh, C. J., Viney, E., Willson, T. A., Starr, R., Nicola, N. A., Hilton, D. J. and Alexander, W. S. (2000) Gigantism in mice lacking suppressor of cytokine signalling-2. Nature 405:1069-73. https://doi.org/10.1038/35016611
  140. Mildner, A. M. and Clarke, S. D. 1991. Porcine fatty acid synthase: cloning of a complementary DNA, tissue distribution of its mRNA and suppression of expression by somatotropin and dietary protein. J. Nutr. 121:900-907. https://doi.org/10.1093/jn/121.6.900
  141. Mohan, S., C. Libanati, C. Dony, K. Lang, N. Srinivasan and D. J. Baylink. 1995. Development, validation, and application of a radioimmunoassay for insulin-like growth factor binding protein-5 in human serum and other biological fluids. J Clin. Endocrinol. Metab. 80:2638-2645. https://doi.org/10.1210/jc.80.9.2638
  142. Moller, S., A. Juul, U. Becker and J. H. Henriksen. 2000. The acidlabile subunit of the ternary insulin-like growth factor complex in cirrhosis: relation to liver dysfunction. J. Hepatol. 32:441-446. https://doi.org/10.1016/S0168-8278(00)80395-5
  143. Moutoussamy, S., F. Renaudie, F. Lago, P. A. Kelly and J. Finidori. 1998. Grb10 identified as a potential regulator of growth hormone (GH) signaling by cloning of GH receptor target proteins. J. Biol. Chem. 273:15906-15912. https://doi.org/10.1074/jbc.273.26.15906
  144. Musashi, M., S. Ota and N. Shiroshita. 2000. The role of protein kinase C isoforms in cell proliferation and apoptosis. Int. J. Hematol. 72:12-19.
  145. Okada, S. and J. J. Kopchick. 2001. Biological effects of growth hormone and its antagonist. Trends Mol. Med. 7:126-132. https://doi.org/10.1016/S1471-4914(01)01933-5
  146. O'Mahoney, J. V., M. R. Brandon and T. E. Adams. 1994. Identification of a liver-specific promoter for the ovine growth hormone receptor. Mol. Cell Endocrinol. 101:129-139. https://doi.org/10.1016/0303-7207(94)90227-5
  147. Ooi, G. T., F. J. Cohen, L. Y. Tseng, M. M. Rechler and Y. R. Boisclair. 1997. Growth hormone stimulates transcription of the gene encoding the acid- labile subunit (ALS) of the circulating insulin-like growth factor- binding protein complex and ALS promoter activity in rat liver. Mol. Endocrinol. 11:997-1007. https://doi.org/10.1210/me.11.7.997
  148. Ooi, G. T., K. R. Hurst, M. N. Poy, M. M. Rechler and Y. R. Boisclair. 1998. Binding of STAT5a and STAT5b to a single element resembling a gamma- interferon- activated sequence mediates the growth hormone induction of the mouse acidlabile subunit promoter in liver cells. Mol. Endocrinol. 12:675-687. https://doi.org/10.1210/me.12.5.675
  149. Oster, M. H., P. J. Fielder, N. Levin and M. J. Cronin. 1995. Adaptation of the growth hormone and insulin-like growth factor-I axis to chronic and severe calorie or protein malnutrition. J. Clin. Invest. 95:2258-2265.
  150. Park, S. H., X. Liu, L. Hennighausen, H. W. Davey and D. J. Waxman. 1999. Distinctive roles of STAT5a and STAT5b in sexual dimorphism of hepatic P450 gene expression. Impact of STAT5a gene disruption. J. Biol. Chem. 274:7421-7430. https://doi.org/10.1074/jbc.274.11.7421
  151. Peters, J. P. 1986. Consequences of accelerated gain and growth hormone administration for lipid metabolism in growing beef steers. J. Nutr. 116:2490-2503. https://doi.org/10.1093/jn/116.12.2490
  152. Pocius, P. A. and J. H. Herbein. 1986. Effects of in vivo administration of growth hormone on milk production and in vitro hepatic metabolism in dairy cattle. J. Dairy Sci. 69:713-720. https://doi.org/10.3168/jds.S0022-0302(86)80460-X
  153. Powell-Braxton, L., P. Hollingshead, C. Warburton, M. Dowd, S. Pitts-Meek, D. Dalton, N. Gillett and T. A. Stewart. 1993. IGFI is required for normal embryonic growth in mice. Genes Dev. 7:2609-2617. https://doi.org/10.1101/gad.7.12b.2609
  154. Prosser, C. G., S. R. Davis, S. C. Hodgkinson and M. A. Mohler. 1995. Pharmacokinetics and bioactivity of intact versus truncated IGF-I during a 24-h infusion into lactating goats. J. Endocrinol. 144:99-107. https://doi.org/10.1677/joe.0.1440099
  155. Prosser, C. G., I. R. Fleet, A. N. Corps, E. R. Froesch and R. B. Heap. 1990. Increase in milk secretion and mammary blood flow by intra-arterial infusion of insulin-like growth factor-Iinto the mammary gland of the goat. J. Endocrinol. 126:437-443. https://doi.org/10.1677/joe.0.1260437
  156. Ram, P. A. and D. J. Waxman. 1999. SOCS/CIS protein inhibition of growth hormone-stimulated STAT5 signaling by multiple mechanisms. J. Biol. Chem. 274:35553-35561. https://doi.org/10.1074/jbc.274.50.35553
  157. Renaville, R., M. Hammadi and D. Portetelle. 2002. Role of the somatotropic axis in the mammalian metabolism. Domest. Anim. Endocrinol. 23:351-360. https://doi.org/10.1016/S0739-7240(02)00170-4
  158. Rhoads, R. P., P. L. Greenwood, A. W. Bell and Y. R. Boisclair. 2000. Organization and regulation of the gene encoding the sheep acid-labile subunit of the 150-kilodalton insulin-like growth factor-binding protein complex. Endocrinol. 141:1425-1433. https://doi.org/10.1210/en.141.4.1425
  159. Rhoads, R. P., J. W. Kim, B. J. Leury, L. H. Baumgard, N. Segoale, S. J. Frank, D. E. Bauman and Y. R. Boisclair. 2004. Insulin increases the abundance of the growth hormone receptor in liver and adipose tissue of periparturient dairy cows. J. Nutr. 134:1020-1027. https://doi.org/10.1093/jn/134.5.1020
  160. Rhoads, R. P., J. W. Kim, M. E. Van Amburgh, R. A. Ehrhardt, S. J. Frank and Y. R. Boisclair. 2007. Effect of nutrition on the GH responsiveness of liver and adipose tissue in dairy cows. J. Endocrinol. 195:49-58. https://doi.org/10.1677/JOE-07-0068
  161. Ridderstrale, M., E. Degerman and H. Tornqvist. 1995. Growth hormone stimulates the tyrosine phosphorylation of the insulin receptor substrate-1 and its association with phosphatidylinositol 3-kinase in primary adipocytes. J. Biol. Chem. 270:3471-3474. https://doi.org/10.1074/jbc.270.8.3471
  162. Rivera, V. M., C. K. Miranti, R. P. Misra, D. D. Ginty, R. H. Chen, J. Blenis and M. E. Greenberg. 1993. A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. Mol. Cell. Biol. 13:6260-6273. https://doi.org/10.1128/MCB.13.10.6260
  163. Ron, D. and M. G. Kazanietz. 1999. New insights into the regulation of protein kinase C and novel phorbol ester receptors. FASEB J. 13:1658-1676. https://doi.org/10.1096/fasebj.13.13.1658
  164. Ropke, R., H. Sauerwein, B. Stoffel, K. Hagen-Mann, S. von Ahnen and H. H. D. Meyer. 1994. Extended aspects of growth hormone (GH) action: GH receptor mRNA expression in various bovine tissues and effects of a long term treatment with GH on GHR mRNA and on GH binding in liver. J. Repro. Develop. 40:227-234. https://doi.org/10.1262/jrd.40.227
  165. Saharinen, P., K. Takaluoma and O. Silvennoinen. 2000. Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol. Cell. Biol. 20:3387-3395. https://doi.org/10.1128/MCB.20.10.3387-3395.2000
  166. Scharf, J. G., G. Ramadori, T. Braulke and H. Hartmann. 1995. Cellular localization and hormonal regulation of biosynthesis of insulin-like growth factor binding proteins and of the acidlabile subunit within rat liver. Prog. Growth Factor Res. 6:175-180. https://doi.org/10.1016/0955-2235(95)00031-3
  167. Schwartzbauer, G. and R. K. Menon. 1998. Regulation of growth hormone receptor gene expression. Mol. Genet. Metab. 63:243-253. https://doi.org/10.1006/mgme.1998.2685
  168. Sechen, S. J., F. R. Dunshea and D. E. Bauman. 1990. Somatotropin in lactating cows: effect on response to epinephrine and insulin. Am. J. Physiol. 258:E582-588.
  169. Seve, B., O. Ballevre, P. Ganier, J. Noblet, J. Prugnaud and C. Obled. 1993. Recombinant porcine somatotropin and dietary protein enhance protein synthesis in growing pigs. J. Nutr. 123:529-540. https://doi.org/10.1093/jn/123.3.529
  170. Shuai, K. 1999. The STAT family of proteins in cytokine signaling. Prog. Biophys. Mol. Biol. 71:405-422. https://doi.org/10.1016/S0079-6107(98)00051-0
  171. Sinowatz, F., D. Schams, S. Kolle, A. Plath, D. Lincoln and M. J. Waters. 2000. Cellular localisation of GH receptor in the bovine mammary gland during mammogenesis, lactation and involution. J. Endocrinol. 166:503-150. https://doi.org/10.1677/joe.0.1660503
  172. Slootweg, M. C., M. P. de Groot, M. P. Herrmann-Erlee, I. Koornneef, W. Kruijer and Y. M. Kramer. 1991. Growth hormone induces expression of c-jun and jun B oncogenes and employs a protein kinase C signal transduction pathway for the induction of c-fos oncogene expression. J. Mol. Endocrinol. 6:179-188. https://doi.org/10.1677/jme.0.0060179
  173. Smit, L. S., D. J. Meyer, N. Billestrup, G. Norstedt, J. Schwartz and C. Carter-Su. 1996. The role of the growth hormone (GH) receptor and JAK1 and JAK2 kinases in the activation of Stats 1, 3, and 5 by GH. Mol. Endocrinol. 10:519-533. https://doi.org/10.1210/me.10.5.519
  174. Smith, W. C., J. Kuniyoshi and F. Talamantes. 1989. Mouse serum growth hormone (GH) binding protein has GH receptor extracellular and substituted transmembrane domains. Mol. Endocrinol. 3:984-990. https://doi.org/10.1210/mend-3-6-984
  175. Sodhi, R. and Y. S. Rajput. 2007. Interaction of bovine growth hormone with buffalo adipose tissue and identification of signaling molecules in its action. Asian-Aust. J. Anim. Sci. 20(7):1030-1038. https://doi.org/10.5713/ajas.2007.1030
  176. Stofega, M. R., J. Herrington, N. Billestrup and C. Carter-Su. 2000. Mutation of the SHP-2 binding site in growth hormone (GH) receptor prolongs GH-promoted tyrosyl phosphorylation of GH receptor, JAK2, and STAT5B. Mol. Endocrinol. 14:1338-1350. https://doi.org/10.1210/me.14.9.1338
  177. Suwanichkul, A., Y. R. Boisclair, R. C. Olney, S. K. Durham and D. R. Powell. 2000. Conservation of a growth hormoneresponsive promoter element in the human and mouse acidlabile subunit genes. Endocrinol. 141:833-838. https://doi.org/10.1210/en.141.2.833
  178. Takahashi, Y., H. Kaji, Y. Okimura, K. Goji, H. Abe and K. Chihara. 1996. Brief report: short stature caused by a mutant growth hormone. N. Engl. J. Med. 334:432-436. https://doi.org/10.1056/NEJM199602153340704
  179. Teglund, S., C. McKay, E. Schuetz, J. M. van Deursen, D. Stravopodis, D. Wang, M. Brown, S. Bodner, G. Grosveld and J. N. Ihle. 1998. Stat5a and Stat5b proteins have essential and nonessential, or redundant, roles in cytokine responses. Cell 93:841-850. https://doi.org/10.1016/S0092-8674(00)81444-0
  180. Thirone, A. C., C. R. Carvalho and M. J. Saad. 1999. Growth hormone stimulates the tyrosine kinase activity of JAK2 and induces tyrosine phosphorylation of insulin receptor substrates and Shc in rat tissues. Endocrinol. 140:55-62. https://doi.org/10.1210/en.140.1.55
  181. Tollet, P., C. Legraverend, J. A. Gustafsson and A. Mode. 1991. A role for protein kinases in the growth hormone regulation of cytochrome P4502C12 and insulin-like growth factor-I messenger RNA expression in primary adult rat hepatocytes. Mol. Endocrinol. 5:1351-1358. https://doi.org/10.1210/mend-5-9-1351
  182. Tollet-Egnell, P., A. Flores-Morales, A. Stavreus-Evers, L. Sahlin and G. Norstedt. 1999. Growth hormone regulation of SOCS-2, SOCS-3, and CIS messenger ribonucleic acid expression in the rat. Endocrinol. 140:3693-3704. https://doi.org/10.1210/en.140.8.3693
  183. Twigg, S. M. and R. C. Baxter. 1998. Insulin-like growth factor (IGF)-binding protein 5 forms an alternative ternary complex with IGFs and the acid-labile subunit. J. Biol. Chem. 273:6074-6079. https://doi.org/10.1074/jbc.273.11.6074
  184. Twigg, S. M., M. C. Kiefer, J. Zapf and R. C. Baxter. 1998. Insulin-like growth factor-binding protein 5 complexes with the acid- labile subunit. Role of the carboxyl-terminal domain. J. Biol. Chem. 273:28791-28798. https://doi.org/10.1074/jbc.273.44.28791
  185. Uchijima, Y., A. Takenaka, S. Takahashi and T. Noguchi. 1995. Production of insulin-like growth factors and their binding proteins in primary cultures of rat liver parenchymal and nonparenchymal cells. Biosci. Biotechnol. Biochem. 59:1503-1515. https://doi.org/10.1271/bbb.59.1503
  186. Udy, G. B., R. P. Towers, R. G. Snell, R. J. Wilkins, S. H. Park, P. A. Ram, D. J. Waxman and H. W. Davey. 1997. Requirement of STAT5b for sexual dimorphism of body growth rates and liver gene expression. Proc. Natl. Acad. Sci. USA 94:7239-7244. https://doi.org/10.1073/pnas.94.14.7239
  187. Ueki, I., G. T. Ooi, M. L. Tremblay, K. R. Hurst, L. A. Bach and Y. R. Boisclair. 2000. Inactivation of the acid labile subunit gene in mice results in mild retardation of postnatal growth despite profound disruptions in the circulating insulin-like growth factor system. Proc. Natl. Acad. Sci. USA 97:6868-6873. https://doi.org/10.1073/pnas.120172697
  188. VanderKuur, J., G. Allevato, N. Billestrup, G. Norstedt and C. Carter-Su. 1995. Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2. J. Biol. Chem. 270:7587-7593. https://doi.org/10.1074/jbc.270.13.7587
  189. Vanderkuur, J. A., E. R. Butch, S. B. Waters, J. E. Pessin, K. L. Guan and C. Carter-Su. 1997. Signaling molecules involved in coupling growth hormone receptor to mitogen-activated protein kinase activation. Endocrinol. 138:4301-4307. https://doi.org/10.1210/en.138.10.4301
  190. Verdier, F., S. Chretien, O. Muller, P. Varlet, A. Yoshimura, S. Gisselbrecht, C. Lacombe and P. Mayeux. 1998. Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein. J. Biol. Chem. 273:28185-28190. https://doi.org/10.1074/jbc.273.43.28185
  191. Vernon, R. G., M. C. Barber and E. Finley. 1991. Modulation of the activity of acetyl-CoA carboxylase and other lipogenic enzymes by growth hormone, insulin and dexamethasone in sheep adipose tissue and relationship to adaptations to lactation. Biochem. J. 274 (Pt 2):543-548. https://doi.org/10.1042/bj2740543
  192. Walton, P. E. and T. D. Etherton. 1986. Stimulation of lipogenesis by insulin in swine adipose tissue: antagonism by porcine growth hormone. J. Anim. Sci. 62:1584-159. https://doi.org/10.2527/jas1986.6261584x
  193. Walton, P. E., T. D. Etherton and C. S. Chung. 1987. Exogenous pituitary and recombinant growth hormones induce insulin and insulin-like growth factor 1 resistance in pig adipose tissue. Domest. Anim. Endocrinol. 4:183-189. https://doi.org/10.1016/0739-7240(87)90014-2
  194. Walton, P. E., T. D. Etherton and C. M. Evock. 1986. Antagonism of insulin action in cultured pig adipose tissue by pituitary and recombinant porcine growth hormone: potentiation by hydrocortisone. Endocrinol. 118:2577-2581. https://doi.org/10.1210/endo-118-6-2577
  195. Wandji, S. A., J. E. Gadsby, F. A. Simmen, J. A. Barber and J. M. Hammond. 2000. Porcine ovarian cells express messenger ribonucleic acids for the acid- labile subunit and insulin-like growth factor binding protein-3 during follicular and luteal phases of the estrous cycle. Endocrinol. 141:2638-2647. https://doi.org/10.1210/en.141.7.2638
  196. Weber, M. S., S. Purup, M. Vestergaard, R. M. Akers and K. Sejrsen. 2000. Regulation of local synthesis of insulin-like growth factor-I and binding proteins in mammary tissue. J. Dairy Sci. 83:30-37. https://doi.org/10.3168/jds.S0022-0302(00)74851-X
  197. Woelfle, J., D. J. Chia and P. Rotwein. 2003. Mechanisms of growth hormone action: identification of conserved Stat5 binding sites that mediate GH-induced insulin-like growth factor-I gene activation. J. Biol. Chem. 278(51):51261-51266. https://doi.org/10.1074/jbc.M309486200
  198. Woelfle, J. and P. Rotwein. 2004. In vivo regulation of growth hormone-stimulated gene transcription by STAT5b. Am. J. Physiol. Endocrinol. Metab. 286:E393-401. https://doi.org/10.1152/ajpendo.00389.2003
  199. Wolf, R. F., M. J. Heslin, E. Newman, D. B. Pearlstone, A. Gonenne and M. F. Brennan. 1992. Growth hormone and insulin combine to improve whole-body and skeletal muscle protein kinetics. Surgery 112:284-291; discussion 291-292.
  200. Xu, S., S. C. Cwyfan-Hughes, J. W. van der Stappen, J. Sansom, J. L. Burton, M. Donnelly and J. M. Holly. 1995. Insulin-like growth factors (IGFs) and IGF-binding proteins in human skin interstitial fluid. J. Clin. Endocrinol. Metab. 80:2940-2945. https://doi.org/10.1210/jc.80.10.2940
  201. Yakar, S., J. L. Liu, A. M. Fernandez, Y. Wu, A. V. Schally, J. Frystyk, S. D. Chernausek, W. Mejia and D. Le Roith. 2001. Liver-specific igf-1 gene deletion leads to muscle insulin insensitivity. Diabetes 50:1110-1118. https://doi.org/10.2337/diabetes.50.5.1110
  202. Yakar, S., J. L. Liu, B. Stannard, A. Butler, D. Accili, B. Sauer and D. Le Roith. 1999. Normal growth and development in the absence of hepatic insulin-like growth factor I. Proc. Natl. Acad. Sci. USA. 96:7324-732. https://doi.org/10.1073/pnas.96.13.7324
  203. Yakar, S., C. J. Rosen, W. G. Beamer, C. L. Ackert-Bicknell, Y. Wu, J. L. Liu, G. T. Ooi, J. Setser, J. Frystyk, Y. R. Boisclair and D. Le Roith. 2002. Circulating levels of IGF-1 directly regulate bone growth and density. J. Clin. Invest. 110:771-781. https://doi.org/10.1172/JCI0215463
  204. Yi, W., S. O. Kim, J. Jiang, S. H. Park, A. S. Kraft, D. J. Waxman and S. J. Frank. 1996. Growth hormone receptor cytoplasmic domain differentially promotes tyrosine phosphorylation of signal transducers and activators of transcription 5b and 3 by activated JAK2 kinase. Mol. Endocrinol. 10:1425-1443. https://doi.org/10.1210/me.10.11.1425
  205. Yokota, I., H. Hayashi, J. Matsuda, T. Saijo, E. Naito, M. Ito, Y. Ebina and Y. Kuroda. 1998. Effect of growth hormone on the translocation of GLUT4 and its relation to insulin-like and anti-insulin action. Biochim. Biophys. Acta. 1404:451-456. https://doi.org/10.1016/S0167-4889(98)00077-9
  206. Zapf, J. 1995. Insulin-like growth factor binding proteins and tumor hypoglycemia. Trends Endocrinol. Metab. 6:37-42. https://doi.org/10.1016/1043-2760(94)00144-S
  207. Zapf, J., C. Hauri, M. Waldvogel and E. R. Froesch. 1986. Acute metabolic effects and half-lives of intravenously administered insulinlike growth factors I and II in normal and hypophysectomized rats. J. Clin. Invest. 77:1768-1775. https://doi.org/10.1172/JCI112500
  208. Zhou, G.. I., Q. Zhu, H. G. Jin and S. I. Guo. 2006. Genetic variation of growth hormone gene and its relationship with milk production traits in china Holstein cows. Asian-Aust. J. Anim. Sci. 19(3):315-318.. https://doi.org/10.5713/ajas.2006.315
  209. Zhu, T., E. L. Goh, R. Graichen, L. Ling and P. E. Lobie. 2001. Signal transduction via the growth hormone receptor. Cell Signal. 13:599-616. https://doi.org/10.1016/S0898-6568(01)00186-3
  210. Zhu, T., E. L. Goh and P. E. Lobie. 1998. Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. Fak is not required for stat-mediated transcription. J. Biol. Chem. 273:10682-10689. https://doi.org/10.1074/jbc.273.17.10682
  211. Zou, L., L. A. Burmeister and M. A. Sperling. 1997 Isolation of a liver-specific promoter for human growth hormone receptor gene. Endocrinol. 138:1771-1774. https://doi.org/10.1210/en.138.4.1771

피인용 문헌

  1. The Endocrine Regulation of Chicken Growth vol.23, pp.12, 2010, https://doi.org/10.5713/ajas.2010.10329