참고문헌
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- Cobb, M. H. 1999. MAP kinase pathways. Prog. Biophys. Mol. Biol. 71:479-500. https://doi.org/10.1016/S0079-6107(98)00056-X
- 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
- Cramer, S. D. and F. Talamantes. 1993. The growth hormone receptor and growth hormone-binding protein:structure, functions, and regulation. New York.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Finidori, J. 2000. Regulators of growth hormone signaling. Vitam. Horm. 59:71-97. https://doi.org/10.1016/S0083-6729(00)59004-9
- 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
- Fowden, A. L. 1995. Endocrine regulation of fetal growth. Reprod. Fertil. Dev. 7:351-363. https://doi.org/10.1071/RD9950351
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Krebs, D. L. and D. J. Hilton. 2000. SOCS: physiological suppressors of cytokine signaling. J. Cell Sci. 113:2813-2819.
- 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
- 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
- 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
- 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
- Laron, Z. 1993. An update on Laron syndrome. Arch. Dis. Child. 68:345-346. https://doi.org/10.1136/adc.68.3.345
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- Mathews, L. S., B. Enberg and G. Norstedt. 1989. Regulation of rat growth hormone receptor gene expression. J. Biol. Chem. 264:9905-9910.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- The Endocrine Regulation of Chicken Growth vol.23, pp.12, 2010, https://doi.org/10.5713/ajas.2010.10329