• Clinical and Experimental Pediatrics
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• v.49 no.7
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• pp.703-709
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• 2006

Since the advent of growth hormone(GH), children with a wide variety of growth disorders have received GH treatment. In GH deficiency(GHD), Turner syndrome, chronic renal failure, children born small for gestational age, Prader-Willi syndrome, and idiopathic short stature, the therapeutic effects and safety profile of GH are reviewed. GH therapy has been clearly shown to improve height velocity and final adult height in a variety of pediatric conditions in which growth is compromised irrespective of GHD. Early initiation and individualization of GH treatment has the potential to normalize childhood growth. The supra-physiological doses of GH have been shown to increase height velocity during childhood and final height in non-GHD conditions. Adverse events during GH therapy are uncommon and often not drug related. However continued surveillance into adult life is crucial, especially in children receiving supra-physiological doses or whose underlying condition increases their risk of adverse effects.

• Development and Reproduction
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• v.6 no.1
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• pp.31-35
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• 2002

The major urinary proteins(MUPs) of mice that bind hydrophobic molecules known as pheromones are regulated in part by the actions of growth hormone. The expression of the MUPs was therefore investigated in transgenic mice that express a human growth hormone-releasing factor gene from a metallothionein gene promoter(MT-GRF) and as a result have elevated growth hormone levels. MUPs were severely down-regulated in the urine of these animals compared to normal mice or to control transgenic mice expressing another gene(the inhibin a subunit) from the same metallothionein promoter(MT-Inh) and more MUPs disappeared in male mice than female ones. MUPs were also down-regulated in the urine of the UT-GRF-injected mice. In addition, it was observed that the urine of the MT-GRF mice included a high molecular weight protein that co-migrates with the major serum protein albumin, indicating an impairment in glomerular filtration within the kidney. The urinary loss of serum proteins was more severe in male MT-GRF mice than female ones. Thus the overexpression of human GRF mimics changes observed in MUP protein expression and glomerular function in other models of growth hormone hypersecretion with sex-dependent differential effects.

• Asian-Australasian Journal of Animal Sciences
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• v.2 no.3
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• pp.254-256
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• 1989

• Journal of the Korean Chemical Society
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• v.52 no.6
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• pp.608-613
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• 2008

• Journal of mucopolysaccharidosis and rare diseases
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• v.1 no.1
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• pp.23-27
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• 2015

Recent research trends of human growth hormone (hGH) are divided into improved first-generation products, long-acting second-generation products, and biosimilar products. Among the improved first-generation products studies, studies of injection devices are being actively conducted. The long-acting second-generation products are focused on extending the half-life of hGH, and depending on the results of the clinical trials, the candidates are expected to lead the future hGH market. Finally, biosimilar has had less impact on the hGH market before now; however, expectations of low-cost products still remainas an opportunity.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.5
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• pp.757-766
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• 2002

Growth hormone-releasing peptide-2 (GHRP-2, also named KP102) is a new hexapeptide of a series of synthetic growth hormone-releasing peptides (GHRPs) which stimulates the secretion of growth hormone (GH) in vitro and in vivo in several species including calf, sheep and pig. The GH-releasing activity of GHRP-2 is two to three times more effective than that of the original GHRP-6, and GHRP-1 in the rats and humans. To date, GHRP-2 seems to be the most potent member of the family of GHRPs. Since the GHRPs are short peptides (5-7 amino acid residues), they are synthesized easily and are not as readily degraded in plasma as GHreleasing hormone (GHRH). These features ameliorate their potential on domestic animals because of their chemical nature the GHRPs are efficacious when administered i.v. orally or orally. However, studies in cow, pig and sheep do not indicate such a close relationship between GHRH, somatostatin (SS) and GH, calling into question the general applicability of the human and rat models. Perhaps there is an important role for an endogenous GHRP in the regulation of GH secretion in domestic animals. This review provides an overview on the current knowledge of physiological role of GHRP-2 in domestic animals.

• Clinical and Experimental Pediatrics
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• v.53 no.9
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• pp.845-851
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• 2010

Purpose: Recombinant human growth hormone (rhGH) has been widely used to treat short stature. However, there are some concerns that growth hormone treatment may induce skeletal maturation and early onset of puberty. In this study, we investigated whether rhGH can directly affect the neuronal activities of of gonadotropin-releasing hormone (GnRH). Methods: We performed brain slice gramicidin-perforated current clamp recording to examine the direct membrane effects of rhGH on GnRH neurons, and a whole-cell voltage-clamp recording to examine the effects of rhGH on spontaneous postsynaptic events and holding currents in immature (postnatal days 13-21) and adult (postnatal days 42-73) mice. Results: In immature mice, all 5 GnRH neurons recorded in gramicidin-perforated current clamp mode showed no membrane potential changes on application of rhGH (0.4, $1{\mu}g/mL$). In adult GnRH neurons, 7 (78%) of 9 neurons tested showed no response to rhGH ($0.2-1{\mu}g/mL$) and 2 neurons showed slight depolarization. In 9 (90%) of 10 immature neurons tested, rhGH did not induce any membrane holding current changes or spontaneous postsynaptic currents (sPSCs). There was no change in sPSCs and holding current in 4 of 5 adult GnRH neurons. Conclusion: These findings demonstrate that rhGH does not directly affect the GnRH neuronal activities in our experimental model.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.554-556
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• 2003

This research was focused on expression, purification and characterization of ubiquitin-specific protease 1 (UBP1) expressed in recombinant Escherichia coli. Various systems were constructed by fusing polycationic fusion tails or fusion partners to the C- or N-terminus of the product protein. In particular, UBP1 containing 6 histidine residues at the N-terminal end showed best results in terms of expression level and purification efficiency. The N-terminal $6{\times}His-tagged$ UBP1 was overproduced in recombinant E. coli using high cell density cultivation technology and purified using immobilized metal affinity chromatography. The molecular weight of UBP1 was found to be 83,500 daltons. The optimum temperature and pH for the enzyme reaction when ubiquitin-human growth hormone (hGH) was used as a substrate were $40^{\circ}C$ and pH 8.0, respectively.

• Biotechnology and Bioprocess Engineering:BBE
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• v.6 no.4
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• pp.306-308
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• 2001

A recombinant human growth hormone(hGH) was expressed as a secretory product in the yeast Saccharomyuces cerevisiae. There different leader sequences derived from the mating fac-tor $\alpha$1(MF$\alpha$1) inulinase and invertase were used to direct the secretion of hGH into the extracel-lular medium. Among three leader sequences tested, the inulinase leader sequence was found to be the most efficient in the secretory expression of hGH. In contrast, no hGH was detected in the ex-tracellular medium with the invertase leader sequence. After 48 h shake-flask culture, the yields of hGH secreted into th emedium by the invertase. MF$\alpha$1 inulinase and invertase leader sequences were approximately 0, 0.3 and 0.9 mg/L, respectively. The secretion efficiencies were also found to be 0, 3.8 and 13% for the invertase , MG$\alpha$1 and inulinase leader sequences, respectively.

• YAKHAK HOEJI
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• v.34 no.6
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• pp.439-446
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• 1990

The general pharmacological actions of recombinant human growth hormone (rHGH) were investigated. It had hypothermic action but neither sedative nor analgesic action. No pharmacological effects were observed in isolated guinea pig ileum and tracheal muscle and rat fundus and uterus. Slight hypotensive action with no effect on respiration was revealed at a dose of 20 IU/kg i.v. of rHGH in rabbits. The rHGH exhibited a weak inhibitory action of glucose tolerance in normal rats, significantly lowered the blood glucose contents in adrenalectomized rats 20 min after i.v. administration (80IU/kg), and produced a significant inhibitory effect on in vitro glycerol release in epinephrine-stimulated epididymal fat pad segments of rats.