• 제목/요약/키워드: Recombinant human growth hormone

검색결과 48건 처리시간 0.027초

Neutralizing Effects of Antiserum by Repeated Subcutaneous Administration of Recombinant Human Growth Hormone (rhGH)

  • Song, Yeon-Jung;Park, Shin-Hye;Park, Seung-Kook;Yeon, Je-Deuk
    • Biomolecules & Therapeutics
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    • 제10권3호
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    • pp.175-179
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    • 2002
  • Human growth hormone (hGH) forms antibody by repeated administration. The present study investigated to confirm formation of antibody by repeated subcutaneous administration of hGH for two months in rats and dogs. In this result, hGH-injected sera were significantly higher than control sera by 1:1,000,000 of dilution factor. After antibody formed sera (anti-hGH sera) and control sera were added to 30 $\mu\textrm{g}$/ml hGR, the complex incubated for overnight at $30^{\circ}C$. Anti-hGH sera decreased hGH contents about 90% compared to control sera. Also, body weight gain conducted decreased about 67% compared to control sera in hypophysectomised rat. Inconclusion, repeated administration of hGH formed antibody because hGH was foreign protein to rats and dogs. And formed antibody of hGH was blocked and decreased many efficacy of hGH, the antibody was proved to be neutralizing antibody. Thus, because neutralizing antibodies were decreased pharmacological effects of hGH, administration more than two months were no significance.

Gene Expression Related to Cognitive Function in Growth Hormone-treated Mice with Prader-Willi Syndrome

  • Ko, Ah-Ra
    • Journal of mucopolysaccharidosis and rare diseases
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    • 제2권2호
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    • pp.38-40
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    • 2016
  • Prader-Willi syndrome (PWS) is a rare genetic disorder often caused by a deletion of the chromosome 15q11-q13 region inherited from the father or by maternal disomy 15. Growth hormone deficiency with short stature, hypogonadism, cognitive and behavioral problems, analgesia, decreased gastric motility and decreased ability to vomit with hyperphagia are common in PWS leading to severe obesity in early childhood, if not controlled. The goal of this study is to investigate the effects of recombinant human GH (rhGH, henceforth designated GH) on the gene expression related to cognitive function in the brain of PWS mouse model (Snord116del). GH restored the mRNA expression level of several genes in the cerebellum. These data suggest the effect of GH on the expression of cognitive function related genes in cerebellum may provide a mechanism for the GH-induced brain function in PWS patients.

Effects of human growth hormone on gonadotropin-releasing hormone neurons in mice

  • Bhattarai, Janardhan P.;Kim, Shin-Hye;Han, Seong-Kyu;Park, Mi-Jung
    • Clinical and Experimental Pediatrics
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    • 제53권9호
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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.

The New Strategy of Formulation of Human Growth Hormone Aggregate within PLGA Microspheres for Sustained Release

  • 김홍기;박태관
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2000년도 춘계학술발표대회
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    • pp.541-545
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    • 2000
  • For the sustained release formulation of recombinant human growth hormone (rhGH), dissociable rhGH aggregates were microencapsulated within poly(D,L-lactic-co-glycolic acid) [PLGA] microparticles. rhGH aggregates with 2 - 3 m Particle diameter were first produced by adding a small volume of aqueous rhGH solution into a partially water miscible organic solvent phase(ethyl acetate) containing PLGA. These rhGH aggregates were then microencapsulated within PLGA polymer phase by extracting ethyl acetate into an aqueous phase pre-saturated with ethyl acetate. The resultant microparticles were 2 - 3 m in diameter similar to the size of rhGH aggregates, suggesting that PLGA polymer was coated around the protein aggregates. Release profiles of rhGH from these microparticles were greatly affected by changing the volume of the incubation medium. The release rhGH species consisted of mostly monomeric form with having a correct conformation. This study reveals that sustained rhGH release could be achieved by microencapsulating reversibly dissociable protein aggregates within biodegradable polymers.

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Anti-CHH Antibody Causes Impaired Hyperglycemia in Penaeus monodon

  • Treerattrakool, Supattra;Udomkit, Apinunt;Panyim, Sakol
    • BMB Reports
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    • 제39권4호
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    • pp.371-376
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    • 2006
  • Crustacean hyperglycemic hormone (CHH) plays a major role in controlling glucose level in the haemolymph and also triggers important events during molting and reproductive cycles. In Penaeus monodon, three types of CHH, namely Pem-CHH1, Pem-CHH2 and Pem-CHH3, have been previously characterized. In this study, mouse polyclonal antibody was raised against recombinant Pem-CHH1 that was expressed in Escherichia coli. The anti-Pem-CHH1 antibody recognized all three types of Pem-CHHs but did not cross-react with either related hormone, molt-inhibiting hormone of P. monodon, or unrelated human growth hormone. The hyperglycemic activity in the extract from the eyestalk neural tissues was significantly depleted after incubating with anti-Pem-CHH antibody. Direct injection of the antibody into shrimp caused about 30-50% reduction in the haemolymph glucose level. The result demonstrates the ability of anti-Pem-CHH1 antibody to deplete the activity of CHH in vivo, and thus provides a possibility of using anti-Pem-CHH1 antibody to inhibit the hormone activity as a strategy to modulate growth and reproduction in this species.

Effects of Three Dietary Growth Hormones on Growth Performance and Lysozyme Activity in Juvenile Olive Flounder, Paralichthys olivaceus

  • Lee, Seung-Hyung;Yoo, Gwang-Yeol;Park, Gun-Jun;Kim, Young-Chul;Lee, Jun-Ho;Bai, Sung-Chul C.
    • Fisheries and Aquatic Sciences
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    • 제11권4호
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    • pp.183-189
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    • 2008
  • In this study, tests were conducted to investigate the effects of three dietary growth hormones, administered in various amounts, on the growth performance and lysozyme activity in juvenile olive flounder, Paralichthys olivaceus. Three dietary growth hormones, recombinant human growth hormone (rHGH), recombinant bovine somatotropin A (rBST A) and recombinant bovine somatotropin B (rBST B) were tested at three different supplemental levels (10, 20 or 40 mg/kg body weight per week) by a $3{\times}3$ factorial design and a complete randomized design in comparison to a control group. Fish were fed one of the ten experimental diets (control, $rHGH_{10}$, $rHGH_{20}$, $rHGH_{40}$, rBST $A_{10}$, rBST $A_{20}$, rBST $A_{40}$, rBST $B_{10}$, rBST $B_{20}$ and rBST $B_{40}$) for 6 weeks and afterward were analyzed for growth performance by measuring weight gain (WG), feed efficiency (FE), specific growth rate (SGR) and protein efficiency ratio (PER). Based on the factorial design analysis, fish fed rHGH diets demonstrated significantly higher growth performance than fish fed rBST A or rBST B diets. However there were no significant differences in WG, FE, SGR and PER between fish fed rBST A and rBST B diets. Neither hormone level nor the interaction between the different hormones and their various levels had a significant effect on WG, FE, SGR, PER, lysozyme activity or whole-body proximate composition. A complete randomized design analysis confirmed fish fed $rHGH_{10}$, $rHGH_{20}$, $rHGH_{40}$, rBST $A_{10}$, rBST $A_{20}$, rBST $A_{40}$, rBST $B_{20}$ and rBST $B_{40}$ diets for 6 weeks showed higher WG than fish fed the control diet (P<0.05). A higher FE was observed in fish fed $rHGH_{10}$, $rHGH_{20}$, $rHGH_{40}$, rBST $A_{20}$ and rBST $A_{40}$ diets in comparison to fish fed the control diet. Fish fed all graded rHGH, rBST A and rBST B supplemented diets showed a higher SGR than fish fed the control diet. Regarding PER, fish fed $rHGH_{10}$, $rHGH_{20}$, $rHGH_{40}$, rBST $A_{10}$, rBST $A_{20}$, rBST $A_{40}$ and rBST $B_{20}$ diets were higher than fish fed the control diet. Furthermore, the lysozyme activity of fish fed a diet of $rHGH_{20}$ was significantly higher than that of fish fed any other diet. The results measuring the growth and development of the fish clearly suggest the biopotency of dietary rHGH could be higher than those of both dietary rBST A and rBST B. Further implied is the probability that within the range of 10 to 40 mg/kg BW/week the dietary growth hormones could accelerate growth performance, and that 20 mg rHGH/kg BW/week could possibly enhance lysozyme activity in juvenile olive flounder, Paralichthys olivaceus.

코돈 최적화 및 샤페론 공발현을 통한 활성 형태의 재조합 인간 상피세포성장인자의 발현 (Expression of Recombinant Human Epidermal Growth Factor as a Active Form through Codon Optimization with E. coli and Co-expression of Chaperone)

  • 장은빈;김준수;이우일
    • 한국산학기술학회논문지
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    • 제21권9호
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    • pp.559-568
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    • 2020
  • 세포 분열 및 성장 촉진에 영향을 주는 상피세포 성장인자(Epidermal Growth Factor, EGF)는 다양한 의학적 용도를 갖고 있는 호르몬 단백질이다. 본 연구에서는 human EGF 유전자를 대장균 코돈에 최적화 하고 pRSET 벡터에 클로닝하여 발현벡터를 구축하였다. Human EGF를 봉입체가 아닌 활성이 있는 형태로의 과량 발현을 위해 코돈의 최적화와 더불어 최초로 샤페론 공발현이 시도되었다. 발현된 Native protein 형태의 재조합 human EGF는 고순도로 정제하기 위해 Ion Exchange Chromatography를 2번 연속적으로 수행하여 순수 분리 정제되었고, ELISA 분석결과 99% 이상으로 재조합 EGF의 활성도가 상업용 EGF와 유사하게 나타났으며, 세포증식시험 결과 인간 재조합 EGF는 인체 피부 섬유아세포의 세포증식을 촉진하는 것으로 확인 되었다. 본 연구의 인간 EGF 발현 시스템은 양적인 측면 뿐 아니라 성공적인 활성형태의 발현으로 추가적인 재접힘 과정 및 N 말단의 융합부분을 제거하기 위한 크로마토그래피 작업이 필요가 없다는 점에서 기존의 방법들에 대체 될 수 있는 효과적인 인간 EGF 발현 시스템을 제공하고 있다.

Real time optimization of fed-batch culture of recombinant yeast

  • 나정걸;김현한;장용근;정봉현
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2001년도 추계학술발표대회
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    • pp.81-84
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    • 2001
  • A real time optimization algorithm for fed-batch cultures of recombinant yeast to determine the optimal substrate feed rate profile has been developed. Its development involved four key steps: (1) development of reliable adaptive model. (2) development of optimization algorithm. (3) design of on-line model update algorithm to be incorporated into the optimization algorithm and (4) experimental validation. A recombinant Saccharomyces cerevisiae producing human parathyroid hormone (hPTH) was chosen as the model strain. It was found to be very successful in maintaining cell growth and galactose consumption at leigh levels, thus resulting in significant improvements in the productivity (up to 2.1 times) and intact hPTH concentration (up to 1.5 times) compared with the case of an intermittent glucose and galactose, or galactose feeding.

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In Vitro에서 Retrovirus Vector System을 이용한 인간 성장 호르몬 유전자의 발현 (Expression of Human Growth Hormone Gene using Retrovirus Vector System In Vitro)

  • 김민기;구본철;권모선;김태완
    • Reproductive and Developmental Biology
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    • 제35권3호
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    • pp.251-256
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    • 2011
  • Human growth hormone (hGH), one of the most important hormones in medicine, is secreted from anterior pituitary gland. Its broad physiological function includes body growth, cell regeneration, increasement of muscle volume, bone density, body fat reduction, and so on. Due to the wide range of therapeutic effects, the hGH produced from E. coli has been commercialized already. In this study, we asked whether it is possible to produce recombinant hGH efficiently from various cultured mammalia cells. To meet this purpose, we chose a retrovirus vector system for transfer and expression of the hGH gene in various mammalian cells. Analyses of RT-PCR, ELISA, and Western blot to determine expression of the hGH gene showed the highest production of the hGH was determined from chicken embronic fibroblast (CEF) cells with the concentration of 8.58 ${\mu}g$/ml. The biological activity of the hGH was similar to the commercially available counterpart. These results suggest that mass production of hGH is possible not only in the E. coli but also in the various mammalian cells.