• Journal of Ginseng Research
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• v.18 no.2
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• pp.102-107
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• 1994

When at liver homogenates were incubated with 1mM $CCl_4$ for five min, glycogen level was decreased, while treatment with protein fraction $G_4$ increased the glycogen level. In addition $G_4$ inhibited the phosphorylation of 34 KD and 118 KD polypeptides induced by $CCl_4$. These protein were more strongly phosphorylated by $Ca^{2+}$/calmodulin-dependent kinase than by C-kinase. Since 34 KD polypeptide was solely phosphorylated by NaF (50mM), an inhibitor of both glycogen syntheses and phosphoprotein phosphates, it is inferred that 3 KD polypeptide is glycogen synthase-likd protein. Because glycogen synthesis is inhibited by phosphorylation of $Ca^{2+}$-dependent glycogen syntheses, it is suggested that $G_4$ increased liver glycogen level by inhibiting phosphorylation of 34 KD polypeptide which is thought to glycogen syntheses-like protein.

• The Korean Journal of Zoology
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• v.39 no.2
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• pp.123-131
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• 1996

In this study, we examined the expression of heat shock proteins (HSPs) in fish cell line CHSE-2lnl and human HeLa cells exposed to heat shock. In fish CHSE-214 cells HSP70 was the major polvpeptide induced by an elevated temperature or an amino acid analog, while in HeLa cells HSP90 as well as HSP70 were prominently enhanced in response to these stresses. Pretreatment of actinomvcin D prior to heat shock completely inhibited the induction of fish HSP70, indicating the transcriptional regulation of fish HSP70 gene expression. In HeLa and CHSE-214 cells either recovering from heat shock or experiencing prolonged heat shock, attenuation in the HSP90 a'nd HSP70 induction occurred but both induction and repression of HSP70 synthesis appear 19 precede those of HSP90. Moreover, attenuation did not occur in the syntheses of 40 kDa and 42 kOto proteins which were only induced in CHSE-214 cells. The enhanced syntheses of these he proteins continued as long as CHSE-214 cells were Siven heat shock. These results suggest that down-regulation of HSP syntheses during prolonged heat shock may be controlled by several different. as vet undefined, mechanisms.

• Archives of Pharmacal Research
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• v.14 no.4
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• pp.325-329
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• 1991

Effects of Lycii Fructus on primary cultured chicken embryonic brain cells were studied by microscopic observation, determination of the activity of pyruvate dehydrogenase complex (PDHC), and syntheses of protein, RNA and DNA. The brain cells were prepared from the brains or 10-day-old chicken embryos and cultured with a deficient medium. The activity of PDHC in the brain cells cultured with a deficient medium was increased to 1.8 times by the addition of $30\;{\mu}g/ml$ of the total methanol extract of Lycii Fructus. To seek the active fraction, total methanol extract was further fractionated by the polarity. The survival rate of neuronal cells was significantly increased by the addition of $100\;{\mu}g/ml$ of the buthanol or aqueous fraction. At this concentration, the significant increase of the syntheses of protein and RNA, but not of DNA, indicates that the fractions may act on the neuronal cells which are known to be non-dividing cells.

• Korean Journal of Poultry Science
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• v.43 no.4
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• pp.213-218
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• 2016

This study was conducted to investigate the effect of taurine supplementation on heat shock protein 70 and in vitro protein turnover in broiler chicks under chronic heat stress. Chicks were allocated into 3 groups of 10 birds per group; the control group was maintained at a temperature of $24^{\circ}C$ without taurine (CO group), the heat-stressed group maintained at a temperature of $34^{\circ}C$ without taurine (HO group), and heat-stressed group maintained at a temperature of $34^{\circ}C$ with taurine (HT group). The final body and liver weights of broilers in the HO and HT groups were significantly lower than those of broilers in the CO group (P<0.05). However, these parameters of the broilers in the HT group were significantly higher than those of broilers in the HO group (P<0.05). The heat shock protein 70 (hsp70) concentration in the liver of broilers in the HO group was significantly higher than that of broilers in the CO and HT groups, but the hsp70 concentration in the liver of broilers in the HT group was not different from that of broilers in the CO group. Liver homogenates of 21 day-old broilers were incubated at temperatures of $37^{\circ}C$ and $45^{\circ}C$ to prove the effect of high temperature and taurine on total protein syntheses. Neither high temperature nor taurine supplementation affected protein syntheses in liver homogenates of the broilers. However, the more the temperature increased, the more the degradation rates of cytoplasmic protein in liver homogenates increased; however, taurine supplementation had no effects on the protein syntheses in the liver of the broiler. It is possible that taurine indirectly affected protein turnover via various physiological mechanisms.

• Proceedings of the Korea Crystallographic Association Conference
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• 2000.05a
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• pp.11-11
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• 2000

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.29-32
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• 2000

• Proceedings of the Korean Fiber Society Conference
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• 1989.06a
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• pp.30-31
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• 1989

• Journal of Welding and Joining
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• v.24 no.5
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• pp.15-21
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• 2006

• 한국전기화학회:학술대회논문집
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• 2004.04a
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• pp.5-5
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• 2004

• Proceedings of the Korean Society of Applied Pharmacology
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• 1999.04a
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• pp.27-32
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• 1999