• Korean Journal of Fisheries and Aquatic Sciences
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• v.20 no.5
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• pp.431-440
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• 1987

In order to develop a new type of food source for the effective utilization of fish protein, plastein reaction was applied to improve the functional properties of filefish protein. Plasteins were synthesized from a peptic filefish protein hydrolysate by papain, pepsin, $\alpha-chymotrypsin$ and protease(from Streptomyces griceus) under the optimum conditions of previous paper). Also, L-glutamic acid diethylester and L-leucine ethylester were incorporated into plastein during the plastein reaction by papain. And, General composition, yield, molecular weight, amino acid composition, color and IR spectrum of plasteins were measured. The protein, ash and lipid content of the plasteins were $72\~78\%,\;7.4\~11.8\%\;and\;0.3\~0.9\%$ respectively. The yield of plasteins were papain $55.0\%,\;pepsin\;47.6\%,\;\alpha-chymotrypsin\;38.3\%,\;protease\;23.6\%$, glutamic acid-incorporated plastein (Glu-Plastein) $35.0\%$, and leucine-incorporated plastein (Leu-plastein) $45.7\%$. The glutamic acid and leucine content in Glu-plastein and Leu-plastein were $38.7\%,\;41,7\%$, respectively, while the contents in the peptic filefish protein hydrolysate were $16.01\%\;and\;8.16\%$, respectively. The amino acid compositions were similar to that of the original filefish muscle protein. The major molecular weights of the peptic hydrolysate estimated by gel filteration were 2,000 and 310, and those of plasteihs were 21,000 and 4,900 for papain, 24,000 for pepsin, 18,500 for $\alpha-chymotrypsin$ 6,700 for protease, 24,000 for Glu-plastein and 17,000 for Leu-plastein. The structural changes in freeze-dried filefish meat, the FPC and hydrolysate were not observed on the IR spectrum. But plasteins showed amide I band in $1,600\~l,700cm^{-1}$ range and resulted in a strong band in $800\~850\;cm^{-1},\;700\~750\;cm^{-1}\;and\;650\~700\;cm^{-1}$. The amide I band of Glu-plastein was wider than those of other plasteins and had also a small band at $1,440\;cm^{-1}$.

• Journal of Life Science
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• v.30 no.2
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• pp.211-220
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• 2020

The activity of CAR can be regulated not only by ligand binding but also by phosphorylation of regulatory factors involved in extracellular signaling pathways, cross-talk interactions with transcription factors, and the recruitment, degradation, and expression of coactivators and corepressors. This regulation of CAR activity can in turn have effects on the control of diverse physiological homeostasis, including xenobiotic and energy metabolism, cellular proliferation, and apoptosis. CAR is phosphorylated by the ERK1/2 signaling pathway, which causes formation of a complex with Hsp-90 and CCRP, leading to its cytoplasmic retention, whereas phenobarbital inhibits ERK1/2, which causes dephosphorylation of the downstream signaling molecules, leading to the recruitment to CAR of the activated RACK-1/PP2A components for the dephosphorylation, nuclear translocation, and the transcriptional activation of CAR. Activated CAR cross-talks with FoxO1 to induce inhibition of its transcriptional activity and with PGC-1α to induce protein degradation by ubiquitination, resulting in the transcriptional suppression of PEPCK and G6Pase involved in gluconeogenesis. Regulation by CAR of lipid synthesis and oxidation is achieved by its functional cross-talks, respectively, with PPARγ through the degradation of PGC-1α to inhibit expression of the lipogenic genes and with PPARα through either the suppression of CPT-1 expression or the interaction with PGC-1α each to induce tissue-specific inhibition or stimulation of β-oxidation. Whereas CAR stimulates cellular proliferation by suppressing p21 expression through the inhibition of FoxO1 transcriptional activity and inducing cyclin D1 expression, it suppresses apoptosis by inhibiting the activities of MKK7 and JNK-1 through the expression of GADD45B. In conclusion, CAR is involved in the maintenance of homeostasis by regulating not only xenobiotic metabolism but also energy metabolism, cellular proliferation, and apoptosis through diverse cross-talk interactions with extracellular signaling pathways and intracellular regulatory factors.

• Korean Journal of Poultry Science
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• v.20 no.2
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• pp.93-105
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• 1993

This study was carried out to determine the concentrations of previtamin D$_3$(PreD$_3$), lumisterol$_3$(L3), tachystero1$_3$(73), vitamin D$_3$(VD$_3$) and provitamin D$_3$(ProD$_3$) in leg skins of broiler chicks exposed to UVB lights (maximum intensity at 297 nm) with dose of 0.204 or 0.409 mJ/$\textrm{cm}^2$(30 or 60 min irradiation) . The broiler Hubbard line day old chicks(2 dose $\times$9 elapsed time $\times$4 replica＋10 control＝82) were fed VD-deficient diet for 31 days in a windowless subdued light room. The skin was collected at 0, 6, 12, 18, 30, 42, 66, 90 or 138 hr after UVB irradiation. The skin lipid was extracted by 9％ ethyl acetate/n-hexane, and the fraction of VD$_3$ and its analogues was purified by Sep-Pak silica cartridge. The straight phase HPLC was utilized to analyze ProD$_3$ and its products. The mole ％(absolute level expressed in ng/$\textrm{cm}^2$) of PreD$_3$ in leg skin (epidermis＋dermis) was 4.67％(44 ng/$\textrm{cm}^2$) or 3.97％(37 ng/$\textrm{cm}^2$) right after UVB irradiation by 0.204 or 0.409 mJ/$\textrm{cm}^2$(30 or 60 min) at 15 cm distance, respectively. It content in leg skin at 0 hr after exposure was 7.24％(12 ng/$\textrm{cm}^2$) or 0.92％(9 ng/$\textrm{cm}^2$), respectively. The increase in irradiation dose did not affect proportionally the If synthesis.73 concentration in leg skin was 0.58％(S ng/$\textrm{cm}^2$) or 0.57％(6 ng/$\textrm{cm}^2$), respectively 0 hr after irradiation. The VD$_3$ in leg skin of birds exposed to UVB light with dose of 0.204 or 0.409 mJ/$\textrm{cm}^2$ was 2.13％ (21 ng/$\textrm{cm}^2$) or 0.97％ (16ng/$\textrm{cm}^2$), respectively at 0 hr after exposure, 2.72％(26ng/$\textrm{cm}^2$) or 3.84％(37ng/$\textrm{cm}^2$), respectively at 6 hr, and 4.30％ ((33ng/$\textrm{cm}^2$) or 6.40％(76ng/$\textrm{cm}^2$), respectively at 12 hr. The peak concentration of VD$_3$ was presented at 18 or 30 hr when 0.204 or 0.409 mJ/$\textrm{cm}^2$) was treated, respectively. It was shown that 18~30 hr were necessary for the thermal conversion of PreD$_3$ into VD$_3$ in the leg skin of broiler chicks. The ProD$_3$ contents in leg skins of negative control, 0.204 mJ/$\textrm{cm}^2$ and 0.409 mJ/$\textrm{cm}^2$ treated birds were 966, 948 and 815 ng/$\textrm{cm}^2$, respectively at right before and after UVB exposure. It was estimated that 18 or 151 ng/$\textrm{cm}^2$ of ProD$_3$ was isomerized to PreD$_3$, L$_3$, T$_3$ and VD$_3$ when exposed to 0.204 or 0.409 mJ/$\textrm{cm}^2$, respective)y. Consequently it was shown that when double dose of UVB light was applied to irradiate the chick body, more but not double synthesis of VD$_3$ and its analogues was occured in leg skin of brolier chicks.