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Mitochondrial Ribosomal Protein L41 Suppresses Cell Growth in Association with p53 and p27^(Kip1)
유영도,유영아,김미진,정영민,김정진,이승백,황인태,나아람,유봉상 이화여자대학교 세포신호전달연구센터 2006 고사리 세포신호전달 심포지움 Vol. No.8
The p53 protein arrests the cell cycle at the G1 phase when stabilized by the interaction between ribosomal proteins and HDM2 under growth-inhibitory conditions. Meanwhile, p53, when translocated to the mitochondria in response to cell death signals, induces apoptosis via transcription-independent mechanisms. In this report, we demonstrate that the mitochondrial ribosomal protein L41(MRPL41) enhances p53 stability, and contributes to p53-induced apoptosis in response to growth inhibitory conditions such as actinomycin D treatment and serum starvation. An analysis of MRPL41 expression in paired normal and tumor tissues revealed lower expression in tumor tissue. Ectopic MRPL41 expression resulted in inhibition of the growth of cancer cells in tissue culture and tumor growth in nude mice. We discovered that MRPL41protein is localized in the mitochondria, stabilizes the p53 protein, and enhances its translocation to the mitochondria thereby inducing apoptosis. Interestingly, in the absence of p53, MRPL41 stabilizes the p27^(Kip1) protein, and arrests the cell cycle at the G1 phase. These results suggest that MRPL41 plays an important role in p53-induced mitochondria-dependent apoptosis and MRPL41 exerts a tumor-suppressive effect in association with p53 and p27^(Kip1).
Synergistic effect of peroxiredoxin II antisense on cisplatininduced cell death
유영도,YoungMinChung,박종국,안철민,SungKyuKim,김형중 생화학분자생물학회 2002 Experimental and molecular medicine Vol.34 No.4
Peroxiredoxin II (Prx II) is known not only to protectcells from oxidative damage caused by hydrogen per-oxide (H2O2), but also to endow cancer cells with resis-tance to both H 2O2 and cisplatin and to grant themradioresistance. In this study, we examined whetherPrx II antisense could enhance cisplatin-induced celldeath. When gastric cancer cells were transfected withvarious concentrations of Prx II antisense plasmid,pPrxII/AS, and then treated with the same concentra-tions of cisplatin, Prx II antisense enhanced cisplatin-induced cell death. The combination index (CI) at alldoses of the combination was below 1, indicating thatPrx II antisense sensitized cisplatin-induced cell death.This synergism was also observed in the cells trans-fected with a Prx II antisense oligomer. Our presentresults, therefore, suggest that Prx II antisense wouldbe a very good sensitizer for cisplatin, and that Prx II asa target for chemosensitizers constitutes a promisingavenue for future research.
유영아(劉英雅) 한국목간학회 2011 목간과 문자 Vol.8 No.-
張家山漢簡 『二年律令』 「傅律」은 국가가 稅役부과 대상을 파악하고 장부에 등재하기 위하여 대상자를 정의하는 ‘傅’의 기준과 절차를 규정한 것이다. 특히 그 규제의 기준이 爵級에 의하여 차등으로 적용되는 것이 많았다. 354簡에서 357簡까지는 爵級에 따라 ?米의 지급, 授杖, 免老, 晥老에 도달하는 연령을 달리 규정하고 있다. 358簡은 簡이 둘로 나누어져 있고 글자가 결여된 곳이 있기는 하지만 5인이상의 子가 낳아서 그들이 일정한 연령에 도달할 경우 父가 免老가 되는데, 그 연령이 父爵 혹은 爵에 의해 규정된다. 359簡-365簡에서는 有爵子의 後者(爵계승자)를 제외한 子들에게 父爵에 비해 일정등급 체감된 爵을 사여하고 인원에 제한을 두었다. 또한 父의 爵級과 본인의 爵級에 따라 각각 상이한 傅의 연령을 규정하여 爵 4級 不更 이하 및 無爵者인 경우 子가 傅되는 연령은 20세였고, 20세이상 24세까지는 父爵과 본인 爵에 따라 우대 받았다. 한편 ‘傅’의 대상을 연령 이외에 장애와 신장을 기준으로 분류하였으며, 父의 家業이 세습되는 職責인 경우에도 ‘傅’의 연령이 정해진 것으로 보인다.
유영도,한문희,김지영,Yoo, Young-Do,Han, Moon-Hi,Kim, Ji-Young 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.2
프로트롬빈 두단계측정법에서 프로트롬빈을 트롬빈으로 전환시키는데 Echis carinatus독으로부터 분리된 프로트롬빈 활성화 효소인 프로트롬빈을 트롬빈으로 약 30분이내에 거의 전환시켰다. 생성된 트롬빈의 활성은 반응시간이 20시간 경과하여도 안정하게 유지되었다. 한편 프로트롬빈을 혈장-혈청 혼합물을 이용하여 트롬빈으로 전환시켰을 때는 약 9분정도 경과되면 생성된 트롬빈의 활성이 감소함을 보여주었다. 트롬빈 효소의 기질로써 피브리노젠과 합성핵원체 기질을사용하여 프로트롬빈을 측정할 수 있는 농도의 범위를 조사하였다. Clotting assay에서 프로트롬빈 측정 가능범위는 2 ${\mu}g/ml$-100 ${\mu}g/ml$이었으며 chromogenic assay에서는 0.2 ${\mu}g/ml$-16 ${\mu}g/ml$이었다. 프로트롬빈을 활성화시키지 않고 직접 측정하기위하여 효소를 이용한 면역측정법 (ELlSA)을 개발하였다. lndirect ELlSA방법에 의해서는 최소 40 ng/ml, sandwich ELlSA를 사용하여 소 혈장의 프로트롬빈 농도를 측정 한 결과 224 ng/ml이었으며 within-run은 9.3%, between-run은 15.8%의 변화를 보여주었다. In a two-stage assay of prothrombin, prothrombin was activated to thrombin by ecarin, the prothrombin activator from the venom of Echis carinatus, in the absence of calcium ions and phospholipid. The activation was almost complete within 30 minutes and the thrombin generated was not inhibited by the ecarin activation mixtures for a incubation time up to at least 20 hours, while it was inhibited by the absorbed plasma- serum mixture after 9-minute incubation. Two different substrates, fibrinogen and a synthetic chromogenic substrate, were used for assays of the thrombin activity and compared in their sensitivies in detection of prothrombin. The standard curve was linear between 2 ${\mu}g/ml$ of prothrombin concentration in the clotting assay, and between 0.2 ${\mu}g/ml$ and 16 ${\mu}g/ml$ in the chromogenic assay. In addition we developed the enzyme-linked-immunosorbent assays for the direct measurement of prothrombin. The minimum detectable concentrations of prothrombin by the indirect ELISA and the sandwich ELISA were 40 ng/ml and 3 ng/ml, respectively. The prothrombin level in bovine plasma was determined to be 224 ng/ml by the sandwich ELISA. The reliability of the sandwich ELISA was demonstrated by the within runs and between runs tests, which were 9.3% and 15.8%, respectively.
포로트롬빈의 측정시스템 : 프로트롬빈 활성화 효소로써 ecarin 을 사용한 두단계 측정법과 효소를 이용한 면역측정법 ( ELISA )
유영도,한문희,김지영 ( Young Do Yoo,Moon Hi Han,Ji Young Kim ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.2
In a two-stage assay of prothrombin, prothrombin was activated to thrombin by ecarin, the prothrombin activator from the venom of Echis carinatus, in the absence of calcium ions and phospholipid. The activation was almost complete within 30 minutes and the thrombin generated was not inhibited by the ecarin activation mixtures for a incubation time up to at least 20 hours, while it was inhibited by the absorbed plasma-serum mixture after 9-minute incubation. Two different substrates, fibrinogen and a synthetic chromogenic substrate, were used for assays of the thrombin activity and compared in their sensitivies in detection of prothrombin. The standard curve was linear between 2 ㎍/㎖ of prothrombin concentration in the clotting assay, and between 0.2 ㎍/㎖ and 16 ㎍/㎖ in the chromogenic assay. In addition we developed the enzyme -linked -immunosorbent assays for the direct measurement of prothrombin. The minimum detectable concentrations of prothrombin by the indirect ELISA and the sandwich ELISA were 40 ng/㎖ and 3 ng/㎖, respectively. The prothrombin level in bovine plasma was determined to be 224 ng/㎖ by the sandwich ELISA. The reliability of the sandwich ELISA was demonstrated by the within runs and between runs tests, which were 9.3% and 15.8%, respectively.