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궁경1호전(宮頸1號煎)이 자궁경부암세포(子宮頸部癌細胞)(HeLa Cell)에 미치는 영향(影響)
강영금,최창민,조한백,유심근,Kang, Young-Keum,Choe, Chang-Min,Cho, Han-Back,Yoo, Sim-Keun 대한한방부인과학회 2005 大韓韓方婦人科學會誌 Vol.18 No.1
To address the ability of Kung-Kyung-Ilho-Jeon(KK) to induce cell death, we investigated the effect of KK on cell viability. Forty-eight hours later, loss of viability occurred following KK exposure in a dose-dependent manner. The treatment of KK, a commonly used herb formulation in Korea and China, caused a decrease in cell viability. KK also resulted in apoptotic morphology a brightly blue-fluorescent condensed nuclei by Hoechst 33258-staining, and reduction of cell volume. Our results show that KK induces caspase-3 and -9 activation in a time-dependent manner. In addtion, the translocation of cytochrome c release into cytoplasm has been observed under the presence of $5mg/m{\ell}$ KK. The subsequent loss of mitochondria membrane potential is collapsed by the addition of KK. Our immunoblotting data show that PARP, a well known caspase-3 and -6 substrate, is cleaved by KK. We show that a pro-apoptotic protein, Bax is increased in the presence of KK but that the amount of Bcl-2 is not changed. We suggest that Bax, a critical protein which can regulate channel of mitochondria to release cytochrome c, is a key protein in KK-induced apoptosis of Hela human cervical carcinoma cells
김국래,강영금,조현수 한국구조생물학회 2014 Biodesign Vol.2 No.1
G-protein-coupled receptors (GPCRs) are seven-transmembrane proteins that play important roles in signal transductionfrom the extracellular compartment to the cytoplasm. GPCR malfunction has been implicated in various diseases such ascancer, allergy, neuronal disease, rheumatism, and obesity. Because of the importance of GPCRs, GPCR-targeting drugsoccupy approximately 40% of the total drug market. Recently, three-dimensional structures of many GPCRs have beensuccessfully ascertained on the basis of various developed methods that improve protein stabilization, crystallization, anddiffraction. Some GPCR structures have elucidated the underlying activation mechanism by allowing comparison betweenthe receptor’s inactive and active states. β-adrenergic receptor bound with G-protein trimeric complex (Gαβγ) structure hasalso been determined. To date, XFEL technology is the latest technology used to determine GPCR structures. In this review,we describe GPCR structures, structure-based activation mechanisms and principles, and the application of XFEL indetermining GPCR structures and development of GPCR-based drugs.