This paper describes the traditional Ondol medical care, the specific combination of ancient and contemporary examples to be articulated. As a traditional Korean culture, to be extracted from the historical perspective, it described the relationship and origins between them, From a health perspective, in accordance with the logic and pharmacologyit introduced Ondol as the important principle of health care equipment. The modern architecture of some common harmful to the body, from the perspective of Ondol, it should be improved and based on scientific proof to the theory.

Wntsignaling is involved in the normal development and tumorigenesis via epithelial- mesenchymal transition (EMT). init iated by down-regul ation of E-cadherin by the transc ription factor Snail. Wnt signaling inhi bits Sna il phosph o rylation t hrough Axin2-dependent pathway that sustains nuclear accumul ation 0 1' Snail by driving CSK3ß nucleocytoplasmic export then consequently increases Snail protein levels and induces an EMT However. the roles of Wnt and Axin expression and their functional implication on Snail dependent EMT program a re not clear du ring the multistep carcinogenic process. We examined that canonical Wnt signaling engagingmul t istep carcinogenic process of uterine cervical cancer through Wnt-Axin2-Snail axis. In nonnal cervi cal mucosa, Wntl. Wnt3a. and Axin2 mRNA expression were locali zed in basal cell layer suggesting that canonical Wnt is required for maintenance of self-renewal program of cervica l epi theli al cells. With progression to cervical int r aepithelial neoplasia (CIN) and carcinoma. Wntl, Wnt3a‘ Axin2, and Snail expression were gradually increased in patient samples suggesting that canonical Wnt pathway is involved in earl y step of carcinogenesis in uterine cervix. LRP6 and Axin2 transfected cells showed the highly increased nuclear Snai l resul ted from dec reased level 0 1' nu clear GSK3ß , indicating that LRP6- Axin2 serves to stabili ze Sna il protein levels and susLains iLs nllclear acc llrnulation by driv ing GSK3ß . RNA interference of Axin2 and Snail on SiHa cells relieved E-cadherin proximal promotel‘ activity and block the in 띠 vo chorioalantoic membra ne ln VaSlOn These results suggest the canon ical Wnt signa ling regul ating Axin2-GSK3ß compartmentalization may important for stabi li zation of E- cad herin repressor Snail during the multistep carcinogen ic process of uteri ne cervix. It may lead to not only tracing the proper biomarker 0 [' ca ncer progression‘ but a lso the development oJ new targets for therapeutic intervention in cancer

This study was conducted to examine the effect of IRES controlled reporter gene on screening and production of recombinant human erythropoietin (EPO) proteins from cultured CHO cells. The cDNA was cloned for EPO from human liver cDNA. Using site-directed mutagenesis, we generated recombinant human EPO (rhEPO) with two additional N-glycosylations (Novel erythropoiesis-stimulating protein: NESP). Wild type hEPO and NESP were cloned into expression vectors with GFP reporter gene under regulatory control of CMV promoter and IRES so that the vectors could express both rhEPO and GFP. The expression vectors were transfected to cultured CHO-K1 cells. Under microscopy, expression of GFP was visible. Using supernatant of the culture, ELISA assay, immunocytochemistry and in vitro assay using EPO dependant cell line were performed to estimate biological activity to compare the production characteristics (secretion levels, etc.) between rhEPO and NESP. The activity of NESP protein, obtained by mutagenesis, was described and compared with its rhEPO counterpart produced under same conditions. Although NESP had less secretion level in CHO cell line, the biological activity of NESP was greater than that of rhEPO. These results are consistent with previous researches. We also demonstrated that rhEPO and GFP proteins expressed simultaneously from transfected CHO cell line. Therefore we conclude that use of GFP reporter gene under IRES control could be used to screen and produce rhEPO in cultured CHO cells.