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백융기 漢陽大學校 基礎科學硏究所 1991 基礎科學論文集 Vol.10 No.-
인체 아포리포단백질 E 유전자의 intragenic sequences 내에 존재하는 전사조절군을 mapping 하기 위하여 이 유전자의 전 지역을 6개 부분으로 자른후 testing vector인 pTK1 plasmid의 upstream 쪽에 삽입 하여 subcloning 하였다. 이로부터 얻어진 recombinant DNA는 DNA uptake 율이 가장 높은 CHO cell에 transfection 시켜 각각의 CAT activity를 측정한 결과 최소한 2개 지역이 enhancer-like 기능을 갖고 있음을 확인하였다. 이들은 -365/+35 지역 (I)과 +23/+806지역(II)으로서 I은 비교적 non-cell type specificity를 갖는 반면, II는 부분적인 cell type specificity를 보여주었다. 특히 II지역의 +160/+190부분은 gel retardation assay에 의해 3개의 핵단백질 결합부위를 갖고 있음이 확인되었다. 이 결과는 아포리포단백질 E의 전사적인 조절에 복합적인 cis-acting regulatory elements와 trans-acting factor가 관여하고 있음을 시사한다. To identify the transcriptional regulatory elements resided in the intragenic sequences of the human apolipoprotein (apo-) E gene, the whole gene (-0.6kb to ++1.5kb) was excised into six fragments and each of which was then subcloned inti the 5'-upstream of the testing vector, pTK1 plasmid which contains thymidine kinase-deriven chloramphenicol acetyltransferase(CAT) coding gene. The apo-E/CAT recombinants were transfected into the chinese hamster ovary (CHO) cells which beared the highest transfection efficiency among the cell lines examined. The CAT analyses using the protein extracts obtained from the CHO cells indicate that there are at least two enhancer-like sequences within 1.1 kilobase (kb) fragment spanning nucleotides -365 to +35(I) and the intron regulatory sequences spanning nucelotides +23 to +806(II). The region I shows non-cell type specificity while II confers partial cell type specificity. DNaseI footprinting assay and gel retardation analyses revealed that there are at least three nuclear proteins that bind specifically to the regionII. Thus, the transcriptional control of the human apo-E gene appears to require the multiple cis-action regulatory elements as well as trans-action factors.
Alterations of Protein Expression in Macrophages in Response to Candida albicans Infection
백융기,Yu-Kyong Shin,김기영 한국분자세포생물학회 2005 Molecules and cells Vol.20 No.2
Although macrophages are an important first line of cellular defense, they are unable to effectively kill phagocytosed C. albicans. To determine the physiological basis of this inability, we investigated the alterations of macrophage proteins caused by C. albicans infection. Since the formation of C. albicans hyphae caused cell death, proteins were prepared 3 h after infection and examined by two-dimensional gel electrophoresis (2-DE). The most prominent changes were in glycolytic enzymes, which could have caused energy depletion of the infected cells. Also changed were proteins involved in maintenance of cellular integrity and NO production. Treatment of the macrophages with either cytochalasin D or taxol did not alter their inability to kill C. albicans. Our results indicate that multiple factors contribute to cell death as the pathogenic form of C. albicans becomes fully active inside macrophage cells.