Methoxycarbonyl Group as a Conformational Regulator for The Benzene Ring of Triphenylamines

A series of triphenylamine derivatives bearing a methoxycarbonyl group on the benzene ring was synthesized. The structural and physical properties based on the introduction of the methoxycarbonyl group into benzene ring were investigated by single crystal X-ray diffraction, computational studies and spectroscopic methods. It was revealed that the methoxycarbonyl group has not only structural control but also a definite electronic effect on the triphenylamine structure

Rho-mDia1 ジョウホウ デンタツ ケイロ ニ ヨル APC c-Src オ カイシタ イドウ サイボウ ノ キョクセイ ハツゲン キコウ オヨビ サイボウ セッチャクハン サイヘン キコウ ノ カイセキ

京都大学0048新制・課程博士博士(医学)甲第12878号医博第3038号新制||医||938(附属図書館)UT51-2007-H151京都大学大学院医学研究科脳統御医科学系専攻(主査)教授 影山 龍一郎, 教授 鍋島 陽一, 教授 大森 治紀学位規則第4条第1項該当Doctor of Medical ScienceKyoto UniversityDA

Retrospective Proteomic Analysis of a Novel, Cancer Metastasis-Promoting RGD-Containing Peptide

Patients who undergo surgical extirpation of a primary liver carcinoma followed by radiotherapy and chemotherapy leading to complete remission are nevertheless known to develop cancerous metastases 3–10 years later. We retrospectively examined the blood sera collected over 8 years from 30 patients who developed bone metastases after the complete remission of liver cancer to identify serum proteins showing differential expression compared to patients without remission. We detected a novel RGD (Arg-Gly-Asp)-containing peptide derived from the C-terminal portion of fibrinogen in the sera of metastatic patients that appeared to control the EMT (epithelial-mesenchymal transition) of cancer cells, in a process associated with miR-199a-3p. The RGD peptide enhanced new blood vessel growth and increased vascular endothelial growth factor levels when introduced into fertilized chicken eggs. The purpose of this study was to enable early detection of metastatic cancer cells using the novel RGD peptide as a biomarker, and thereby develop new drugs for the treatment of metastatic cancer

The Rho-mDia1 Pathway Regulates Cell Polarity and Focal Adhesion Turnover in Migrating Cells through Mobilizing Apc and c-Src

Directed cell migration requires cell polarization and adhesion turnover, in which the actin cytoskeleton and microtubules work critically. The Rho GTPases induce specific types of actin cytoskeleton and regulate microtubule dynamics. In migrating cells, Cdc42 regulates cell polarity and Rac works in membrane protrusion. However, the role of Rho in migration is little known. Rho acts on two major effectors, ROCK and mDia1, among which mDia1 produces straight actin filaments and aligns microtubules. Here we depleted mDia1 by RNA interference and found that mDia1 depletion impaired directed migration of rat C6 glioma cells by inhibiting both cell polarization and adhesion turnover. Apc and active Cdc42, which work together for cell polarization, localized in the front of migrating cells, while active c-Src, which regulates adhesion turnover, localized in focal adhesions. mDia1 depletion impaired localization of these molecules at their respective sites. Conversely, expression of active mDia1 facilitated microtubule-dependent accumulation of Apc and active Cdc42 in the polar ends of the cells and actin-dependent recruitment of c-Src in adhesions. Thus, the Rho-mDia1 pathway regulates polarization and adhesion turnover by aligning microtubules and actin filaments and delivering Apc/Cdc42 and c-Src to their respective sites of action