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Session X : Cell death in cancer Poster X, 43 The anti-cancer activity of decursin and decursinol isolated from Angelica gigas Nakai Mi-Jeong Kim1,2, Won-Yoon Chung1, Jin-Eun Kim1,2, Seung Hwa Son1, Sang Kook Lee3, Kwang-Kyun Park1,2 1Department of Oral Biology, Oral Science Research Institute, Oral Cancer Research Institute, Yonsei university College of Dentistry, Seoul 120-752, Republic of Korea, 2Brain Korea 21 Project for Medical Science, Yonsei University, Seoul Republic of Korea 120-752, Republic of Korea, 3College of Pharmacy , Ewha Womans University, Seoul Republic of Korea 120-750 E-mail: kimmi780507@hanmail.net Angiogenesis, the process of vascular growth by sprouting of preexisting vessels, plays a crucial role in tumor growth and metastasis. Vascular endothelial cell proliferation and migration are critical steps in angiogenesis and are regulated by various growth factors such as vascular endothelial growth factor (VEGF). Angelica gigas Nakai root has been traditionally used in Korean folk medicine as a tonic and for treating anemia and other common disease. In the present study, we observed that decursin and decursinol isolated from A. gigas inhibited VEGF-induced proliferation and migration of human umbilical vein endothelial cells (HUVECs). Also, these compounds showed antiangiogenic activity in a mouse Matrigel plug assay and CAM assay. In addition, decursin and decursinol inhibited the formation of tumor nodules in spontaneous lung metastasis induced with murine colon cancer CT-26 cells in BALB/c mice. Our results suggest that decursin and decursinol possess an antimetastatic potential by suppressing VEGF-induced angiogenesis. Furthermore, to explain the mechanism for how decursin and decursinol block VEGF-induced angiogenesis, we investigated their effect on PI3k/Akt/eNOS signaling in HUVECs. - 376 -
Session X : Cell death in cancer Poster X, 44 ER stress induces Jpk, which inhibits cell cycle progression in F9 teratocarcinoma cell Hye Sun Kim, Kyoung-Ah Kong, Hyunjoo Chung, Sungdo Park, and Myoung Hee Kim Department of Anatomy, Embryology Lab., Brain Korea 21 Project for Medical Science, Yonsei University College of Medicine, Seoul 120-752, Korea. E-mail: goldfish79@hanmail.net; mhkim1@yumc.yonsei.ac.kr A Jopock (Jpk), a trans-acting factor associating with the position-specific regulatory element of murine Hoxa-7, has shown to induce cell death in both prokaryotic and eukaryotic cells when introduced and overexpressed. Since Jpk protein harbors a transmembrane domain (TM) and a putative ER-retension signal at the N-terminus, a subcellular localization of the protein was analyzed after fusing it into the green fluorescent protein (GFP). Both N-term (Jpk-EGFP) and C-term fused-Jpk (EGFP-Jpk) showed to be localized in the endoplasmic reticulum (ER) when analyzed under the fluorescence microscopy after staining the cells with ER- and MitoTracker. Through deletion analysis TM turned out to be important for ER localization of Jpk. When flow cytometric analysis was performed, both cells expressing Jpk- EGFP and EGFP-Jpk led cell cycle arrest and subsequent apoptotic cell death. In order to see whether Jpk is expressed during ER-stress mediated apoptosis, F9 cells were treated with DTT, an ER-stress inducer. In the presence of 4 mM of DTT, about 50% of cells died strongly expressing (7 fold) Jpk as well as Grp78, a molecular chaperone and Chop-10, a well known protein arresting cells at the G0/G1 phase and apoptosis. In summery, excess ER stress inducing apoptosis upregulated the expression of Jpk, which seemed to inhibit the cell cycle progression. These results altogether suggest that Jpk could be a useful cell death triggering molecule applicable for cancer therapy. - 377 -
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- 1 - Luxembourg, January 25th to 2
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Table of content PREFACE ..........
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Preface In 1998, we organized the f
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Acknowledgments This meeting has be
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Group B (15h00 - 17h00) Session V.
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- 11 - Exhibition
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Visit our Expo (in alphabetical ord
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Thursday January 26th, 2006 (Early
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Thursday January 26th, 2006 (Evenin
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Regulation of inflammation and gluc
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Saturday January 28th, 2006 (Early
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Oral presentations (by alphabetical
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4: : Lottin S, Vercoutter-Edouart A
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the B-Raf/mitogen-activated/extrace
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Albertini MC, Accorsi A, Citterio B
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AP-1-dependent gene expression in s
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Jaks and cytokine receptors - an in
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The Role of Met-Gab1 Signalling in
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The mammalian tumor suppressor Scri
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SIGNAL TRANSDUCTION BY STRESS-ACTIV
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Title to be announced Caroline Dive
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Mechanisms of DNA methylation in ma
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Blocking the "4 Integrin-Paxillin I
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Regulation of NF-kB-dependent trans
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The immunomodulator AS101 induces g
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Signaling pathways leading to the a
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Boute, N., Jockers, R. and Issad, T
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Jespsen JS, Sorensen MD and Wengel
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8. Nishikawa, H., Kawai, K., Tanaka
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9) Proteome analysis of rat pancrea
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MicroRNA is an anti-apoptotic facto
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Resveratrol inhibits phorbol ester-
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Cross-talk between angiotensin II a
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Multiple role of histamine H 1 rece
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PI3K Targeting by the Beta-GBP Cyto
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D.P. Chopra, R.E. Menard, J. Janusz
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[2] Meijer, L., Flajolet, M. and Gr
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[4] Niemand, C., Nimmesgern, A., Ha
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Oncogenic signaling by mutant p53 M
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activity of the Peroxisome Prolifer
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Restauration of SHIP-1 activity in
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Hypoxia Signaling. Impact on Tumor
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5. Sokolov EI, Zykov KA, Pukhalsky
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HOW ANTITOXIC AND ANTICANCER AGENTS
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Listeria monocytogenes induced Rac1
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Epigenetic Regulation of Stem Cell
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Survey on in vitro cell death induc
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Distinct roles of IRF-3 and IRF-7 i
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Redox-Sensitive Transcription Facto
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Epigenic control of MHC2TA transcri
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Attenuation of MSK1-driven NF-kB ge
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Talking to chromatin: Silencers Sil
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Ubiquitin ligase Smurf1 controls os
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Workshop presentations (by alphabet
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Ambion MicroRNAs (miRNAs) are small
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Organizer: BIOBASE GmbH Date: Janua
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Reliable and efficient gene Knock-d
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Exploring ubiquitin signaling with
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Poster presentations Poster are cla
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Session I : protein domains Poster
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Session II. Receptor signaling and
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Session II : Receptor signaling and
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Session III. Protein kinase cascade
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Session III : Protein kinase cascad
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Session IV. Protein kinase inhibito
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IV. Protein kinase inhibitors: insi
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IV. Protein kinase inhibitors: insi
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V. Phosphatases as key cell signali
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VI. Proteasome degradation pathways
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VI. Proteasome degradation pathways
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Session VII. Stem cell specific cel
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VIII. Inflammation specific signali
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Session XI : Cell death and cardiov
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Session XI: Cell death and cardiova
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Session XII : Cell death and neurod
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Session XIII : Cell signaling pathw
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Session XIV : Transcriptional and t
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Session XV : Reactive oxygen specie
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Session XVI : Chemopreventive agent
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Session XVII : Cell signaling in he
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Dr. Nassera Aouali L-1526 Luxembour
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Dr. Giordano Bianchi Clinic of inte
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Mrs. Isabel Burghardt Laboratory of
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Pr. Czeslaw Cierniewski 92-215 Lodz
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Dr. Mark Ginsberg Mail code 0726 92
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Dr. Jochen Hefl Division of Signal
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Mr. Jan Jepsen 2100 Copenhagen DNK
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Pr. Young Min Kim Division of Biolo
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Mr. Christoph Lahtz AG Tumorgenetik
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Pr. Etta Livneh 84105 Beer Sheva IS
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Mrs. Rasa Merzvinskyte Department o
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Mr. Gustav Nilsonne Department of L
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Mrs. Christel Péqueux Tumour and D
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Dr. Gabriella Regis Tumor Immunolog
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