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Session XVII : Cell signaling in health and disease Poster XVII, 53 HSP90 INHIBITION BY GELDANAMYCIN UPREGULATES EXPRESSION OF HEAT SHOCK PROTEINS IN PC-12 CELLS. Christina B. Wiegand 1, Madhavi J. Rane3, Leroy R. Sachleben Jr 2, Rachel Wu 3 and Evelyne Gozal 1,2 Depts of Pharm. & Tox.1, Pediatrics2, Medicine3, University of Louisville, Louisville, KY Heat shock proteins (Hsps) play a role in cellular injury, proteins repair and ubiquitination, or induction of apoptosis when cells are beyond repair. Hsp90 regulates the function of its client proteins and can bind Akt kinase or heat shock factor (HSF). Upon cellular stress HSF is released to the nucleus to induce Hsps transcription. Geldanamycin (GA) binds Hsp90 ATPbinding site, inhibiting its ATPase function and disrupting protein associations. We previously showed that 6h sustained hypoxia (SH; 0.1% O2) increased Akt-Hsp90 binding and Akt phosphorylation in PC-12 cells, without altering cell survival. However, 24h SH decreased Akt phosphorylation, coinciding with the onset of cell death. GA induced cell death and decreased Akt expression in a dose dependent manner, with higher toxicity in normoxia (RA; 21% O2) than in SH, and disrupted Hsp90-Akt association without affecting SHinduced Akt phosphorylation. Because of Hsps dual function in cellular repair and apoptosis, we hypothesized that GA may affect cell survival by disrupting Hsp90 binding with additional Hsps or with HSF. To determine whether GA modulates Hsps expression, GAtreated cells were exposed to 6h, 12h, and 24h RA or SH. GA increased Hsp25, Hsp70 and Hsp90 expression independently from FiO2, while Akt/Hsp90 binding was differentially altered in SH and RA. Thus, increased Hsps expression observed in GA-treated PC-12 cells may result from the dissociation of HSF from Hsp90 and its subsequent translocation independently from the hypoxic stress. Increased Hsps expression may initially protect cells from cytotoxic effects of low GA concentrations, as suggested by GA dose-dependent effect on cell survival. However, longer GA exposures may increase cell death resulting from accumulating damaged proteins or SH-related energy depletion. We are currently investigating changes in HSF association with the Hsp90 complex in SH and RA GA-treated cells. These findings suggest that disruption of Hsp90 chaperone functions by GA leads to inactivation of survival pathways, alterations in the protein associations of Hsp90 complexes, and induction of stress proteins targeting cells to apoptosis. NIH F30-NS051998-01, HL- 074296, 2 P20 RR15576-06, and AHA 0335278N. - 660 -
Session XVII : Cell signaling in health and disease Poster XVII, 54 The effect of UV-irradiation on telomerase activity and other stress-related proteins in lens epithelial cells WU Zhi-hong,(!"!) ZHANG Jin-shong#"#$% Department of Ophthalmology, the Forth Affiliated Hospital, China Medical University. Shenyang 110001, China Corresponding author: WU Zhi-hong Email: fswuzhihong@sina.com&bjwuzhihong@yahoo.com Background To investigate the change and role of telomerase activity and other stressrelated proteins UV-induced DNA damage and repair in lens epithelial cells. Methods Human lens epithelial cells were irradiated at UV-doses 0.0(control group) and 0.5'1.5'2.5'3.5'5.0'7.5'10.0 mJ/cm2(treated 1~7group). telomerase activity was determined by Telomerase Repeat Amplification Protocol-Enzyme Linked Immunosorbent Assay#TRAP-ELISA%(P53'P21'growth arrest and DNA damage inducible (GADD45)'proliferating cell nuclear antigen(PCNA) and P16 protein levels were analyzed by Western blotting. Results Telomerase activity in control group and treated 1~7group showed increased tendency, compairing in 8 groups, there are significant difference (F=45.65,P
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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 IX. Novel compounds targeti
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Session X : Cell death in cancer -
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Session X : Cell death in cancer Po
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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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Page 675 and 676: Dr. Nassera Aouali L-1526 Luxembour
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