Hotelbuchung
Hotel Registration
Grußwort
Welcome address
Beteiligte Gesellschaften
Societies involved
DOG Information
DOG Information
Eröffnung des Kongresses
Opening Ceremony
Preise
Awards
Ablauf der Tagung 2003
General overview of congress
Lageplan der Räumlichkeiten
Map of Congress Center
Wissenschaftliche Themen
Scientific topics
Symposien
Symposia
Wissenschaftliches Programm
Scientific program
Posterpräsentationen
Poster Presentation
Kurse
Courses
Begleitende Veranstaltungen
Accompanying program
Arbeitssitzungen
Working sessions
Rahmenprogramm
Social program
Allgemeine Informationen
General Information
Autorenindex
Index of Authors
Industrieaussteller
Commercial exhibitors
Sponsoren
Sponsors
Impressum
DOG Homepage
Abstract
Abstract
A Proteomic Approach to PVR: Comparative Proteome Analysis of Native, Differentiated and Cultured, Dedifferentiated Human RPE Cells
Alge C. S.1,2, Suppmann S. 2,3, Priglinger S. G.1, Neubauer A. S.1, Welge-Lussen U.1, Ueffing M. 2,3, Kampik A. 1,2
1Department of Ophthalmology, Ludwig-Maximilians University, Munich; 2Clinical Cooperation Group Ophthalmogenetics, Ludwig-Maximilians University; 3GSF-Research Center for Environment and Health, Oberschleißheim
Purpose: Dedifferentiation of retinal pigment epithelial (RPE) cells is considered to be a crucial event in the pathogenesis of proliferative vitreoretinopathy (PVR). In an attempt to better understand the pathophysiology of early PVR, the protein expression pattern of native, differentiated RPE cells was to that of cultured, thereby dedifferentiated RPE cells.
Method: Differentiated, native human RPE cells and dedifferentiated, cultured human RPE cells were analyzed by 2-D electrophoresis. Total cellular proteins were separated by isoelectric focusing using immobilized pH gradients (IPG 3-10) and electrophoresis on 9 - 15% gradient polyacrylamide gels. Proteins were visualized by silver staining. 2-DE gels of both cell-types were then compared and spots of interest were analyzed by MALDI-TOF (matrix-assisted laser desorption ionization time of flight) mass spectroscopy. The resulting peptide mass fingerprints were searched against the NCBInr, MSDB and EnsemblC database to identify the respective prote