Thioredoxin family proteins in physiology and disease [Elektronische Ressource] / Eva-Maria Hanschmann. Betreuer: Christopher Horst Lillig

Vom Fachbereich Medizin der Philipps-Universität Marburg als Dissertationangenommen am: 02.09.2011Gedruckt mit Genehmigung des Fachbereichs:Dekan: Prof. Dr. med. Matthias RothmundReferent: PD Dr. rer. nat. Christopher Horst LilligKorreferent: Prof. Dr. med. Joachim HoyerDepartment of Clinical Cytobiology and Cytopathology, Prof. Dr. Roland Lill, Medical Faculty of the Philipps-Universität Marburg______________________________________________________________________Thioredoxin family proteins i nphysiology and diseaseEva-Maria HanschmannMarburg, 2011Numerous cellular processes are controlled by redox regulation via posttranslationa lmodifications at thiol (SH) groups, i.e. for instance the formation of disulfi de bonds(S-S), glutathionylation (S-SG) and nitrosylation (S-NO). Redox signaling is m ediatedby reactive oxygen species (ROS) and reactive nitrogen species (RNS) and members of the thioredoxin family of proteins. Exemplary human Trx1 is depicted in the cove rpicture. Redox signaling is essential for regulating the fate of a cell . Hence,disregulation of redox control ha bes en implicated in various diseases leading e.g. toenhanced proliferation in cancer or to apoptosis in degenerative disorders. The cover picture depicts a healthy cell to the left and a cell undergoing apoptos is to theright, characterised by condensation of DNA, membrane blebbing and phagocytosi s ofdamaged organelles.