Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/34092
Title: Synthesis, characterization and detection of novel protein modifications in vitro and in vivo : [kumulative Dissertation]
Author(s): Baldensperger, TimLook up in the Integrated Authority File of the German National Library
Referee(s): Glomb, Marcus A.Look up in the Integrated Authority File of the German National Library
Pischetsrieder, MonikaLook up in the Integrated Authority File of the German National Library
Granting Institution: Martin-Luther-Universität Halle-Wittenberg
Issue Date: 2020
Extent: 1 Online-Ressource (131 Seiten)
Type: HochschulschriftLook up in the Integrated Authority File of the German National Library
Type: Doctoral thesis
Exam Date: 2020-07-21
Language: English
URN: urn:nbn:de:gbv:3:4-1981185920-342875
Abstract: Die enzymatische Acetylierung von Lysinseitenketten ist ein etablierter Mechanismus in der Regulation der Epigenetik und des Metabolismus. Neueste Studien konnten strukturell verwandte nicht-enzymatische Acylierung von Lysin durch reaktive α-Dicarbonyle und Acyl CoA Thioester identifizieren. Das Ziel der vorliegenden Dissertation war die Entwicklung und Validierung einer robusten Analytik, um die Mechanismen und Funktionen dieser neuartigen Lysinacylierungen in Alterungs- und Krankheitsprozessen aufzuklären. Es wurden die Konzepte von oxidativem Stress, Dicarbonylstress und RACS Stress in Modellsystemen kombiniert und Änderungen der posttranslationalen Modifikationen im Alterungsprozess wurden verfolgt sowie Muster identifiziert. Nicht enzymatische Modifikation von Proteinen wurde als möglicher Mechanismus im Alterungsprozess postuliert.
The enzymatic acylation of lysine is a major regulatory mechanism in epigenetics and metabolism. Recent studies discovered structural related non-enzymatic acylation of lysine by highly reactive α-dicarbonyls and acyl-CoA thioesters. The aim of the present thesis was the development and validation of a robust analytical method to elucidate the causes and consequences of these novel acyl lysine modifications in aging and disease. Finally, the concepts of oxidative, dicarbonyl, and RACS stress were combined using model systems and changes of posttranslational modifications in the aging process were monitored and patterns identified. Hence, non enzymatic modification of proteins was suggested as a potential mechanism in hallmarks of aging.
URI: https://opendata.uni-halle.de//handle/1981185920/34287
http://dx.doi.org/10.25673/34092
Open Access: Open access publication
License: In Copyright
Appears in Collections:Interne-Einreichungen

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