The glyoxalase system in the functional genomic era ...
Glycation is a major cause of spontaneous damage to cellular and extracellular proteins in physiological systems. Protein glycation by glucose occurs by reaction with N-terminal and lysyl side chain amino groups .There are also reactive dicarbonyl metabolites in physiological systems such as methylglyoxal (MG). MG is formed by the spontaneous degradation of triosephosphates. MG and other dicarbonyls modify proteins to form advanced glycation endproduct (AGE) with a 200-50 000-fold higher reactivity than glucose. The enzymatic defence against glycation involves several enzymes such as glyoxalases and aldo-keto reduktases. The decline of expression of enzymes of the enzymatic defence against glycation may be key to increased protein glycation in different diseases such as diabetes and the aging phenotype. Prof. Paul Thornally is head of the Protein Damage and Systems Biology Research Group, Division of Metabolic & Vascular Health, Warwick Medical School, University of Warwick, UK. He is called the father of "Glyoxalases". For more information see at: Glyoxalase on Facebook: Glyoxalase on YouTube: History, Regulation, Protein/nucleotide damage Diese Veranstaltung wird von der SLÄK mit 2 Fortbildungspunkten bewertet.
- Prof. Paul J. Thornalley
- Prof. Dr. Gerd Birkenmeier