Institute for Genetics, Faculty of Math. Nat. Sciences
Prof. Dr. Marcus Krüger
Principal Investigator, Institute for Genetics
Prof. Dr. Marcus Krüger and his team are using quantitative high-resolution mass spectrometry to analyze protein changes in various disease models. Their aim is to identify novel disease-related pathways and to identify biomarkers as targets for therapeutic approaches. They use stable isotope labeling of amino acids in cell culture (SILAC) and in living animals to investigate protein dynamics under normal and disturbed conditions.
Our research: The proteome, the whole set of proteins in a cell, cannot be deduced entirely from the genome. For example, post-translational modifications (PTMs) are important for the dynamic regulation of protein activity, translocation, and stability. Moreover, PTMs are critical for signaling pathways and the deregulation of modifying enzymes often leads to diseases, such as cancer and type 2 diabetes mellitus. Prof. Krüger and his research group are applying large-scale quantitative proteomics to investigate signal transduction pathways in various mouse models.
Our successes: The Krüger group is involved in transferring the SILAC technology to various model organisms, including worms, zebra fish, and rodents. This allows them to determine protein concentrations and protein turnover in living animals using mass spectrometry (LC-MS/MS).
Our goals: The group is aiming to identify protein and PTM profiles in living model organisms with relevance to human diseases. With long-term goals of developing new treatment methods, these scientists intend to use the profiles as targets for new therapeutic agents. In personalized medicine of the future, unbiased proteome analysis will be employed in addition to genome-wide strategies for the individual treatment of human patients.
Our methods/techniques: The Krüger laboratory uses SILAC labeling of model organisms to quantify proteins and regulatory PTMs accurately. The group uses the enrichment of PTMs, such as phosphorylation and acetylation, via affinity- and antibody-based methods.
Figure 1: Schematic workflow of a generic shotgun approach. Proteins from biological samples were extracted and digested with proteases. The analysis with liquid chromatography (LC) and mass spectrometry (MS) then results in large data sets of MS and tandem mass spectrometry (MS/MS) data containing quantitative peptide information.