The primary focus is to develop new and efficient quantitative mass spectrometric and affinity chromatographic strategies for the characterization of posttranslational modifications of proteins from highly complex mixtures and apply these strategies to the study of clinical relevant samples. Furthermore we aim to develop selected reaction monitoring mass spectrometry-based assays to validate and quantify several candidate proteins simultaneusly.
Novel metastasis-associated markers are identified using quantitative proteomic analysis. One project focuses on identifying novel cell surface proteins that are expressed differently on metastasizing compared to non-metastasizing breast cancer cells. These proteins may influence the ability of breast cancer cells to metastasize and could have utility as therapeutic targets. Proteins are identified by membrane purification, labeling and quantitative mass spectrometry analysis. A large panel of candidate proteins have been identified and the clinical relevance of these cell surface markers is evaluated using large panels of tissue biopsies from breast cancer patients with well-characterized medical histories and follow-up. In other studies surface markers associated with breast cancer stem cells are identified, as there is a paucity of such markers. Finally, we are studying posttranslational modifications, such as phosphorylations and glycosylations, to identify altered expression between metastasizing vs. non-metastasizing cells and in breast cancer cells that exhibit resistance to endocrine treatment.
Discovery and targeted characterization of mitochondrial phosphoproteins are used to stydy the pathogenesis of insulin resistance in skeletal muscle and adipose tissue of patients with type 2 diabetes using mass spectrometry based quantitative phosphoproteomics. Mass spectrometry based characterization of skeletal muscle proteome, mitoproteome, phosphoproteome, and phosphotyrosine proteome, and quantitative studies in individuals with insulin resistance.
Our projects are aimed at determining quantitative and qualitative changes in the proteinaceous components of arterial tissue in different disease situations. We use material from a large biobank, which contains human arterial tissue removed at different operations at Odense University Hospital. The primary focus is on alterations in the arterial proteome in relation to diabetes, gender, smoking and uremia. Knowledge about protein changes in the arterial proteome in relation to specific risk factors, will improve our basic understanding of arterial diseases and point out new treatment targets.
Different diseases are associated with specific changes in the plasma or urine proteome. Using a MS-based approach, we are searching to identify such specific alterations in the protein content, to identify new markers for clinical important conditions. Our interest is mainly cardiovascular diseases.