PD Dr. Daniela G. Seidler


University of Münster
Institute for Physiological Chemistry and Pathobiochemistry
Waldeyerstraße 15
48149 Münster
Germany
 
Email:
Net:
dgseidle@uni-muenster.de
physiolchem.klinikum.uni-muenster.de

The main focus of Dr. Seidlers group, located in the Institute for Physiological Chemistry and Pathobiochemistry at the University of Münster, Germany, is the characterization of the matrix proteoglycan decorin with emphasis on glycosaminoglycan chain biosynthesis, structures and matrix organisation. Glycosaminoglycans are linear polysaccharide chains which are highly sulphated and are involved in growth factor interactions. The glycosaminoglycan chain of decorin is either of chondroitin (CS) or dermatan sulphate (DS) type, depending on the tissue, where the proteoglycan is expressed. For example, decorin contains 80% DS in skin compared to only 20% in cartilage. The importance of the glycosaminoglycan chain of decorin was exemplified by an Ehlers-Danlos syndrome patient with a defect in the biosynthesis of decorin. The patient’s fibroblasts synthesised 50% of decorin without a glycosaminoglycan chain and the remaining glycosaminoglycan chain showed a reduced amount of dermatan sulphate. In addition to cutis laxa the patient suffered from a wound healing deficiency.
CS/DS is synthesized in the Golgi compartment on proteoglycan core proteins and is subsequently secreted into the extracellular matrix or attached to cell surface. One cell concurrently is able to synthesise a CS-proteoglycan and DS-proteoglycan. Many growth factors, chemokines and cytokines that bind to cell surface heparan sulphates also are able to interact with DS, and are thought to act as co-receptors for these ligands. The structure of sulfation and epimerization, meaning the binding motifs of DS that bind FGFs and other cytokines are not known yet. Therefore, our group is interested in the compositional analysis of the DS glycosaminoglycan chains that are required for binding of growth factors, e.g. FGF-1, FGF-7 and FGF-8.


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