Principal Investigator, Head of Biochemistry II
The research focus of Prof. Dr. Mats Paulsson and his team is the structure and functions of extracellular matrix proteins. Their aim is to understand how the extracellular matrix regulates cell function and how functional disorders can lead to the development of disease. The group has identified new building blocks of type VI collagen and now aims to explore in greater depth the interactions between specific extracellular matrix components, cytokines and growth factors.
Our research: Prof. Mats Paulsson and his research group are looking at the structure and functions of extracellular matrix proteins. Their particular interest lies in the regulation of cell function by the extracellular matrix and the way in which functional disorders can lead to disease. At the present time, these scientists are studying how mutations in matrix proteins may trigger hereditary diseases, such as chondrodysplasias and premature osteoarthritis.
Our successes: The team’s greatest recent success has been the identification of three new alpha chains of type VI collagen. Based on these findings, the scientists have developed new structural models of collagen VI, which will contribute to greater understanding of the pathological mechanisms of muscular dystrophies and other diseases.
Our goals: Prof. Paulsson’s team aims to gain in-depth understanding of the interactions between microfibrils in the extracellular matrix, cytokines and growth factors. The researchers are working on evidence that mutations in microfibrillar proteins impact on cytokines and various growth processes.
Our methods/techniques: The Paulsson laboratory makes use of recombinant protein expression and protein characterization in combination with high resolution electron microscopy, small angle X-ray scattering (SAXS), and X-ray crystallography to reveal how microfibrillar proteins are linked and to build improved structural models.
Figure 1: Matrilin-3 expression in a mouse knee joint
Figure 2: Muscle disease causing collagen VI mutations mapped onto the new a3N5 domain structure (Becker et al., Structure 22, 199-208)