NBS-nytt
03.08.2020
Brith Bergum
MSc Brith Bergum at the Broegelmann Research Laboratory, Department of Clinical Science, Faculty of Medicine, University of Bergen, defended her thesis Carbamylation in an inflammatory and uremic environment" for the degree of PhD on the 22nd of January 2020. The work was carried out under the supervision of Professor Piotr Mydel and Professor Roland Jonsson.
Carbamylation of lysine residues and protein N-termini is an ubiquitous, non-enzymatic post-translational modification that can profoundly affect the structure and biological properties of proteins. PTMs have been shown to play pivotal role in triggering autoimmunity and in hemostasis and bleeding disorders. During PhD Brith Bergum showed that antibodies against carbamylated proteins (anti-CarP) are present in patients with primary Sjögren's syndrome and are strongly correlated with disease severity. Anti-CarP antibodies could potentially help identifying patients with more active disease and at risk of developing additional comorbidity. As aggregation and cross-linking of fibrin monomers rely on lysine residues, it is likely that carbamylation impacts fibrinogen processing. Interestingly, platelets exposed to cyanate had reduced adhesion to fibrinogen, and thrombin activated platelet aggregation was altered in vitro and in hemodyliazed patients. Carbamylated fibrinogen was found to alter clot morphology, reduced mechanical stability and an increased resistance to fibrinolysis. The results indicated that carbamylation might play crucial role in abnormal coagulation, leading to increased bleeding and thrombotic complications found in HD patients. In conclusion her results showed detrimental effect of carbamylation on protein functions contributing to adverse effects seen in patients with an inflammatory and uremic environment.
Marte Sneeggen
MSc Erna Irene Heggland at the Sea Lice Research Centre, Department of Biological Sciences, Faculty of Mathematics and Natural Sciences, University of Bergen, defended her thesis Hematophagy in the salmon louse (Lepeophtheirus salmonis). Characterization of genes and proteins involved in parasite blood-feeding" for the degree of PhD on the 13th of February 2020. The work was carried out under the supervision of Professor Frank
Gå til medietCarbamylation of lysine residues and protein N-termini is an ubiquitous, non-enzymatic post-translational modification that can profoundly affect the structure and biological properties of proteins. PTMs have been shown to play pivotal role in triggering autoimmunity and in hemostasis and bleeding disorders. During PhD Brith Bergum showed that antibodies against carbamylated proteins (anti-CarP) are present in patients with primary Sjögren's syndrome and are strongly correlated with disease severity. Anti-CarP antibodies could potentially help identifying patients with more active disease and at risk of developing additional comorbidity. As aggregation and cross-linking of fibrin monomers rely on lysine residues, it is likely that carbamylation impacts fibrinogen processing. Interestingly, platelets exposed to cyanate had reduced adhesion to fibrinogen, and thrombin activated platelet aggregation was altered in vitro and in hemodyliazed patients. Carbamylated fibrinogen was found to alter clot morphology, reduced mechanical stability and an increased resistance to fibrinolysis. The results indicated that carbamylation might play crucial role in abnormal coagulation, leading to increased bleeding and thrombotic complications found in HD patients. In conclusion her results showed detrimental effect of carbamylation on protein functions contributing to adverse effects seen in patients with an inflammatory and uremic environment.
Marte Sneeggen
MSc Erna Irene Heggland at the Sea Lice Research Centre, Department of Biological Sciences, Faculty of Mathematics and Natural Sciences, University of Bergen, defended her thesis Hematophagy in the salmon louse (Lepeophtheirus salmonis). Characterization of genes and proteins involved in parasite blood-feeding" for the degree of PhD on the 13th of February 2020. The work was carried out under the supervision of Professor Frank
