senior lecturer , head of department
Supervisor: FAUST, Zsuzsanna
Co-supervisor: Dr. NAGY, Tamás
It is well known that intracellular signaling mechanisms aprticipating in the malignant transformation of the cell. For example the mutant protein coded by the fusion gen bcr-abl is an activated tyrosin-kinase which results in increased phosphorylation on many signaling protein. Despite the recognition of protein O-Glycosylation as a signaling mechanism is a more recent event, it seems to be more and more obvious that it plays a significant role in the development of malignant diseases. During O-Glycosylation, a single N-acetyl-glucosamine molecule is linked to the Ser/Thr residues of proteins. This process can be reversible, can be competing with phosphorylation for the same Ser/Thr sites and occurs on a large scale of various types of proteins. E.g. the proto-oncogen c-myc or the tumor-supressor p53 can both be O-Glycosylated. Interestingly, the cells’ carbohydrate metabolism is associated (in both direction) with O-Glycosylation. Influencing O-Glycosylation (by specific drugs) can impact the glucose uptake of the cells and could be exploited as therapeutic target in malignant diseases.
In this research, our aim is to study the level of protein O-Glycosylation in various malignant hematologic diseases. Characterizing O-GlcNAc levels could be a useful diagnostic marker, but also the basis for developing new therapies.