Research: Biochemistry and Molecular Biology

Molecular Mechanism of RAGE Ligand Recognition:
The Receptor for Advanced Glycation Endproducts (RAGE) is a pattern recognizing cell surface protein and interacts with multiple ligands, including advanced glycation endproducts, protein amyloids and S100 proteins. We are investigating the recognition of S100 proteins by RAGE on the molecular level. We use biophysical and genetic engineering methods to define RAGE - S100 binding interfaces and develope probes to modulate RAGE/S100 interactions.

Role of RAGE/S100 in Cellular Signaling:
RAGE emerges as a major receptor for secreted S100 proteins and many effects of extracellular S100 proteins are RAGE dependent. More than half of the 21 currently known S100 proteins interact with RAGE and trigger specific cellular responses that can vary between cell types. We are interested in defining the role of RAGE on the auto- and paracrine activity of S100 proteins screted by melamona cell. We have developed epitope specific antibodies to probe RAGE / S100 signaling in cell based assays.

Protein Dephosphorylation:
Protein phosphorylation is a major mechanism of signal transduction in eukaryotic cells. Some bacterial and viral human pathogens encode protein phosphatases in their genomes and seem to use these to overcome defense mechanisms of host cells. We are interested in defining structural and functional differences between eukaryotic and prokaryotic protein phosphatases.

Teaching
BCH 3034 ­ Biochemistry II

Selected Publications
See Group Home Page

Group Home Page
www.science.fau.edu/chemistry/svetter/