Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Maarten Swart

DPhil Student

The role of sulfatase-2 (a heparan sulfate proteoglycan modifying enzyme) in regulating immune function.

The effect of cytokines, chemokines and growth factors on immune cells is fine-tuned by their interactions with heparan sulfate (HS) proteoglycans (PG), which can bind over 400 different proteins. Binding to HS can establish gradients, protect proteins from proteolysis, fine-tune their bioactivity (e. g. by chemokine oligomerization) and influence receptor binding. HSPGs are composed of a core protein that carries one or more linear, covalently-attached HS polysaccharide side chain, consisting of N-acetylglucosamine (GlcNAc) and hexuronic acid disaccharide repeats. These HS side chains are extensively modified by N-, 2-O, 3-O and 6-O sulfation, enabling proteins to bind to HS through their positively charged amino acids (Arg and Lys). 6-O sulfation is the only sulfation pattern that can be post-synthetically fine-tuned by the extracellular sulfatase SULF2 that removes 6-O sulfate groups. This indicates that SULF2 is important for the for the regulation of the bioactivity of mediators that bind to HS. I aimed to study if SULF2 affects inflammation in rheumatoid arthritis and which cell types/ mediators are involved.