Previous studies have shown that differential glycosylation of antibodies can influence their immune response. If the galactose residue is lacking in the carbohydrate chain, in this case called G0-IgG antibodies, it is more likely to have a pro-inflammatory immune response and higher disease severity in various autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus. On the other hand, galactolysed and sialylated antibodies correlate with anti-inflammatory effects in rheumatoid arthritis.

Although little is known about the formation and regulation of differentially glycosylated IgG antibodies, two enzymes that appear to influence the glycosylation of the antibodies have been identified the glycosyl-transferases B4GALT1 and ST6GAL1. These two enzymes are differentially expressed in B cells. The signaling pathways of the expression of these two glycosyl-transferases have not been investigated in detail yet.

Therefore, the aim of this project is to elucidate the signal transduction of the expression of the glycosyltransferases B4GALT1 and ST6GAL1 in activated B cells and plasma cells.