Title : Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric
myeloperoxidase : glycosylation is required for optimal enzymatic activity
Abstract :
- The involvement of myeloperoxidase ( MPO ) in various inflammatory conditions has been the scope of many recent studies
- Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known
- Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated
- Analyses showed the presence of five N-glycans at positions 323, 355, 391, 483, 729 in both proteins
- Site by site analysis demonstrated a well conserved micro- and macro-heterogeneity and more complex-type N-glycans for the recombinant form
- Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity
- Data are discussed with regard to biosynthesis and the three-dimensional structure of MPO