Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
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Van Antwerpen P, Slomianny MC, Boudjeltia KZ, Delporte C, Faid V, Calay D, Rousseau A, Moguilevsky N, Raes M, Vanhamme L, Furtmuller PG, Obinger C, Vanhaeverbeek M, Neve J, Michalski JC
Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
J Biol Chem. 2010 May 21;285(21):16351-9. doi: 10.1074/jbc.M109.089748. Epub 2010 Mar 23.
- PubMed ID
- 20332087 [ View in PubMed]
- 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.