Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity
Autor: | Van Antwerpen, Pierre, Slomianny, Marie-Christine, Zouaoui Boudjeltia, Karim, Delporte, Cédric, Faid, Valegh, Calay, Damien, Rousseau, Alexandre, Moguilevsky, Nicole, Raes, Martine, Vanhamme, Luc, Furtmüller, Paul G, Obinger, Christian, Vanhaeverbeek, Michel, Neve, Jean, Michalski, Jean-Claude |
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Jazyk: | angličtina |
Rok vydání: | 2010 |
Předmět: |
Polysaccharides -- chemistry
Glycosylation Peroxidase -- metabolism Peroxidase -- genetics Neutrophils -- enzymology Polysaccharides -- metabolism CHO Cells Sciences bio-médicales et agricoles Recombinant Proteins carbohydrates (lipids) Cricetulus Cricetinae Polysaccharides -- genetics Animals Humans Protein Multimerization Protein Structure Quaternary Peroxidase -- chemistry |
Zdroj: | The Journal of biological chemistry, 285 (21 |
Popis: | 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. Comparative Study Journal Article Research Support, Non-U.S. Gov't SCOPUS: ar.j info:eu-repo/semantics/published |
Databáze: | OpenAIRE |
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