Glycosylation Pattern of Mature Dimeric Leukocyte and Recombinant Monomeric Myeloperoxidase
| Autor: | Martine Raes, Jean Nève, Jean-Claude Michalski, Nicole Moguilevsky, Pierre Van Antwerpen, Cédric Delporte, Damien Calay, Valegh Faid, Marie-Christine Slomianny, Alexandre Rousseau, Luc Vanhamme, Karim Zouaoui Boudjeltia, Michel Vanhaeverbeek, Christian Obinger, Paul G. Furtmüller |
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| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
Glycosylation biology Chinese hamster ovary cell Cell Biology biology.organism_classification Biochemistry Molecular biology law.invention carbohydrates (lipids) chemistry.chemical_compound Enzyme Biosynthesis chemistry law Myeloperoxidase biology.protein Recombinant DNA Cricetulus Molecular Biology Peroxidase |
| Zdroj: | Journal of Biological Chemistry. 285:16351-16359 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m109.089748 |
| 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. |
| Databáze: | OpenAIRE |
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