TY - JOUR
T1 - Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase
T2 - Glycosylation is required for optimal enzymatic activity
AU - Van Antwerpen, P.
AU - Slomianny, M.-C.
AU - Boudjeltia, K.Z.
AU - Delporte, C.
AU - Faid, V.
AU - Calay, D.
AU - Rousseau, A.
AU - Moguilevsky, N.
AU - Raes, Martine
AU - Vanhamme, L.
AU - Furtmüller, P.G.
AU - Obinger, C.
AU - Vanhaeverbeek, M.
AU - Nève, J.
AU - Michalski, J.-C.
N1 - MEDLINE® is the source for the MeSH terms of this document.
PY - 2010/5/21
Y1 - 2010/5/21
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77952397954&partnerID=8YFLogxK
U2 - 10.1074/jbc.M109.089748
DO - 10.1074/jbc.M109.089748
M3 - Article
AN - SCOPUS:77952397954
SN - 0021-9258
VL - 285
SP - 16351
EP - 16359
JO - The Journal of Biological Chemistry
JF - The Journal of Biological Chemistry
IS - 21
ER -