成熟二聚体白细胞和重组单体髓过氧化物酶的糖基化模式：糖基化是获得最佳酶活性所必需的。
Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
机构信息
Laboratory of Pharmaceutical Chemistry and the Analytical Platform of Institute of Pharmacy, UniversitéLibre de Bruxelles, Brussels, Belgium.
出版信息
J Biol Chem. 2010 May 21;285(21):16351-9. doi: 10.1074/jbc.M109.089748. Epub 2010 Mar 23.
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.
摘要
髓过氧化物酶 (MPO) 在各种炎症条件下的参与一直是许多最近研究的范围。除了其研究充分的催化活性外，其整体结构和糖基化模式在生物学功能中的作用几乎未知。在这里，研究了从中性粒细胞中纯化的天然二聚体人 MPO 和在中国仓鼠卵巢细胞中重组表达的单体 MPO 的 N-聚糖组成。分析表明，两种蛋白质在位置 323、355、391、483、729 处均存在 5 种 N-聚糖。逐个位点的分析表明，重组形式的 N-聚糖具有更好的保守性和微观与宏观不均一性，并且具有更复杂的类型。对糖基化和去糖基化重组 MPO 的生物学功能的比较表明，糖基化对于最佳酶活性是必需的。数据是关于 MPO 的生物合成和三维结构进行讨论的。
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