Glycosylation of site-specific glycans of α1-acid glycoprotein and alterations in acute and chronic inflammation
Glycosylation of site-specific glycans of α1-acid glycoprotein and alterations in acute and chronic inflammation
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DOI：
10.1016/j.bbagen.2005.03.012
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发表时间：
2005-08-30
影响因子：
3
通讯作者：
Matsumoto, K
中科院分区：
文献类型：
--
作者：
Higai, K;Aoki, Y;Matsumoto, K
背景：α(1)-酸性糖蛋白(AGP)是一种急性时相反应物，在5个ASN连接的糖基化位点广泛糖基化。在许多病理生理状态中，包括炎症、类风湿性关节炎和癌症，已有报道ASN连接的多糖(N-聚糖)的改变。我们研究了急、慢性炎症患者血清AGP各糖基化位点N-糖链的变化。方法：用Glu-C消化血清中纯化的AGP，用反相高效液相色谱法分离释放的糖肽。用基质辅助激光解吸电离飞行时间质谱仪分析N-糖苷酶处理后释放的N-糖链。结果：N-糖基化1、3、4和5位点在分支结构上存在部位差异。急性炎症患者血清中，双触角增加，三触角和四触角结构减少，α1，3-岩藻糖基化增加，大多数糖基化位点。在慢性炎症患者血清中，检测到3和4位的三触角α1，3-岩藻糖基化和3、4和5位的四触角α1，3-岩藻糖化的比率增加。虽然急性和慢性血清的定点定向分支结构无显著差异，但在2、4、5位的三触角和3、4位的四触角有显著差异。结论：正常人AGP糖基化位点的N-糖链组成变化不大，而急性炎症患者血清中每个糖基化位点的双前房和α1，3-岩藻糖化N-糖基化结构的数目明显增加。(C)2005 Elsevier B.V.保留所有权利。
Background: alpha(1)-Acid glycoprotein (AGP), an acute phase reactant, is extensively glycosylated at five Asn-linked glycosylation sites. In a number of pathophysiological states, including inflammation, rheumatoid arthritis, and cancer, alterations of Asn-linked glycans (N-glycans) have been reported. We investigated alteration of N-glycans at each of glycosylation sites of AGP in the sera of patients with acute and chronic inflammation.Methods: AGP purified from sera was digested with Glu-C and the liberated glycopeptides were isolated by reverse phase HPLC. N-glycans released with peptide N-glycosidase F and followed by neuraminidase treatment were analyzed by matrix-assisted laser desorption ionization-time of flight mass spectrometry.Results: Site-specific differences in branching structures were observed among N-glycosylation sites 1, 3, 4 and 5. Within the sera of patients with acute inflammation, increases in bi-antennary and decreases in tri- and tetra-antennary structures, were observed, as well as increases in alpha 1,3-fucosylation, at most glycosylation sites. In the sera of patients with chronic inflammation, increased rates of tri-antennary alpha 1,3-fucosylation at sites 3 and 4 and tetra-antennary alpha 1,3-fucosylation at sites 3, 4 and 5 were detected. Although there were no significant differences between acute and chronic sera in site directed branching structures, significant differences of alpha 1,3-fucosylation were detected in tri-antennary at sites 2, 4 and 5 and in tetra-antennary at sites 3 and 4.Conclusion: Little variation in the N-glycan composition of the glycosylation sites of AGP was observed among healthy individuals, while the sera of patients with acute inflammation demonstrated increased numbers of bi-antermary and alpha 1,3-fucosylated N-glycan structures at each glycosylation site. (c) 2005 Elsevier B.V. All rights reserved.