Altered glycosylation of α1-acid glycoprotein in patients with inflammation and diabetes mellitus
Altered glycosylation of α1-acid glycoprotein in patients with inflammation and diabetes mellitus
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DOI：
10.1016/s0009-8981(02)00427-8
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发表时间：
2003-03-01
影响因子：
5
通讯作者：
Matsumoto, K
中科院分区：
文献类型：
--
作者：
Higai, K;Azuma, Y;Matsumoto, K
背景资料：在某些病理生理条件下，如炎症类风湿性关节炎和糖尿病（DM），急性期蛋白α（1）-酸性糖蛋白（AGP）的天冬酰胺连接聚糖（N-聚糖）模式的改变已被报道。在这项研究中，我们研究了从急性炎症患者（n = 5），2型糖尿病（n = 5）和健康个体（n = 5）的血清中纯化的AGP的N-聚糖结构。方法：用肽N-糖苷酶F（PNGase F）从变性AGP中释放N-聚糖，用纤维素柱纯化。通过基质辅助激光解吸电离飞行时间质谱（MALDI-TOFMS）结合外切糖苷酶消化分析N-聚糖。结果如下：我们发现炎症患者的双触角复合聚糖和α 1 -3岩藻糖基化双、三和四触角聚糖增加，三触角聚糖减少。这些结果支持与伴刀豆球蛋白A（ConA）和橙黄粉虱凝集素（AALs）结合的增加。在糖尿病患者中，AGP的N-聚糖模式的发病机制特异性变化不显著。结论：MALDI-TOFMS方法灵敏度高，适用于临床样品中N-聚糖的分析。(C)2003 Elsevier Science B. V.保留所有权利。
Background: In certain pathophysiological conditions, such as inflammation rheumatoid arthritis and diabetes mellitus (DM), alterations in asparagine-linked glycan (N-glycan) patterns of the acute-phase protein, alpha(1)-acid glycoprotein (AGP), have been reported. In this study, we investigated N-glycan structures of AGP purified from the sera of patients with acute inflammation (n = 5), type 2 diabetes mellitus (n = 5), and healthy individuals (n = 5). Methods: N-Glycans were released with peptide N-glycosidase F (PNGase F) from denatured AGP and purified with cellulose cartridge. N-glycans were analyzed by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOFMS) in combination with exoglycosidase digestion. Results: We revealed increases in bi-antennary complex glycans and in alpha1-3 fucosylated bi-, tri-, and tetra-antennary glycans and a decrease in tri-antennary glycans in inflammation patients. These results support increases in bindings to concanavalin A (ConA) and Aleuria aurantia lectins (AALs). In diabetic patients, the pathogenesis-specific change in N-glycan patterns of AGP was not significant. Conclusions: The MALDI-TOFMS method is sensitive and suitable for profiling analysis of N-glycans in clinical samples. (C) 2003 Elsevier Science B.V. All rights reserved.