Horvath Csaba Memorial Laboratory of Bioseparation Sciences, Research Center for Molecular Medicine, Doctoral School for Medicine, Faculty of Medicine, University of Debrecen, Hungary.
Department of Dentoalveolar Surgery and Dental Outpatient Care, Faculty of Dentistry, University of Debrecen, Debrecen, Hungary.
Curr Mol Med. 2020;20(10):781-788. doi: 10.2174/1566524020666200413114151.
Application of capillary electrophoresis with laser induced fluorescence detection (CE-LIF) to identify the N-glycosylation structures of serum and saliva IgA from healthy controls and patients with malignant hematological diseases having cytostatic treatment induced mild oral mucosal lesions.
Altered N-glycosylation of body fluid glycoproteins can be an effective indicator of most inflammatory processes. Immunoglobulin A (IgA) is the second highest abundant immunoglobulin and has a major role in the immune-defense against potential pathogen attacks. While IgA is abundant in serum, secretory immunoglobulin A (sIgA) is one of the most prevalent proteins in mucosal surfaces, such as in saliva.
Our aim was to investigate the changes of IgA glycosylation in serum and saliva as a response to an administered cytostatic treatment in patients with malignant hematological disorders.
Capillary electrophoresis with laser induced fluorescent detection (CE-LIF) was used to analyze the N-glycosylation profiles of Z(IgA1) partitioned immunoglobulin A in pooled serum and saliva of 10 control subjects and 8 patients with malignant hematological diseases having cytostatic treatment induced mild oral mucosal lesions.
Eight of 31 and four of 38 N-glycans in serum and saliva, respectively, showed significant (p<0.05) differences upon comparison to the control group. Thirteen glycans were present in the saliva but not in the serum, on the other hand, six structures were found in the serum samples not present in the saliva.
The developed Z(IgA1) partitioning and the high resolution CE-LIF based glyocoanalytical methods provided an efficient and sensitive workflow to detect and monitor IgA glycosylation alterations in serum and saliva with the scope for widespread molecular medicinal use.
应用毛细管电泳激光诱导荧光检测（CE-LIF）来鉴定健康对照者和接受细胞毒性治疗引起轻度口腔黏膜炎的恶性血液病患者的血清和唾液 IgA 的 N-糖基化结构。
体液糖蛋白的 N-糖基化改变可能是大多数炎症过程的有效指标。免疫球蛋白 A（IgA）是第二丰富的免疫球蛋白，在针对潜在病原体攻击的免疫防御中起主要作用。虽然 IgA 在血清中含量丰富，但分泌型免疫球蛋白 A（sIgA）是黏膜表面（如唾液）中最常见的蛋白质之一。
我们的目的是研究恶性血液病患者接受细胞毒性治疗后，IgA 糖基化在血清和唾液中的变化。
使用毛细管电泳激光诱导荧光检测（CE-LIF）分析了 10 名健康对照者和 8 名接受细胞毒性治疗引起轻度口腔黏膜炎的恶性血液病患者的混合血清和唾液中 Z（IgA1）分区免疫球蛋白 A 的 N-糖基化谱。
与对照组相比，血清和唾液中的 31 个和 38 个 N-聚糖中，有 8 个和 4 个分别有显著差异（p<0.05）。有 13 个糖基在唾液中存在而在血清中不存在，另一方面，有 6 个结构在血清样本中存在而不在唾液中存在。
所开发的 Z（IgA1）分区和基于高分辨率 CE-LIF 的糖分析方法提供了一种高效灵敏的工作流程，用于检测和监测血清和唾液中的 IgA 糖基化改变，具有广泛的分子医学用途。
