摘要
目标:应用毛细管电泳-激光诱导荧光检测(CE-LIF)检测健康人及接受细胞抑制治疗的恶性血液病患者血清和唾液IgA的N-糖基化结构。 背景:体液糖蛋白的N-糖基化改变可以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,在免疫防御潜在的病原体攻击中起重要作用。血清中IgA含量丰富,而分泌型免疫球蛋白A (secretory immunoglobulin A, sIgA)是黏膜表面最常见的蛋白之一,如唾液。 目的:我们的目的是研究血清和唾液中IgA糖基化的变化,作为对恶性血液病患者给予细胞抑制治疗的反应。 方法:采用毛细管电泳-激光诱导荧光检测技术(CE-LIF)分析10例对照组和8例用细胞抑制剂治疗所致轻度口腔黏膜病变的恶性血液病患者的混合血清和唾液中Z(IgA1)部分免疫球蛋白A的N-糖基化谱。 结果:血清和唾液中31种N-聚糖中有8种和38种N-聚糖中有4种与对照组相比差异显著(p<0.05)。唾液中有13种聚糖,而血清中没有,另一方面,血清中有6种结构在唾液中没有。 结论:所开发的Z(IgA1)分割和基于CE-LIF的高分辨率糖基分析方法为检测和监测血清和唾液中IgA糖基化变化提供了高效、灵敏的工作流程,具有广泛的分子药用价值。
关键词: 毛细管电泳,IgA
Current Molecular Medicine
Title:N-glycomic Analysis of Z(IgA1) Partitioned Serum and Salivary Immunoglobulin A by Capillary Electrophoresis
Volume: 20 Issue: 10
关键词: 毛细管电泳,IgA
摘要:
Aims: 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.
Background: 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.
Objective: 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.
Methods: 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.
Results: 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.
Conclusion: 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.
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N-glycomic Analysis of Z(IgA1) Partitioned Serum and Salivary Immunoglobulin A by Capillary Electrophoresis, Current Molecular Medicine 2020; 20 (10) . https://dx.doi.org/10.2174/1566524020666200413114151
DOI https://dx.doi.org/10.2174/1566524020666200413114151 |
Print ISSN 1566-5240 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5666 |
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