Inter-tissue glycan heterogeneity: site-specific glycoform analysis of mouse tissue N-glycoproteomes using MS1-based glycopeptide detection method assisted by lectin microarray.

IF 3.8 2区 化学 Q1 BIOCHEMICAL RESEARCH METHODS
Chiaki Nagai-Okatani, Azusa Tomioka, Daisuke Tominaga, Hiroaki Sakaue, Atsushi Kuno, Hiroyuki Kaji
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引用次数: 0

Abstract

To understand the biological and pathological functions of protein glycosylation, the glycan heterogeneities for each glycosite in a single glycoprotein need to be elucidated depending on the type and status of cells. For this aim, a reliable strategy is needed to compare site-specific glycoforms of multiple glycoprotein samples in a comprehensive manner. To analyze this "inter-heterogeneity" of samples, we previously introduced an MS1-based glycopeptide detection method, "Glyco-RIDGE." Here, to elucidate inter-tissue glycan heterogeneities, this estimation method was applied to site-specific N-glycoforms of glycoproteins from six normal mouse tissues (liver, kidney, spleen, pancreas, stomach, and testis). The analyses of desialylated glycopeptides estimated 11,325 site-specific N-glycoforms with 239 glycan compositions at 1260 sites (1122 non-redundant core peptides) in 800 glycoproteins, revealing inter-tissue differences in macro-, micro-, and meta-glycan heterogeneities. To obtain detailed information on their glycan features and tissue distribution, the Glyco-RIDGE results were compared with laser microdissection-assisted lectin microarray (LMD-LMA)-based mouse tissue glycome mapping data deposited on LM-GlycomeAtlas, as well as MS-based mouse tissue glycome data deposited on GlycomeAtlas. This integrated approach supported the certainty of Glyco-RIDGE results and suggested that inter-tissue differences exist in glycan motifs, such as alpha-galactose and bisecting N-acetylglucosamine, in both whole tissue glycomes and specific glycoproteins, Anpep and Lamc1. In addition, the comparison with LMD-LMA-based tissue glycome mapping data suggested the possibility of estimating the tissue distribution of the assigned glycans and glycopeptides. Taken together, these findings demonstrate the utility of an integrated approach using MS assisted by LMA for large-scale analyses.

为了了解蛋白质糖基化的生物学和病理学功能,需要根据细胞的类型和状态阐明单个糖蛋白中每个糖基复合体的糖异质性。为此,需要一种可靠的策略来全面比较多个糖蛋白样本中特定位点的糖型。为了分析样本的这种 "异质性",我们之前推出了一种基于 MS1 的糖肽检测方法--"Glyco-RIDGE"。在此,为了阐明组织间糖的异质性,我们将这种估算方法应用于六种正常小鼠组织(肝脏、肾脏、脾脏、胰腺、胃和睾丸)中糖蛋白的特定位点 N-糖共聚形式。通过对去氨酰化糖肽的分析,在 800 个糖蛋白的 1260 个位点(1122 个非冗余核心肽)上估算出了 11,325 个位点特异性 N-糖链,239 个糖链组成,揭示了组织间在大聚糖、微聚糖和元聚糖异质性上的差异。为了获得有关糖蛋白特征和组织分布的详细信息,Glyco-RIDGE 的结果与保存在 LM-GlycomeAtlas 上的基于激光显微切割辅助凝集素芯片(LMD-LMA)的小鼠组织糖蛋白图谱数据以及保存在 GlycomeAtlas 上的基于 MS 的小鼠组织糖蛋白数据进行了比较。这种综合方法支持了 Glyco-RIDGE 结果的确定性,并表明在整个组织糖蛋白和特定糖蛋白(Anpep 和 Lamc1)中,α-半乳糖和双链 N-乙酰葡糖胺等糖基团存在组织间差异。此外,与基于 LMD-LMA 的组织糖粒图谱数据的比较表明,有可能估算出所分配的聚糖和糖肽的组织分布。总之,这些研究结果证明了在 LMA 的辅助下使用 MS 进行大规模分析的综合方法的实用性。
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来源期刊
CiteScore
8.00
自引率
4.70%
发文量
638
审稿时长
2.1 months
期刊介绍: Analytical and Bioanalytical Chemistry’s mission is the rapid publication of excellent and high-impact research articles on fundamental and applied topics of analytical and bioanalytical measurement science. Its scope is broad, and ranges from novel measurement platforms and their characterization to multidisciplinary approaches that effectively address important scientific problems. The Editors encourage submissions presenting innovative analytical research in concept, instrumentation, methods, and/or applications, including: mass spectrometry, spectroscopy, and electroanalysis; advanced separations; analytical strategies in “-omics” and imaging, bioanalysis, and sampling; miniaturized devices, medical diagnostics, sensors; analytical characterization of nano- and biomaterials; chemometrics and advanced data analysis.
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