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

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ANALYTICAL AND BIOANALYTICAL CHEMISTRY 2025年第5期417卷 973-988页

作者： Nagai-Okatani, Chiaki Tomioka, Azusa Tominaga, Daisuke Sakaue, Hiroaki Kuno, Atsushi Kaji, Hiroyuki Natl Inst Adv Ind Sci & Technol Cellular & Mol Biotechnol Res Inst Mol & Cellular Glycoprote Res Grp Tsukuba Ibaraki 3058565 Japan Nagoya Univ Inst Glycocore Res iGCORE Furo Cho Nagoya Aichi 4648601 Japan

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.

关键词： Glycoproteomics Site-specific glycoform Glycan heterogeneity Mass spectrometry Tissue glycome mapping lectin microarray

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Glycomic profiling of parathyroid neoplasms via lectin microarray analysis

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ENDOCRINE 2025年第3期87卷 1224-1234页

作者： Zheng, Qingyuan Cui, Ming Xiao, Jinheng Yang, Sen Chen, Tianqi Shi, Yanan Hu, Ya Liao, Quan Chinese Acad Med Sci & Peking Union Med Coll Peking Union Med Coll Hosp Dept Gen Surg State Key Lab Complex Severe & Rare Dis Beijing Peoples R China Chinese Acad Med Sci & Peking Union Med Coll Peking Union Med Coll Hosp Inst Clin Med Biomed EngnFac Natl Infrastruct Translat Med Beijing Peoples R China

PurposeParathyroid carcinoma (PC) is a rare malignancy with a poor prognosis. Diagnosis of PC is often difficult in clinical practice and efficient diagnostic markers are still needed for differential diagnosis. Aberrant glycosylations of glycoproteins were identified with lectin microarray in various cancers, while relevant information is lacking in PC. MethodsIn this study, 8 PC and 6 parathyroid adenoma (PA) tissues were assessed using a microarray consisting of 70 lectins. Overall lectin-specific glycosylation patterns were compared between PA and PC tissues. lectins with significant differential response between PC and PA were further validated by lectin histochemistry. ResultsThe difference in signal intensities was found in 71.4% (50/70) of the lectins between the two groups (P < 0.05). The vast majority of PCs had higher intensity signals than PAs (PCs vs. PAs, ratio >1) and amaranthus caudatus (ACL) showed the most significantly different response between them (ratio = 2.45). lectin histochemistry further confirmed higher ACL intensity in PCs than in PAs. The differentially expressed glycans in PC tissues were primarily glucose, mannose, and galactose-based. ConclusionPC presented unique glycomic features and ACL may serve as a candidate diagnostic marker for PC.

关键词： Parathyroid carcinoma Parathyroid tumor Glycosylation lectin microarray Biomarker

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lectin microarray based glycan profiling of exosomes for dynamic monitoring of colorectal cancer progression

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ANALYTICA CHIMICA ACTA 2024年 1316卷 342819页

作者： Sun, Xudong Chen, Bowen Shan, Yongjie Jian, Minghong Wang, Zhenxin Chinese Acad Sci Changchun Inst Appl Chem State Key Lab Electroanalyt Chem Changchun 130022 Peoples R China Univ Sci & Technol China Sch Appl Chem & Engn Hefei 230026 Peoples R China First Hosp Jilin Univ Gen Surg Ctr Dept Thyroid Surg Changchun 130021 Peoples R China Chinese Acad Sci Changchun Inst Appl Chem Natl Analyt Res Ctr Electrochem & Spect Changchun 130022 Peoples R China Chinese Acad Sci Changchun Inst Appl Chem 5625 Ren Min St Changchun 130022 Peoples R China

Background: Exosomes, as emerging biomarkers in liquid biopsies in recent years, offer profound insights into cancer diagnostics due to their unique molecular signatures. The glycosylation profiles of exosomes have emerged as potential biomarkers, offering a novel and less invasive method for cancer diagnosis and monitoring. Colorectal cancer (CRC) represents a substantial global health challenge and burden. Thus there is a great need for the aberrant glycosylation patterns on the surface of CRC cell -derived exosomes, proposing them as potential biomarkers for tumor characterization. Results: The interactions of 27 lectins with exosomes from three CRC cell lines (SW480, SW620, HCT116) and one normal colon epithelial cell line (NCM460) have been analyzed by the lectin microarray. The result indicates that Ulex Europaeus Agglutinin I (UEA-I) exhibits high affinity and specificity towards exosomes derived from SW480 cells. The expression of glycosylation related genes within cells has been analyzed by high -throughput quantitative polymerase chain reaction (HT-qPCR). The experimental result of HT-qPCR is consistent with that of lectin microarray. Moreover, the limit of detection (LOD) of UEA-I microarray is calculated to be as low as 2.7 x 10 5 extracellular vehicles (EVs) mL -1 (three times standard deviation (3 sigma) of blank sample). The UEA-I microarray has been successfully utilized to dynamically monitor the progression of tumors in mice -bearing SW480 CRC subtype, applicable in tumor sizes ranging from 2 mm to 20 mm in diameter. Significance: The results reveal that glycan expression pattern of exosome is linked to specific CRC subtypes, and regulated by glycosyltransferase and glycosidase genes of mother cells. Our findings illuminate the potential of glycosylation molecules on the surface of exosomes as reliable biomarkers for diagnosis of tumor at early stage and monitoring of cancer progression.

关键词： lectin microarray Glycosylation Exosome Colorectal cancer

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Use of lectin microarray to differentiate gastric cancer from gastric ulcer

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World Journal of Gastroenterology 2014年第18期20卷 5474-5482页

作者： Wei-Li Huang Yang-Guang Li Yong-Chen Lv Xiao-Hui Guan Hui-Fan Ji Bao-Rong Chi Department of Hepatology the First Clinic Hospital of Jilin University Department of Gastroenterology Affiliated Hospital of Beihua University Laboratory of Medicinal Chemical Biology College of Life SciencesNankai University Department of General Surgery the Central Hospital of Jilin City

AIM: To investigate the feasibility of lectin microarray for differentiating gastric cancer from gastric ulcer. METHODS: Twenty cases of human gastric cancer tissue and 20 cases of human gastric ulcer tissue were collected and processed. Protein was extracted from the frozen tissues and stored. The lectins were dissolved in buffer, and the sugar-binding specificities of lectins and the layout of the lectin microarray were summarized. The median of the effective data points for each lectin was globally normalized to the sum of medians of all effective data points for each lectin in one block. Formalin-fixed paraffin-embedded gastric cancer tissues and their corresponding gastric ulcer tissues were subjected to Ag retrieval. Biotinylated lectin was used as the primary antibody and HRP-streptavidin as the secondary antibody. The glycopatterns of glycoprotein in gastric cancer and gastric ulcer specimens were determined by lectin microarray, and then validated by lectin histochemistry. Data are presented as mean +/- SD for the indicated number of independent experiments. RESULTS: The glycosylation level of gastric cancer was significantly higher than that in ulcer. In gastric cancer, most of the lectin binders showed positive signals and the intensity of the signals was stronger, whereas the opposite was the case for ulcers. Significant differences in the pathological score of the two lectins were apparent between ulcer and gastric cancer tissues using the same lectin. For MPL and VVA, all types of gastric cancer detected showed stronger staining and a higher positive rate in comparison with ulcer, especially in the case of signet ring cell carcinoma and intra-mucosal carcinoma. GalNAc bound to MPL showed a significant increase. A statistically significant association between MPL and gastric cancer was observed. As with MPL, there were significant differences in VVA staining between gastric cancer and ulcer. CONCLUSION: lectin microarray can differentiate the different

关键词： Gastric cancer Gastric ulcer lectin microarray lectin histochemistry Differentiate

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lectin microarray analysis of isolated polysaccharides from Sasa veitchii

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BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 2017年第9期81卷 1687-1689页

作者： Yagi, Hirokazu Tateno, Hiroaki Hayashi, Kyoko Hayashi, Toshimitsu Takahashi, Katsuhiko Hirabayashi, Jun Kato, Koichi Tsuboi, Masamichi Nagoya City Univ Grad Sch Pharmaceut Sci Nagoya Aichi Japan Natl Inst Adv Ind Sci & Technol Biotechnol Res Inst Drug Discovery BRD Tsukuba Ibaraki Japan Chubu Univ Inst Life & Hlth Sci Kasugai Aichi Japan Hoshi Univ Inst Med Chem Tokyo Japan Natl Inst Nat Sci Inst Mol Sci Okazaki Aichi Japan Natl Inst Nat Sci Okazaki Inst Integrat Biosci Okazaki Aichi Japan Univ Tokyo Grad Sch Pharmaceut Sci Tokyo Japan

We report lectin microarray profile of the polysaccharide fraction derived from Sasa veitchii leaf that exhibits anti-influenza activity. This fraction showed higher reactivities with lectins known as binders to oligo-mannose, fucose, or galactose. Our findings along with previously reported monosaccharide components suggest that the polysaccharide can be cross-reactive with cell surface receptors involved in immune system, thereby exerting anti-influenza activity.

关键词： lectin microarray polysaccharides Sasa veitchii anti-influenza virus activity

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lectin microarray analyses reveal host cell-specific glycan profiles of the hemagglutinins of influenza A viruses

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VIROLOGY 2019年 527卷 132-140页

作者： Hiono, Takahiro Matsuda, Atsushi Wagatsuma, Takanori Okamatsu, Masatoshi Sakoda, Yoshihiro Kuno, Atsushi Natl Inst Adv Ind Sci & Technol Biotechnol Res Inst Drug Discovery Glycosci & Glycotechnol Res Grp Tsukuba Ibaraki 3058568 Japan Keio Univ Sch Med Dept Biochem Shinjuku Ku Tokyo 1608582 Japan Japan Bioind Assoc Project Utilizing Glycans Dev Innovat Drug Discov Chuo Ku Tokyo 1040032 Japan Hokkaido Univ Fac Vet Med Dept Dis Control Microbiol Lab Sapporo Hokkaido 0600818 Japan

Glycan structures on hemagglutinin (HA) of influenza A viruses have been analyzed previously to understand their significance. However, the formerly established methods using mass spectrometry present disadvantages such as procedure complexity, sensitivity, and throughput. Our study has established a novel method for analyzing glycan profiles of HA using lectin microarray techniques. We successfully obtained glycan profiles of HA starting from 1 ml of the 10(6) TCID50 samples through simple antigen enrichment using optimized immunoprecipitation. The profiles were reasonably consistent with known glycan structures of HA. Next, we compared glycan profiles of the HAs prepared from chicken embryos, MDCK, Vero, and A549 cells, and demonstrated the host cell-specific HA glycan profiles. Notably, the HA from MDCK cells was alpha 1-3 galactosylated. Our method provides a highly sensitive and simple procedure for glycan profiling of the viral glycoproteins, thereby paving way for direct glycan analyses of human- and animal-derived virions.

关键词： Influenza A virus lectin microarray Hemagglutinin Glycosylation alpha-Gal

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Glycoprotein profiling of stem cells using lectin microarray based on surface plasmon resonance imaging

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ANALYTICAL BIOCHEMISTRY 2014年 465卷 114-120页

作者： Nand, Amita Singh, Vikramjeet Wang, Peizhe Na, Jie Zhu, Jingsong Natl Ctr Nanosci & Technol Beijing 100190 Peoples R China Univ Chinese Acad Sci Beijing 100049 Peoples R China Tsinghua Univ Sch Med Ctr Stem Cell Biol & Regenerat Med Beijing 100084 Peoples R China

lectin microarrays have emerged as a novel platform for glycan analysis during recent years. Here, we have combined surface plasmon resonance imaging (SPRi) with the lectin microarray for rapid and label-free profiling of stem cells. In this direction, 40 lectins from seven different glyco-binding motifs and three different cell lines-mouse embryonic stem cells (mESCs), mouse-induced pluripotent stem cells (miPSCs), and mouse embryonic fibroblast stem cells (MEFs)-were used. Pluripotent mouse stem cells were clearly distinguished from non-pluripotent stem cells. Eight lectins-DBA, MAL, PHA_E, PHA_L, EEL, AAL, PNA, and SNA-generated maximal value to define pluripotency of mouse stem cells in our experiments. The discriminant function based on lectin reactivities was highly accurate for the determination of stem cell pluripotency. These results suggested that glycomic analysis of stem cells leads to a novel comprehensive approach for quality control in cell-based therapy and regenerative medicine. (c) 2014 Elsevier Inc. All rights reserved.

关键词： lectin microarray SPRi Stem cell Glycoprotein Pluripotency

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Profiling the Cell Surface Glycome of Five Fungi Using lectin microarray (vol 30, pg 147, 2011)

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JOURNAL OF CARBOHYDRATE CHEMISTRY 2011年第7-9期30卷 655-655页

作者： Shibazaki, Azusa Tateno, Hiroaki Akikazu, Ando Hirabayashi, Jun Gonoi, Tohru [a] Medical Mycology Research Center Chiba University Chuo-ku Inohana 1-8-1 Chiba 260-8673 Japan [b] Research Center for Medical Glycoscience National Institute of Advanced Industrial Science and Technology Central 2 1-1-1 Umezono Ibaraki 305-8568 Japan [c] Chiba University Association of Graduate Schools of Science Technology Matsudo 6-4-8 Matsudo-shi Chiba 271-8511 Japan

Fungal surface glycans play roles in cell protection and interaction. Our knowledge of fungal glycans, however, is limited to model yeasts and a few medically/industrially important fungi. We evaluated the usefulness of a lectin microarray in analysis of live cell surface glycans and then applied the technique to glycome of varieties of yeast-form fungi from various phyla and subphyla. We found glycan profiles are different among and within taxonomic groups. For example, Saccharomycotina were classified into two groups, one bound to mannose-specific lectins and the other bound to galactose/N-acetylgalactosamine-specific lectins. In Basidiomycota, Pucciniomycotina yeasts were distinguished from other subphylum members in binding to fucose-specific lectins. Supplemental materials are available for this article. Go to the publisher's online edition of Journal of Carbohydrate Chemistry to view the free supplemental file. View full text Download full text

关键词： Cell wall Fungi Glycans Glycome lectin microarray

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Campylobacter jejuni strain discrimination and temperature-dependent glycome expression profiling by lectin microarray

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CARBOHYDRATE RESEARCH 2014年第1期389卷 123-133页

作者： Kilcoyne, Michelle Twomey, Marcus E. Gerlach, Jared Q. Kane, Marian Moran, Anthony P. Joshi, Lokesh Natl Univ Ireland Natl Ctr Biomed Engn Sci Glycosci Grp Galway Ireland Natl Univ Ireland Sch Nat Sci Galway Ireland

Gram-negative Campylobacter jejuni is the leading cause of bacterial gastroenteritis in humans worldwide and the most frequently identified infectious trigger in patients developing Guillain-Barre syndrome (GBS). While C. jejuni is pathogenic in humans, it is a commensal in avian hosts. Bacterial cell surface carbohydrates are important virulence factors and play roles in adherence, colonisation and infection. The mechanisms leading to infection or persistent colonisation of C. jejuni are not well understood but host temperature may provide an important stimulus for specific adaptation. Thus, examination of the modulation of the total surface glycome of C. jejuni in response to temperature may help shed light on commensal and pathogenic mechanisms for this species. C. jejuni strains 81116 and 81-176 were cultured at 37 and 42 degrees C to simulate human and avian host conditions, respectively, and whole cells were profiled on lectin microarrays constructed to include a wide range of binding specificities. C. jejuni 81116 profiles indicated that the previously characterised lipopolysaccharide (LPS)-like molecule and N-linked glycans were the predominantly recognised cell surface structures while capsular polysaccharide (CPS), lipooligosaccharides (LOS) and N-linked glycosylation were best recognised for strain 81-176 at 37 degrees C. The profiles of both strains varied and were distinguishable at both temperatures. At the higher temperature, reduced dominance of the LPS-like structure was associated with strain 81116 and a change in the relative distribution of CPS and LOS structures was indicated for strain 81-176. This change in LOS molecular mass species distribution between temperatures was confirmed by SDS-PAGE analysis. Additionally, opposite behaviour of certain lectins was noted between the plate agglutination assay and the microarray platform. Insights into the important glycosylation involved in C. jejuni host cell tropism at different growth temperatures w

关键词： Campylobacter jejuni lectin microarray Virulence factors Lipooligosaccharide Lipopolysaccharide Capsular polysaccharide

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LM-GlycomeAtlas Ver. 2.0: An Integrated Visualization for lectin microarray-based Mouse Tissue Glycome Mapping Data with lectin Histochemistry

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JOURNAL OF PROTEOME RESEARCH 2021年第4期20卷 2069-2075页

作者： Nagai-Okatani, Chiaki Zou, Xia Fujita, Noriaki Sogabe, Isami Arakawa, Kouiti Nagai, Misugi Angata, Kiyohiko Zhang, Yan Aoki-Kinoshita, Kiyoko F. Kuno, Atsushi Shanghai Jiao Tong Univ Shanghai Ctr Syst Biomed Minist Educ Key Lab Syst Biomed Shanghai 200240 Peoples R China Natl Inst Adv Ind Sci & Technol Cellular & Mol Biotechnol Res Inst Mol & Cellular Glycoprote Res Grp Tsukuba Ibaraki 3058565 Japan Soka Univ Glycan & Life Sci Integrat Ctr GaLSIC Fac Sci & Engn Hachioji Tokyo 1928577 Japan

Laser microdissection-assisted lectin microarray has been used to obtain quantitative and qualitative information on glycans on proteins expressed in microscopic regions of formalin-fixed paraffin-embedded tissue sections. For the effective visualization of this "tissue glycome mapping" data, a novel online tool, LM-GlycomeAtlas (https://***/lm glycomeadas/index), was launched in the freely available glycoscience portal, the GlyCosmos Portal (haps://*** ). In LM-GlycomeAtlas Version 1.0, nine tissues from normal mice were used to provide one data set of glycomic profiles. Here we introduce an updated version of LM-GlycomeAtlas, which includes more spatial information. We designed it to deposit multiple data sets of glycomic profiles with high-resolution histological images, which included staining images with multiple lectins on the array. The additionally implemented interfaces allow users to display multiple histological images of interest (e.g., diseased and normal mice), thereby facilitating the evaluation of tissue glycomic profiling and glyco-pathological analysis. Using these updated interfaces, 451 glycomic profiling data and 42 histological images obtained from 14 tissues of normal and diseased mice were successfully visualized. By easy integration with other tools for glycoproteomic data and protein glycosylation machinery, LM-GlycomeAtlas will be one of the most valuable open resources that contribute to both glycoscience and proteomics communities.

关键词： glycoinformatics web tool endogenous glycoprotein tissue glycome mapping formalin-fixed paraffin-embedded tissue section laser microdissection lectin microarray histochemistiy

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