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Comparative Glycomic Analysis of Exosome Subpopulations Derived from Pancreatic Cancer Cell Lines

JOURNAL OF PROTEOME RESEARCH 2020年第6期19卷 2516-2524页

作者： Matsuda, Atsushi Kuno, Atsushi Yoshida, Maki Wagatsuma, Takanori Sato, Takashi Miyagishi, Makoto Zhao, Jing Suematsu, Makoto Kabe, Yasuaki Narimatsu, Hisashi Natl Inst Adv Ind Sci & Technol Biotechnol Res Inst Drug Discovery Tsukuba Ibaraki 3058565 Japan Keio Univ Dept Biochem Sch Med Tokyo 1608582 Japan AIST Biomed Res Inst Tsukuba Ibaraki 3058566 Japan

Extracellular vesicles such as exosomes are generally covered with an array of glycans, which are controlled by the hostcell glyco-synthetic machinery, similar to secreted and membrane glycoproteins. Several exosome subpopulations classified by their tetraspanin expression have been investigated in the context of diseases. However, a comparative analysis of their glycomics has never been attempted. Herein, we report a method for the comparative glycomic analysis of exosome subpopulations among pancreatic cancer cell lines. Glycomic profiles were obtained for extracellular vesicles, secreted glycoproteins, and membrane glycoproteins from eight cell lines. Statistical analyses revealed high populations of PHA-L-binding proteins in the vesicles. The surfaces of extracellular vesicles were labeled with Cy3 and captured by magnetic beads with antibodies against tetraspanins (CD9, CD63, and CD81). The coprecipitated vesicles were lysed and subjected to a lectin microarray analysis. A hierarchical clustering analysis using 19 glycomic profiles confirmed that most subpopulations, except CD81-positive exosomes, could be distinguished according to the host-cell species. Principal component analysis and subsequent lectin-affinity capturing of intact exosomes highlighted that CD81-positive exosomes preferentially expressed not PHA-L- but LEL-binding proteins on their surfaces. These data suggested that exosomal glycomics depended on the host-cell type and subpopulation.

关键词： exosome lectin microarray glycomics glycoprotein

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Glycomic analysis of host response reveals high mannose as a key mediator of influenza severity

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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 2020年第43期117卷 26926-26935页

作者： Heindel, Daniel W. Koppolu, Sujeethraj Zhang, Yue Kasper, Brian Meche, Lawrence Vaiana, Christopher A. Bissel, Stephanie J. Carter, Chalise E. Kelvin, Alyson A. Elaish, Mohamed Lopez-Orozco, Joaquin Zhang, Bin Zhou, Bin Chou, Tsui-Wen Lashua, Lauren Hobman, Tom C. Ross, Ted M. Ghedin, Elodie Mahal, Lara K. NYU Dept Chem Biomed Res Inst New York NY 10003 USA Univ Pittsburgh Sch Med Dept Pathol Pittsburgh PA 15261 USA Univ Georgia Ctr Vaccines & Immunol Athens GA 30602 USA Dalhousie Univ Dept Pediat Halifax NS B3H 4R2 Canada Univ Alberta Dept Cell Biol Edmonton AB T6G 2R7 Canada Cairo Univ Poultry Dis Dept Fac Vet Med Cairo 12211 Egypt Univ Alberta Fac Med & Dent High Content Anal Core Edmonton AB T6G 2R7 Canada Icahn Sch Med Mt Sinai Dept Genet & Genom Sci Mt Sinai Ctr Transformat Dis Modeling Icahn Inst Genom & Multiscale Biol New York NY 10029 USA NYU Dept Biol Ctr Genom & Syst Biol New York NY 10003 USA NYU Sch Global Publ Hlth Dept Epidemiol New York NY 10003 USA NIAID Lab Parasit Dis NIH 9000 Rockville Pike Bethesda MD 20892 USA Univ Alberta Dept Chem Edmonton AB T6G 2G2 Canada

Influenza virus infections cause a wide variety of outcomes, from mild disease to 3 to 5 million cases of severe illness and similar to 290,000 to 645,000 deaths annually worldwide. The molecular mechanisms underlying these disparate outcomes are currently unknown. Glycosylation within the human host plays a critical role in influenza virus biology. However, the impact these modifications have on the severity of influenza disease has not been examined. Herein, we profile the glycomic host responses to influenza virus infection as a function of disease severity using a ferret model and our lectin microarray technology. We identify the glycan epitope high mannose as a marker of influenza virus-induced pathogenesis and severity of disease outcome. Induction of high mannose is dependent upon the unfolded protein response (UPR) pathway, a pathway previously shown to associate with lung damage and severity of influenza virus infection. Also, the mannan-binding lectin (MBL2), an innate immune lectin that negatively impacts influenza outcomes, recognizes influenza virus-infected cells in a high mannose-dependent manner. Together, our data argue that the high mannose motif is an infection-associated molecular pattern on host cells that may guide immune responses leading to the concomitant damage associated with severity.

关键词： lectin microarray MBL2 lectin array mannose binding lectin mannan binding lectin

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SugarArray: A User-centred-designed Platform for the Analysis of lectin and Glycan microarrays 13

SugarArray: A User-centred-designed Platform for the Analysi...

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13th International Joint Conference on Biomedical Engineering Systems and Technologies

作者： Sucre, Aurora Pazos, Raquel Reichardt, Niels-Christian Garin-Muga, Alba Biodonostia eHlth Grp Donostia San Sebastian 20014 Spain Vicomtech eHlth & Biomed Applicat Donostia San Sebastian 20014 Spain Glycotechnol Lab CIC BiomaGUNE Paseo Miramon 182 San Sebastian 20014 Spain CIBER BBN Paseo Miramon 182 San Sebastian 20014 Spain

ISBN: (纸本)9789897583988

Glycan and lectin microarrays are two arising technologies, very important to the glycomics field. Glycomics is the science that focuses on defining the structures and functions of carbohydrates in nature. These microarrays provide information regarding the interactions between specific carbohydrates and proteins, and it has many applications in clinical and research settings. Nevertheless, the availability of analytical software for these types of arrays is very limited, so researchers usually perform data processing and analytical pipelines manually, which is very time consuming and prone to error. SugarArray was born as a user-friendly and intuitive stand-alone solution that process the intensity data generated from glycan or lectin array studies, and displays the results to the user in an understandable manner The solution also allows the users to manage the data as needed, create data plots and automatically generate reports. This tool was intended to simplify the processing steps of the analytical pipeline, so the users can focus on what really matters: understanding the results.

关键词： Glycomics lectin microarray Glycan microarray microarray Data Analysis Data Visualization

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Integrated Systems Analysis of the Murine and Human Pancreatic Cancer Glycomes Reveals a Tumor-Promoting Role for ST6GAL1

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Molecular and Cellular Proteomics 2021年 20卷 100160-100160页

作者： Kurz, Emma Chen, Shuhui Vucic, Emily Baptiste, Gillian Loomis, Cynthia Agrawal, Praveen Hajdu, Cristina Bar-Sagi, Dafna Mahal, Lara K. Department of Cell Biology NYU Grossman School of Medicine New York NY United States Department of Chemistry Biomedical Research Institute New York University New York NY United States Department of Biochemistry and Molecular Pharmacology NYU Grossman School of Medicine New York NY United States Department of Pathology NYU Grossman School of Medicine New York NY United States Office of Science and Research NYU Grossman School of Medicine New York NY United States

Pancreatic ductal adenocarcinoma (PDAC) is the third leading cause of cancer death in the United States. Glycans, such as carbohydrate antigen 19-9, are biomarkers of PDAC and are emerging as important modulators of cancer phenotypes. Herein, we used a systems-based approach integrating glycomic analysis of the well-established KC mouse, which models early events in transformation, and analysis of samples from human pancreatic cancer patients to identify glycans with potential roles in cancer formation. We observed both common and distinct patterns of glycosylation in pancreatic cancer across species. Common alterations included increased levels of α-2,3-sialic acid and α-2,6-sialic acid, bisecting GlcNAc and poly-N-acetyllactosamine. However, core fucose, which was increased in human PDAC, was not seen in the mouse, indicating that not all human glycomic changes are observed in the KC mouse model. In silico analysis of bulk and single-cell sequencing data identified ST6 beta-galactoside alpha-2,6-sialyltransferase 1, which underlies α-2,6-sialic acid, as overexpressed in human PDAC, concordant with histological data showing higher levels of this enzyme at the earliest stages. To test whether ST6 beta-galactoside alpha-2,6-sialyltransferase 1 promotes pancreatic cancer, we created a novel mouse in which a pancreas-specific genetic deletion of this enzyme overlays the KC mouse model. The analysis of our new model showed delayed cancer formation and a significant reduction in fibrosis. Our results highlight the importance of a strategic systems approach to identifying glycans whose functions can be modeled in mouse, a crucial step in the development of therapeutics targeting glycosylation in pancreatic cancer. © 2021 American Society for Biochemistry and Molecular Biology Inc.. All rights reserved.

关键词： lectin microarray glycosylation ST6GAL1 pancreatic cancer lectin array

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Overexpressed N-fucosylation on the cell surface driven by FUT3, 5, and 6 promotes cell motilities in metastatic pancreatic cancer cell lines

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BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 2019年第2期511卷 482-489页

作者： Gao, Hui-Feng Wang, Qi-yang Zhang, Ke Chen, Lian-Yu Cheng, Chien-Shan Chen, Hao Meng, Zhi-Qiang Zhou, Shu-min Chen, Zhen Fudan Univ Shanghai Med Coll Dept Oncol Shanghai 200032 Peoples R China Fudan Univ Shanghai Canc Ctr Dept Integrat Oncol Shanghai 200032 Peoples R China Shanghai Jiao Tong Univ Affiliated Peoples Hosp 6 Dept Orthoped Shanghai 200233 Peoples R China Shanghai Jiao Tong Univ Affiliated Peoples Hosp 6 Inst Microsurg Extrem Shanghai 200233 Peoples R China

Pancreatic cancer is a highly malignant tumor of the digestive system. Previous studies have shown that abnormal cell surface glycosylation is associated with cancer metastasis, which suggests that glycosylation changes may open a new window for discovering metastasis-related pathways. In this study, we used a microarray with 55 lectins to screen for altered glycosylation between two metastatic pancreatic cancer lines (Capan-1 and Su.86.86) and two nonmetastatic pancreatic cancer lines (Panc-1 and MIA PaCa-2), and we further analyzed three lectins with high-binding activities (AAL, UEA-I, and PHA-E) in cell motility assays using these pancreatic cancer cells to detect whether blocking certain forms of cell surface glycosylation affects any processes associated with metastasis. As a result, we found that AAL, a fucose-specific lectin, has different binding patterns between metastatic pancreatic cancer and non metastatic pancreatic cancer lines and inhibits cell motility in metastatic pancreatic cancer cells. Furthermore, the N-fucosylation-related genes FUT3, 5, and 6 were found to be responsible for the elevated fucosylation in metastatic pancreatic cells through real-time PCR screening. In summary, our findings that the specific bindings of AAL on cell surfaces and highly expressed FUT3, 5, and 6 in metastatic pancreatic cancer cells, although preliminary, are encouraging, and our established combined method is also suitable for discovering metastasis-related mechanisms in other cancers. (C) 2019 Published by Elsevier Inc.

关键词： Pancreatic cancer cells Metastasis lectin microarray N-fucosylation

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Vaginal Product Formulation Alters the Innate Antiviral Activity and Glycome of Cervicovaginal Fluids with Implications for Viral Susceptibility

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ACS INFECTIOUS DISEASES 2018年第11期4卷 1613-1622页

作者： Koppolu, Sujeethraj Wang, Linlin Mathur, Ayushi Nigam, Jayeshwar A. Dezzutti, Charlene S. Isaacs, Charles Meyn, Leslie Bunge, Katherine E. Moncla, Bernard J. Hillier, Sharon L. Rohan, Lisa C. Mahal, Lara K. NYU Dept Chem Biomed Chem Inst 100 Washington Sq East New York NY 10003 USA Magee Womens Res Inst 204 Craft AveB511 Pittsburgh PA 15213 USA Univ Pittsburgh Sch Med Dept Obstet Gynecol & Reprod Sci 300 Halket St Pittsburgh PA 15213 USA New York State Inst Basic Res Dev Disabil Dept Dev Biochem 1050 Forest Hill Rd New York NY 10314 USA Univ Pittsburgh Dept Pharmaceut Sci Pittsburgh PA 15213 USA

Glycosylated proteins (i.e., mucins, IgG) are important mediators of innate antiviral immunity in the vagina;however, our current knowledge of the role that glycan themselves play in genital immunity is relatively low. Herein, we evaluate the relationship between innate antiviral immunity and glycomic composition in cervicovaginal lavage fluid (CVL) collected as part of a Phase I clinical trial testing the impact of two distinct formulations of the antiretroviral drug dapivirine. Using lectin microarray technology, we discovered that formulation (hydrogel- versus film-based delivery) impacted the CVL glycome, with hydrogel formulations inducing more changes, including a loss of high-mannose. The loss of this epitope correlated to a loss of anti-HIV-1 activity. Glycoproteomic identification of high-mannose proteins revealed a cohort of antiproteases shown to be important in HIV-1 resistance, whose expression covaried with the high-mannose signature. Our data strongly suggests high-mannose as a marker for secreted proteins mediating innate antiviral immunity in vaginal fluids and that drug formulation may impact this activity as reflected in the glycome.

关键词： high-mannose lectin microarray cervicovaginal lavage innate antiviral immunity antiproteases antiviral activity

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Current Technologies for Complex Glycoproteomics and Their Applications to Biology/Disease-Driven Glycoproteomics

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JOURNAL OF PROTEOME RESEARCH 2018年第12期17卷 4097-4112页

作者： Narimatsu, Hisashi Kaji, Hiroyuki Vakhrushev, Sergey Y. Clausen, Henrik Zhang, Hui Noro, Erika Togayachi, Akira Nagai-Okatani, Chiaki Kuno, Atsushi Zou, Xia Cheng, Li Tao, Sheng-Ce Sun, Yangyang Natl Inst Adv Ind Sci & Technol Biotechnol Res Inst Drug Discovery 1-1-1 Umezono Tsukuba Ibaraki 3058568 Japan Univ Copenhagen Copenhagen Ctr Glyc Blegdamsvej 3 DK-2200 Copenhagen Denmark Johns Hopkins Univ Ctr Biomarker Discovery & Translat 400 North Broadway Baltimore MD 21205 USA Shanghai Jiao Tong Univ Shanghai Ctr Syst Biomed Key Lab Syst Biomed Minist Educ 800 Dong Chuan Rd Shanghai 200240 Peoples R China

Glycoproteomics is an important recent advance in the field of glycoscience. In glycomics, glycan structures are comprehensively analyzed after glycans are released from glycoproteins. However, a major limitation of glycomics is the lack of insight into glycoprotein functions. The Biology/Disease-driven Human Proteome Project has a particular focus on biological and medical applications. Glycoproteomics technologies aimed at obtaining a comprehensive understanding of intact glycoproteins, i.e., the kind of glycan structures that are attached to particular amino acids and proteins, have been developed. This Review focuses on the recent progress of the technologies and their applications. First, the methods for large-scale identification of both N- and O-glycosylated proteins are summarized. Next, the progress of analytical methods for intact glycopeptides is outlined. MS/MS-based methods were developed for improving the sensitivity and speed of the mass spectrometer, in parallel with the software for complex spectrum assignment. In addition, a unique approach to identify intact glycopeptides using MS1-based accurate masses is introduced. Finally, as an advance of glycomics, two approaches to provide the spatial distribution of glycans in cells are described, i.e., MS imaging and lectin microarray. These methods allow rapid glycomic profiling of different types of biological samples and thus facilitate glycoproteomics.

关键词： glycoprotein glycoproteome mass spectrometry protein glycosylation glycosylation site-mapping site-specific glycan analysis lectin microarray glycome mapping glycan spatial distribution

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lectin BS-I inhibits cell migration and invasion via AKT/GSK-3β/β-catenin pathway in hepatocellular carcinoma

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JOURNAL OF CELLULAR AND MOLECULAR MEDICINE 2018年第1期22卷 315-329页

作者： Jian, Qiang Yang, Zhao Shu, Jian Liu, Xiawei Zhang, Jing Li, Zheng Northwest Univ Coll Life Sci Lab Funct Glyc Xian Shaanxi Peoples R China Northwest Univ Fac Life Sci Lab Tissue Engn Xian Shaanxi Peoples R China

Hepatocellular carcinoma (HCC) is most common malignant cancer worldwide;however, the mortality rate of HCC remains high due to the invasion and metastasis of HCC. Thus, exploring novel treatments to prevent the invasion of HCC is needed for improving clinical outcome of this fatal disease. In this study, we identified lectin from Bandeiraea simplicifolia seeds (BS-I) binds to metastasis-associated HCC cell surface glycans by a lectin microarray and inhibits HCC cell migration and invasion through downregulating the matrix metalloproteinase 2 (MMP2), matrix metalloproteinase 9 (MMP9) and urokinase-type plasminogen activator (uPA) production. These effects of BS-I were mediated by inhibiting the activation of AKT/GSK-beta/beta-catenin pathway and depended on specificity of lectin BS-I binding to GalNAc. GSK beta inhibitors rescued BS-I-mediated inhibition of migration and invasion of HCC cell. Further, we identified that lectin BS-I interacts with sGrp78, affects membrane localization of sGrp78 and attenuates the binding of sGrp78 and p85 to inhibit the activation of AKT/GSK-beta/beta-catenin pathway. Overexpression of Grp78 or P85 rescues BS-I-mediated inhibition of migration and invasion of HCC cell. These findings demonstrated for the first time that BS-I can act as a novel potential drug to prevent the invasion of HCC.

关键词： hepatocellular carcinoma lectin microarray GRP78 AKT GSK-3 beta/beta-catenin pathway Glycosylation

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Characteristic glycopeptides associated with extreme human longevity identified through plasma glycoproteomics

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BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS 2018年第6期1862卷 1462-1471页

作者： Miura, Yuri Hashii, Noritaka Ohta, Yuki Itakura, Yoko Tsumoto, Hiroki Suzuki, Junya Takakura, Daisuke Abe, Yukiko Arai, Yasumichi Toyoda, Masashi Kawasaki, Nana Hirose, Nobuyoshi Endo, Tamao Tokyo Metropolitan Inst Gerontol Res Team Mech Aging Itabashi Ku 35-2 Sakae Cho Tokyo 1730015 Japan Natl Inst Hlth Sci Div Biol Chem & Biol Kawasaki Ku 3-25-26 Tono Machi Kawasaki Kanagawa 2109501 Japan Tokyo Metropolitan Inst Gerontol Res Team Geriatr Med Itabashi Ku 35-2 Sakae Cho Tokyo 1730015 Japan Keio Univ Sch Med Ctr Supercentenarian Med Res Shinjuku Ku 35 Shinano Machi Tokyo 1608582 Japan Yokohama City Univ Grad Sch Med Life Sci Kanazawa Ku 3-9 Hukuura Yokohama Kanagawa 2360004 Japan Keio Univ Sch Med Ctr Integrated Med Res Shinjuku Ku 35 Shinano Machi Tokyo 1608582 Japan

Background: Glycosylation is highly susceptible to changes of the physiological conditions, and accordingly, is a potential biomarker associated with several diseases and/or longevity. Semi-supercentenarians (SSCs;older than 105 years) are thought to be a model of human longevity. Thus, we performed glycoproteomics using plasma samples of SSCs, and identified proteins and conjugated N-glycans that are characteristic of extreme human longevity. Methods: Plasma proteins from Japanese semi-supercentenarians (SSCs, 106-109 years), aged controls (70-88 years), and young controls (20-38 years) were analysed by using lectin microarrays and liquid chromatography/mass spectrometry (LC/MS). Peak area ratios of glycopeptides to corresponding normalising peptides were subjected to orthogonal projections to latent structures discriminant analysis (OPLS-DA). Furthermore, plasma levels of clinical biomarkers were measured. Results: We found two lectins such as Phaseolus vulgaris, and Erythrina cristagalli (ECA), of which protein binding were characteristically increased in SSCs. Peak area ratios of ECA-enriched glycopeptides were successfully discriminated between SSCs and controls using OPLS-DA, and indicated that tri-antennary and sialylated N-glycans of haptoglobin at Asn207 and Asn211 sites were characterized in SSCs. Sialylated glycans of haptoglobin are a potential biomarker of several diseases, such as hepatocellular carcinoma, liver cirrhosis, and IgA-nephritis. However, the SSCs analysed here did not suffer from these diseases. Conclusions: Tri-antennary and sialylated N-glycans on haptoglobin at the Asn207 and Asn211 sites were abundant in SSCs and characteristic of extreme human longevity. General significance: We found abundant glycans in SSCs, which may be associated with human longevity.

关键词： N-glycosylation lectin microarray LC/MS Longevity Semi-supercentenarian

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Stage-associated differences in the serum N- and O-glycan profiles of patients with non-small cell lung cancer

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CLINICAL PROTEOMICS 2019年第1期16卷 20-20页

作者： Liang, Yiqian Han, Peng Wang, Ting Ren, Hui Gao, Lei Shi, Puyu Zhang, Shuo Yang, Aimin Li, Zheng Chen, Mingwei Xi An Jiao Tong Univ Affiliated Hosp 1 Dept Resp & Crit Care Med Xian 710061 Shaanxi Peoples R China Xi An Jiao Tong Univ Affiliated Hosp 1 Dept Nucl Med Xian 710061 Shaanxi Peoples R China Northwest Univ Coll Life Sci Lab Funct Glyc Xian 710069 Shaanxi Peoples R China Xi An Jiao Tong Univ Affiliated Hosp 1 Dept Otolaryngol Head & Neck Surg Xian 710061 Shaanxi Peoples R China Xian 4 Hosp Dept Resp Med Xian 710004 Shaanxi Peoples R China Xi An Jiao Tong Univ Affiliated Hosp 2 Dept Endocrinol Xian 710004 Shaanxi Peoples R China Xi An Jiao Tong Univ Affiliated Hosp 1 Dept Radiol Xian 710061 Shaanxi Peoples R China

BackgroundLung cancer is the leading cause of cancer death in China and around the world. Early detection is key to improving the survival rate of non-small cell lung cancer (NSCLC). Alteration in glycosylation has been observed in cancers, and glycans can be a source for the development of new biomarkers for *** this glycan biomarker discovery study, we measured serum N- and O-glycan profiles in NSCLC patients with different stages and healthy controls by performing lectin microarray analysis. The alterations of serum glycopatterns were compared between NSCLC patients and controls, and the stage-related changes in serum glycosylation were *** were 18 lectins (e.g., AAL, Jacalin, GSL-I and DBA) to give significantly alterations of serum glycopatterns in lung adenocarcinoma compared with control group. Meanwhile, 16 lectins (e.g., Jacalin, HHL, and PHA-E+L) exhibited significantly alterations of serum glycopatterns in squamous cell carcinoma (SCC) compared with control group. Importantly, most of the lectins showing altered signals exhibited significantly increased or decreased NFIs in patients with early stage adenocarcinoma and *** serum glycan profiles were significantly different between NSCLC and healthy control, and most of the glycosylation changes had occurred at early stage. Further evaluation is needed to examine the diagnostic value of the glycan markers identified in this study.

关键词： Non-small cell lung cancer Protein glycosylation Serum biomarkers lectin microarray Glycomics

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