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Cross Validation of Liquid Chromatography-Mass Spectrometry and lectin array for Monitoring Glycosylation in Fed-Batch Glycoprotein Production

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MOLECULAR BIOTECHNOLOGY 2012年第3期51卷 272-282页

作者： Hayes, Catherine A. Doohan, Roisin Kirkley, David Leister, Kirk Harhen, Brendan Savage, Angela V. Karlsson, Niclas G. Bristol Myers Squibb Co Syracuse NY USA Natl Univ Ireland Sch Chem Galway Ireland

Glycosylation analysis of recombinant glycoproteins is of importance for the biopharmaceutical industry and the production of glycoprotein pharmaceuticals. A commercially available lectin array technology was evaluated for its ability to present a reproducible fingerprint of a recombinant CTLY4-IgG fusion glycoprotein expressed in large scale CHO-cell fermentation. The glycosylation prediction from the array was compared to traditional negative mode capillary LC-MS of released oligosaccharides. It was shown that both methods provide data that allow samples to be distinguished by their glycosylation pattern. This included information about sialylation, the presence of reducing terminal galactose beta 1-, terminal N-acetylglucosamine beta 1-, and antennary distribution. With both methods it was found that a general trend of increased sialylation was associated with an increase of the antenna and reduced amount of terminal galactose beta 1-, while N-acetylglucosamine beta 1- was less affected. LC-MS, but not the lectin array, provided valuable information about the sialic acid isoforms present, including N-acetylneuraminic acid, N-glycolylneuraminic acid and their O-acetylated versions. Detected small amounts of high-mannose structures by LC-MS correlated with the detection of the same epitope by the lectin array.

关键词： Glycosylation High mannose Acetylation N-linked oligosaccharides lectin array Mass spectrometry

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A lectin array analysis for wild-type and α-Gal-knockout pig islets versus healthy human islets

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SURGERY TODAY 2013年第12期43卷 1439-1447页

作者： Miyagawa, Shuji Maeda, Akira Takeishi, Shunsaku Ueno, Takehisa Usui, Noriaki Matsumoto, Shinichi Okitsu, Teru Goto, Masafumi Nagashima, Hiroshi Osaka Univ Grad Sch Med Dept Surg Div Organ Transplantat Suita Osaka 5650871 Japan Moritex Corp Glyc Res Lab Yokohama Kanagawa Japan Natl Ctr Global Hlth & Med Tokyo Japan Univ Tokyo Inst Ind Sci Meguro Ku Tokyo 1538505 Japan Tohoku Univ Int Adv Res & Educ Org Sendai Miyagi 980 Japan Meiji Univ Dept Life Sci Lab Dev Engn Kanagawa Japan

We performed lectin microarray analyses of islets from wild-type (WT) pigs and alpha 1-3galactosyltransferase gene knockout (GKO) pigs and compared the results with the corresponding values for islets from healthy humans. Islets were isolated from the pancreas. After sonication and centrifugation, the proteins in the supernatant from each islet were labeled with Cy3 and applied to a lectin array. Despite negligible expression of the Gal antigen on the adult pig islets (APIs), GKO-islets showed weaker signals, not only for GS-I-B4 but also for PNA, WFA, PTL-I, and GS-I-A4, than the WT islets, indicating reduced contents of alpha-linked GalNAc and Gal beta 1-3GalNAc. In comparing the islets of pigs vs. humans, human islets showed stronger signals for UEA-I, AAL, TJA-II, EEL, WFA, HPA, DBA, SBA and PTL-I, indicating that besides ABO blood type antigens, high levels of fucose and alpha-linked GalNAc are present. On the other hand, the high mannose form was very rich in the APIs. GKO reduced alpha-linked GalNAc, despite negligible expression of the Gal antigen on WT-API. On the other hand, the high-mannose form was richer in both APIs than in healthy human islets. These results provide useful information for future studies.

关键词： Xenotransplantation Glycoantigen lectin array Islets

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Cell surface lectin array: parameters affecting cell glycan signature

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GLYCOCONJUGATE JOURNAL 2013年第3期30卷 195-203页

作者： Landemarre, Ludovic Cancellieri, Perrine Duverger, Eric Univ Orleans GLYcoDIAG F-45067 Orleans 2 France Univ Orleans GlycoBiochim Dept Biol F-45067 Orleans 2 France

Among the "omics", glycomics is one of the most complex fields and needs complementary strategies of analysis to decipher the "glycan dictionary". As an alternative method, which has developed since the beginning of the 21st century, lectin array technology could generate relevant information related to glycan motifs, accessibility and a number of other valuable insights from molecules (purified and non-purified) or cells. Based on a cell line model, this study deals with the key parameters that influence the whole cell surface glycan interaction with lectin arrays and the consequences on the interpretation and reliability of the results. The comparison between the adherent and suspension forms of Chinese Hamster Ovary (CHO) cells, showed respective glycan signatures, which could be inhibited specifically by neoglycoproteins. The modifications of the respective glycan signatures were also revealed according to the detachment modes and cell growth conditions. Finally the power of lectin array technology was highlighted by the possibility of selecting and characterizing a specific clone from the mother cell line, based on the slight difference determination in the respective glycan signatures.

关键词： Carbohydrate Cell lines Glycomics lectin array

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Glycan profiling analysis using evanescent-field fluorescence-assisted lectin array: Importance of sugar recognition for cellular uptake of exosomes from mesenchymal stem cells

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BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 2017年第3期491卷 701-707页

作者： Shimoda, Asako Tahara, Yoshiro Sawada, Shin-ichi Sasaki, Yoshihiro Akiyoshi, Kazunari Kyoto Univ Dept Polymer Chem Grad Sch Engn Nishikyo Ku Kyoto 6158510 Japan Japan Sci & Technol Agcy JST Exploratory Res Adv Technol ERATO Bionanotransporter Project Katsura Inttech CtrNishikyo Ku Kyoto 6158530 Japan

Studies involving the functional analysis of exosomal contents including proteins, DNA, and RNA have been reported. Most membrane proteins and lipids are glycosylated, which controls their physical properties and functions, but little is known about glycans on exosomes owing to the difficulty of analysing them. To shed light on these issues, we collected exosomes from mesenchymal stem cells (MSCs) derived from human adipose tissue for glycan profiling using evanescent-field fluorescence assisted lectin array as well as analysis of their uptake in vivo. Initial analyses showed that the mean diameter of the collected exosomes was 178 nm and they presented with typical exosomal and MSC markers. Regarding the glycan profiling, exosomes interacted more strongly than the membrane of the original MSCs did with a range of lectins, especially sialic acid-binding lectins. The findings also showed that cellular exosome uptake involved recognition by HeLa cell-surface-bound sialic acid-binding immunoglobulin (1g)-like lectins (siglecs). Confirming this siglec-related uptake, in vivo experiments involving subcutaneous injection of the fluorescently labelled exosomes into mice showed their transport into lymph nodes and internalization by antigen-presenting cells, particularly those expressing CD11b. Closer analysis revealed the colocalization of the exosomes with siglecs, indicating their involvement in the uptake. These findings provide us with an improved understanding of the importance of exosomal transport and targeting in relation to glycans on exosomal surfaces, potentially enabling us to standardize exosomes when using them for therapeutic purposes.(C) 2017 Elsevier Inc. All rights reserved.

关键词： Exosome Mesenchymal stem cell Glycan lectin array Sialic acid

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lectin array to detect ionizing radiation-induced changes in cell surface glycans

Lectin array to detect ionizing radiation-induced changes in...

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第十届全国化学生物学学术会议

作者： ZHAO Zhenjun MOUTRIE Vaughan SANTOS Daniel MCROBB Lucinda SHI Bingyan STOODLEY Marcus.A Faculty of Medicine and Health Sciences Macquarie University Genesis Cancer Care Macquarie University Hospital

Background: Our goal is to identify specific markers on the endothelial surface of human brain arteriovenous malformations（AVMs） induced by ionizing radiation that could be used as targets to site-specifically deliver thrombotic agents to block blood flow and eliminate the risk of rupture of these abnormal vessels [1]. Ionizing radiation damages cells, alters biochemical pathways and causes various changes in cellular and molecular levels. Some of the molecular changes on endothelial surface may provide novel vascular targets. In this study,we aimed to examine radiation-induced changes in the endothelial surface glycome using a lectin ***: Cultured human cerebral microvascular endothelial cells（hCMEC/D3） were irradiated at different doses（5 Gy, 15 Gy or 25 Gy） using a linear accelerator, or sham-irradiated（controls）. At day 1, 3 and 7 post-radiation,viable cells were gently harvested by 0.05% trypsin and cell suspensions incubated in the wells of the lectin microarray slides（RayBiotech, GA, USA）,which had been coated with 40 different lectins, each at a precise location. The binding of the cells with the lectins was detected under a microscope. Cell binding to a lectin means the corresponding glycan structure is expressed on the surface of the cells. The number of the cells binding to the spot area indicates the level of ***: Overall, cell binding to UEA-1, PHA-E, PHA-L, PNA, AAL, LEA,STL, MAA and DSA was detected. Radiation at 5 Gy and 15 Gy induced binding to DSA at day 1 post-irradiation, and to LEA and AAL at day 3. Binding to PHA-E and PHA-L was up-regulated at day 3 on cells that received 15 and 25 Gy ***:1. The lectin array can detect cell surface glycan expression on intact cells.2. Ionizing radiation can induce the expression of glycans that bind to DSA, LEA and AAL on the surface of brain endothelial cells.3. The radiation-induced glycan may be used as targets for radiation-guided drug delivery.

关键词： lectin array Cell surface glycan Ionizing radiation Site-specific drug delivery Endothelial cells

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Analysis of a lectin microarray identifies altered sialylation of mouse serum glycoproteins induced by whole-body radiation exposure

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JOURNAL OF RADIATION RESEARCH 2019年第2期60卷 189-196页

作者： Iizuka, Daisuke Izumi, Shunsuke Suzuki, Fumio Kamiya, Kenji Natl Inst Quantum & Radiol Sci & Technol Natl Inst Radiol Sci Dept Radiat Effects Res Inage Ku 4-9-1 Anagawa Chiba 2638555 Japan Hiroshima Univ Dept Expt Oncol Res Inst Radiat Biol & Med Minami Ku 1-2-3 Kasumi Hiroshima 7348553 Japan Hiroshima Univ Grad Sch Sci Dept Math & Life Sci 1-3-2 Kagamiyama Higashihiroshima 7398511 Japan Hiroshima Univ Dept Mol Radiobiol Res Inst Radiat Biol & Med Minami Ku 1-2-3 Kasumi Hiroshima 7348553 Japan

Microarrays containing 45 different lectins were analyzed to identify global changes in the glycosylation of serum glycoproteins from mice exposed to whole-body gamma-radiation. The results showed that radiation exposure increased and decreased the relative amounts of alpha-2,3- and alpha-2,6-sialic acids, respectively. The expression of alpha-2,3- and alpha-2,6-sialyltransferase genes in the liver was analyzed to determine whether changes in their expression were responsible for the sialic acid changes. The increase in alpha-2,3-sialic acid correlated with St3gal5 upregulation after radiation exposure;however, a decrease in St6gal1 expression was not observed. Analysis of a PCR array of genes expressed in irradiated mouse livers revealed that irradiation did not alter the expression of most of the included genes. These results suggest that glycomic screening of serum glycoproteins using lectin microarrays can be a powerful tool for identifying radiation-induced changes in the post-translational addition of sugar moieties to proteins. In addition, the results indicate that altered sialylation of glycoproteins may be an initial response to acute radiation exposure.

关键词： lectin array glycosylation adipsin sialic acid sialyltransferase

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Carbohydrates analysis in herbal glycomics

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TRAC-TRENDS IN ANALYTICAL CHEMISTRY 2013年 52卷 155-169页

作者： Li, Shao-ping Wu, Ding-tao Lv, Guang-ping Zhao, Jing State Key Laboratory of Quality Research in Chinese Medicine Institute of Chinese Medical Sciences University of Macau Macao SAR China

Herbs serve primary healthcare needs and some herbs are widely used as functional foods. Analysis of carbohydrates is essential to understand their structure-function relationships in food science and herbal medicine. However, accurately defining chemical structures of glycans is a challenge due to their chemical heterogeneity and diversity. We review and discuss carbohydrates as new functional ingredients in herbs and functional foods, and their analysis, a novel aspect in quality control and herbal glycomics. (c) 2013 Elsevier Ltd. All rights reserved.

关键词： Atomic force microscopy (AFM) Carbohydrate Chromatography Functional food Herbal glycomics Herbal ingredient lectin array Mass spectrometry (MS) Multiple-angle laser-light scattering (MALLS) Quality control (QC)

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Interrogation of Milk-Driven Changes to the Proteome of Intestinal Epithelial Cells by Integrated Proteomics and Glycomics

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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 2019年第7期67卷 1902-1917页

作者： Morrin, Sinead T. Owens, Rebecca A. Le Berre, Marie Gerlach, Jared Q. Joshi, Lokesh Bode, Lars Irwin, Jane A. Hickey, Rita M. Teagasc Food Res Ctr Moorepk Fermoy P61C996 Cork Ireland Maynooth Univ Dept Biol Maynooth W23 F2H6 Kildare Ireland Natl Univ Ireland Galway Glycosci Grp Natl Ctr Biomed Engn Sci Adv Glycosci Res Cluster Galway H91TK33 Ireland Univ Calif San Diego Dept Pediat La Jolla CA 92093 USA Univ Calif San Diego Larsson Rosenquist Fdn Mother Milk Infant Ctr Res Excellence La Jolla CA 92093 USA Univ Coll Dublin Sch Vet Med Vet Sci Ctr Dublin D04 V1W8 4 Ireland

Bovine colostrum is a rich source of bioactive components which are important in the development of the intestine, in stimulating gut structure and function and in preparing the gut surface for subsequent colonization of microbes. What is not clear, however, is how colostrum may affect the repertoire of receptors and membrane proteins of the intestinal surface and the post-translational modifications associated with them. In the present work, we aimed to characterize the surface receptor and glycan profile of human HT-29 intestinal cells after exposure to a bovine colostrum fraction (BCF) by means of proteomic and glycomic analyses. Integration of label-free quantitative proteomic analysis and lectin array profiles confirmed that BCF exposure results in changes in the levels of glycoproteins present at the cell surface and also changes to their glycosylation pattern. This study contributes to our understanding of how milk components may regulate intestinal cells and prime them for bacterial interaction.

关键词： bovine colostrum proteome receptor glycomics lectin array milk

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Cancer stem cell marker glycosylation: Nature, function and significance

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GLYCOCONJUGATE JOURNAL 2017年第4期34卷 441-452页

作者： Mallard, Brody W. Tiralongo, Joe Griffith Univ Inst Glyc Gold Coast Campus Gold Coast Qld 4222 Australia

Glycans are essential for the maintenance of normal biological function, with alterations in glycan expression being a hallmark of cancer. Cancer stem cells (CSCs) are a subset of cells within a tumour capable of self-renewal, cellular differentiation and resistances to conventional therapies. As is the case with stem cells, marker proteins present on the cell surface are frequently used to identify and enrich CSCs, with the expression of these markers statistical correlating with the likelihood of cancer recurrence and overall patient survival. As such CSC markers are of high clinical relevance. The majority of markers currently used to identify CSC populations are glycoproteins, and although the diverse biological roles for many of these markers are known, the nature and function of the glycan moiety on these glycoproteins remains to be fully elucidated. This mini-review summarises our current knowledge regarding the types and extent of CSC marker glycosylation, and the various roles that these glycans play in CSC biology, including in mediating cell adhesion, metastasis, evading apoptosis, tear shear resistance, tumour growth, maintaining pluripotency, self-renewal, trafficking, maintaining stability, maintaining enzymatic activity and aiding epithelial mesenchymal transitioning. Given that CSCs markers have multiple diverse biological functions, and are potentially of significant diagnostic and therapeutic benefit the search for new markers that are uniquely expressed on CSCs is vital to selectively target/identify this subset of cancer cells. As such we have also outlined how high-throughput lectin microarrays can be used to successfully profile the glycosylation status of CSC and to identify glyco-markers unique to CSCs.

关键词： Cancer Cancer stem cells Cancer stem cell markers CD44 CD133 Glycosylation Glycoproteins lectin array

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A Systems Biology Approach Identifies FUT8 as a Driver of Melanoma Metastasis

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CANCER CELL 2017年第6期31卷 804-+页

作者： Agrawal, Praveen Fontanals-Cirera, Barbara Sokolova, Elena Jacob, Samson Vaiana, Christopher A. Argibay, Diana Davalos, Veronica McDermott, Meagan Nayak, Shruti Darvishian, Farbod Castillo, Mireia Ueberheide, Beatrix Osman, Iman Fenyo, David Mahal, Lara K. Hernando, Eva NYU Sch Med Dept Pathol New York NY 10016 USA NYU Sch Med Perlmutter Canc Ctr Interdisciplinary Melanoma Cooperat Grp New York NY 10016 USA NYU Dept Chem Inst Biomed Chem New York NY 10003 USA NYU Sch Med Dept Biochem & Mol Pharmacol New York NY 10016 USA NYU Sch Med Inst Syst Genet New York NY 10016 USA NYU Sch Med Dept Dermatol New York NY 10016 USA Mt Sinai Hlth Syst Icahn Sch Med Mt Sinai Dept Pathol New York NY 10029 USA

Association of aberrant glycosylation with melanoma progression is based mainly on analyses of cell lines. Here we present a systems-based study of glycomic changes and corresponding enzymes associated with melanoma metastasis in patient samples. Upregulation of core fucosylation (FUT8) and downregulation of alpha-1,2 fucosylation (FUT1, FUT2) were identified as features of metastatic melanoma. Using both in vitro and in vivo studies, we demonstrate FUT8 is a driver of melanoma metastasis which, when silenced, suppresses invasion and tumor dissemination. Glycoprotein targets of FUT8 were enriched in cell migration proteins including the adhesion molecule L1CAM. Core fucosylation impacted L1CAM cleavage and the ability of L1CAM to support melanoma invasion. FUT8 and its targets represent therapeutic targets in melanoma metastasis.

关键词： primary melanoma metastatic melanoma glycosylation lectin microarray lectin array core fucosylation metastasis glycomics FUT8 L1CAM

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