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  1. Article ; Online: Glycoengineering human neural stem cells (hNSCs) for adhesion improvement using a novel thiol-modified N-acetylmannosamine (ManNAc) analog.

    Du, Jian / Liu, Xiao / Yarema, Kevin J / Jia, Xiaofeng

    Biomaterials advances

    2022  Volume 134, Page(s) 112675

    Abstract: This study sets the stage for the therapeutic use of ... ...

    Abstract This study sets the stage for the therapeutic use of Ac
    MeSH term(s) Collagen ; Fibronectins ; Hexosamines ; Humans ; Laminin/pharmacology ; Neural Stem Cells/metabolism ; Sulfhydryl Compounds
    Chemical Substances Fibronectins ; Hexosamines ; Laminin ; Sulfhydryl Compounds ; Collagen (9007-34-5) ; N-acetylmannosamine (X80PR7P73R)
    Language English
    Publishing date 2022-01-21
    Publishing country Netherlands
    Document type Journal Article
    ISSN 2772-9508
    ISSN (online) 2772-9508
    DOI 10.1016/j.msec.2022.112675
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Improving Schwann Cell Differentiation from Human Adipose Stem Cells with Metabolic Glycoengineering.

    Du, Jian / Wang, Zihui / Liu, Xiao / Hu, Cecilia / Yarema, Kevin J / Jia, Xiaofeng

    Cells

    2023  Volume 12, Issue 8

    Abstract: Schwann cells (SCs) are myelinating cells that promote peripheral nerve regeneration. When nerve lesions form, SCs are destroyed, ultimately hindering nerve repair. The difficulty in treating nerve repair is exacerbated due to SC's limited and slow ... ...

    Abstract Schwann cells (SCs) are myelinating cells that promote peripheral nerve regeneration. When nerve lesions form, SCs are destroyed, ultimately hindering nerve repair. The difficulty in treating nerve repair is exacerbated due to SC's limited and slow expansion capacity. Therapeutic use of adipose-derived stem cells (ASCs) is emerging in combating peripheral nerve injury due to these cells' SC differentiation capability and can be harvested easily in large numbers. Despite ASC's therapeutic potential, their transdifferentiation period typically takes more than two weeks. In this study, we demonstrate that metabolic glycoengineering (MGE) technology enhances ASC differentiation into SCs. Specifically, the sugar analog Ac
    MeSH term(s) Humans ; Adipocytes ; Schwann Cells ; Peripheral Nerves ; Cell Differentiation/physiology ; Stem Cells
    Language English
    Publishing date 2023-04-19
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells12081190
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  3. Article ; Online: Protocol Considerations for In Vitro Metabolic Glycoengineering of Non-Natural Glycans.

    Dammen-Brower, Kris / Tan, Elaine / Almaraz, Ruben T / Du, Jian / Yarema, Kevin J

    Current protocols

    2023  Volume 3, Issue 6, Page(s) e822

    Abstract: Metabolic glycoengineering (MGE) refers to a technique where non-natural monosaccharide analogs are introduced into living biological systems. Once inside a cell, these compounds intercept a targeted biosynthetic glycosylation pathway and in turn are ... ...

    Abstract Metabolic glycoengineering (MGE) refers to a technique where non-natural monosaccharide analogs are introduced into living biological systems. Once inside a cell, these compounds intercept a targeted biosynthetic glycosylation pathway and in turn are metabolically incorporated into cell-surface-displayed oligosaccharides, where they can modulate a host of biological activities or be exploited as tags for bioorthogonal and chemoselective ligation reactions. Over the past decade, azido-modified monosaccharides have become the go-to analogs for MGE; at the same time, analogs with novel chemical functionalities continue to be developed. Therefore, one emphasis of this article is to describe a general approach for analog selection and then provide protocols to ensure safe and efficacious analog usage by cells. Once cell-surface glycans have been successfully remodeled by MGE methodology, the stage is set for probing changes to the myriad cellular responses modulated by these versatile molecules. This manuscript concludes by detailing how one of these detection methods-flow cytometry-can be successfully utilized to quantify MGE analog incorporation and set the stage for numerous follow-up applications. © 2023 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Incubation of cells with sugar analogs Support Protocol: Routine growth and maintenance of Jurkat cells Basic Protocol 2: Cell viability assays Basic Protocol 3: Periodate-resorcinol assay to measure analog uptake and incorporation into metabolic pathways Basic Protocol 4: Quantitation of cell-surface glycoconjugates.
    MeSH term(s) Humans ; Polysaccharides/metabolism ; Monosaccharides ; Glycosylation ; Structure-Activity Relationship ; Oligosaccharides
    Chemical Substances Polysaccharides ; Monosaccharides ; Oligosaccharides
    Language English
    Publishing date 2023-04-15
    Publishing country United States
    Document type Journal Article
    ISSN 2691-1299
    ISSN (online) 2691-1299
    DOI 10.1002/cpz1.822
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  4. Article ; Online: Glycoengineering Human Neural and Adipose Stem Cells with Novel Thiol-Modified

    Du, Jian / Agatemor, Christian / Saeui, Christopher T / Bhattacharya, Rahul / Jia, Xiaofeng / Yarema, Kevin J

    Cells

    2021  Volume 10, Issue 2

    Abstract: This report describes novel thiol- ... ...

    Abstract This report describes novel thiol-modified
    MeSH term(s) Adipocytes/metabolism ; Cell Differentiation/physiology ; Glycoconjugates/metabolism ; Hexosamines/metabolism ; Humans ; N-Acetylneuraminic Acid/metabolism ; Stem Cells/metabolism ; Sulfhydryl Compounds/metabolism
    Chemical Substances Glycoconjugates ; Hexosamines ; Sulfhydryl Compounds ; N-Acetylneuraminic Acid (GZP2782OP0) ; N-acetylmannosamine (X80PR7P73R)
    Language English
    Publishing date 2021-02-12
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells10020377
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Strategies for Glycoengineering Therapeutic Proteins.

    Dammen-Brower, Kris / Epler, Paige / Zhu, Stanley / Bernstein, Zachary J / Stabach, Paul R / Braddock, Demetrios T / Spangler, Jamie B / Yarema, Kevin J

    Frontiers in chemistry

    2022  Volume 10, Page(s) 863118

    Abstract: Almost all therapeutic proteins are glycosylated, with the carbohydrate component playing a long-established, substantial role in the safety and pharmacokinetic properties of this dominant category of drugs. In the past few years and moving forward, ... ...

    Abstract Almost all therapeutic proteins are glycosylated, with the carbohydrate component playing a long-established, substantial role in the safety and pharmacokinetic properties of this dominant category of drugs. In the past few years and moving forward, glycosylation is increasingly being implicated in the pharmacodynamics and therapeutic efficacy of therapeutic proteins. This article provides illustrative examples of drugs that have already been improved through glycoengineering including cytokines exemplified by erythropoietin (EPO), enzymes (ectonucleotide pyrophosphatase 1, ENPP1), and IgG antibodies (e.g., afucosylated Gazyva
    Language English
    Publishing date 2022-04-13
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2711776-5
    ISSN 2296-2646
    ISSN 2296-2646
    DOI 10.3389/fchem.2022.863118
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  6. Article: Exploiting metabolic glycoengineering to advance healthcare.

    Agatemor, Christian / Buettner, Matthew J / Ariss, Ryan / Muthiah, Keerthana / Saeui, Christopher T / Yarema, Kevin J

    Nature reviews. Chemistry

    2019  Volume 3, Issue 10, Page(s) 605–620

    Abstract: Metabolic glycoengineering (MGE) is a technique for manipulating cellular metabolism to modulate glycosylation. MGE is used to increase the levels of natural glycans and, more importantly, to install non-natural monosaccharides into glycoconjugates. In ... ...

    Abstract Metabolic glycoengineering (MGE) is a technique for manipulating cellular metabolism to modulate glycosylation. MGE is used to increase the levels of natural glycans and, more importantly, to install non-natural monosaccharides into glycoconjugates. In this Review, we summarize the chemistry underlying MGE that has been developed over the past three decades and highlight several recent advances that have set the stage for clinical translation. In anticipation of near-term application to human healthcare, we describe emerging efforts to deploy MGE in diverse applications, ranging from the glycoengineering of biotherapeutic proteins and the diagnosis and treatment of complex diseases such as cancer to the development of new immunotherapies.
    Language English
    Publishing date 2019-09-06
    Publishing country England
    Document type Journal Article
    ISSN 2397-3358
    ISSN 2397-3358
    DOI 10.1038/s41570-019-0126-y
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  7. Article ; Online: Anticancer Properties of Hexosamine Analogs Designed to Attenuate Metabolic Flux through the Hexosamine Biosynthetic Pathway.

    Saeui, Christopher T / Shah, Sagar R / Fernandez-Gil, Beatriz I / Zhang, Cissy / Agatemor, Christian / Dammen-Brower, Kris / Mathew, Mohit P / Buettner, Matthew / Gowda, Prateek / Khare, Pratik / Otamendi-Lopez, Andrea / Yang, Shuang / Zhang, Hui / Le, Anne / Quinoñes-Hinojosa, Alfredo / Yarema, Kevin J

    ACS chemical biology

    2023  Volume 18, Issue 1, Page(s) 151–165

    Abstract: Altered cellular metabolism is a hallmark of cancer pathogenesis and progression; for example, a near-universal feature of cancer is increased metabolic flux through the hexosamine biosynthetic pathway (HBP). This pathway produces uridine ... ...

    Abstract Altered cellular metabolism is a hallmark of cancer pathogenesis and progression; for example, a near-universal feature of cancer is increased metabolic flux through the hexosamine biosynthetic pathway (HBP). This pathway produces uridine diphosphate
    MeSH term(s) Animals ; Biosynthetic Pathways ; Hexosamines/metabolism ; Pancreatic Neoplasms ; Antineoplastic Agents/pharmacology ; Glucose/metabolism ; Uridine Diphosphate/metabolism ; Acetylglucosamine/metabolism ; Pancreatic Neoplasms
    Chemical Substances Hexosamines ; Antineoplastic Agents ; Glucose (IY9XDZ35W2) ; Uridine Diphosphate (58-98-0) ; Acetylglucosamine (V956696549)
    Language English
    Publishing date 2023-01-10
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.2c00784
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: A versatile design platform for glycoengineering therapeutic antibodies.

    Ludwig, Seth D / Bernstein, Zachary J / Agatemor, Christian / Dammen-Brower, Kris / Ruffolo, Jeffrey / Rosas, Jonah M / Post, Jeremy D / Cole, Robert N / Yarema, Kevin J / Spangler, Jamie B

    mAbs

    2022  Volume 14, Issue 1, Page(s) 2095704

    Abstract: Manipulation of glycosylation patterns, i.e., glycoengineering, is incorporated in the therapeutic antibody development workflow to ensure clinical safety, and this approach has also been used to modulate the biological activities, functions, or ... ...

    Abstract Manipulation of glycosylation patterns, i.e., glycoengineering, is incorporated in the therapeutic antibody development workflow to ensure clinical safety, and this approach has also been used to modulate the biological activities, functions, or pharmacological properties of antibody drugs. Whereas most existing glycoengineering strategies focus on the canonical glycans found in the constant domain of immunoglobulin G (IgG) antibodies, we report a new strategy to leverage the untapped potential of atypical glycosylation patterns in the variable domains, which naturally occur in 15% to 25% of IgG antibodies. Glycosylation sites were added to the antigen-binding regions of two functionally divergent, interleukin-2-binding monoclonal antibodies. We used computational tools to rationally install various N-glycosylation consensus sequences into the antibody variable domains, creating "glycovariants" of these molecules. Strikingly, almost all the glycovariants were successfully glycosylated at their newly installed N-glycan sites, without reduction of the antibody's native function. Importantly, certain glycovariants exhibited modified activities compared to the parent antibody, showing the potential of our glycoengineering strategy to modulate biological function of antibodies involved in multi-component receptor systems. Finally, when coupled with a high-flux sialic acid precursor, a glycovariant with two installed glycosylation sites demonstrated superior in vivo half-life. Collectively, these findings validate a versatile glycoengineering strategy that introduces atypical glycosylation into therapeutic antibodies in order to improve their efficacy and, in certain instances, modulate their activity early in the drug development process.
    MeSH term(s) Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/therapeutic use ; Glycosylation ; Immunoglobulin G/chemistry ; Polysaccharides/chemistry
    Chemical Substances Antibodies, Monoclonal ; Immunoglobulin G ; Polysaccharides
    Language English
    Publishing date 2022-07-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2537838-7
    ISSN 1942-0870 ; 1942-0870
    ISSN (online) 1942-0870
    ISSN 1942-0870
    DOI 10.1080/19420862.2022.2095704
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Comparison of Three Glycoproteomic Methods for the Analysis of the Secretome of CHO Cells Treated with 1,3,4-

    Mertz, Joseph L / Sun, Shisheng / Yin, Bojiao / Hu, Yingwei / Bhattacharya, Rahul / Bettenbaugh, Michael J / Yarema, Kevin J / Zhang, Hui

    Bioengineering (Basel, Switzerland)

    2020  Volume 7, Issue 4

    Abstract: Comprehensive analysis of the glycoproteome is critical due to the importance of glycosylation to many aspects of protein function. The tremendous complexity of this post-translational modification, however, makes it difficult to adequately characterize ... ...

    Abstract Comprehensive analysis of the glycoproteome is critical due to the importance of glycosylation to many aspects of protein function. The tremendous complexity of this post-translational modification, however, makes it difficult to adequately characterize the glycoproteome using any single method. To overcome this pitfall, in this report we compared three glycoproteomic analysis methods; first the recently developed N-linked glycans and glycosite-containing peptides (NGAG) chemoenzymatic method, second, solid-phase extraction of N-linked glycoproteins (SPEG), and third, hydrophilic interaction liquid chromatography (HILIC) by characterizing N-linked glycosites in the secretome of Chinese hamster ovary (CHO) cells. Interestingly, the glycosites identified by SPEG and HILIC overlapped considerably whereas NGAG identified many glycosites not observed in the other two methods. Further, utilizing enhanced intact glycopeptide identification afforded by the NGAG workflow, we found that the sugar analog 1,3,4-
    Language English
    Publishing date 2020-11-10
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2746191-9
    ISSN 2306-5354
    ISSN 2306-5354
    DOI 10.3390/bioengineering7040144
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Book: Handbook of carbohydrate engineering

    Yarema, Kevin J

    2005  

    Author's details edited by Kevin J. Yarema
    Keywords Carbohydrates/Biotechnology ; Carbohydrates/Research/Methodology
    Language English
    Size xxiii, 904 p. :, ill. ;, 24 cm.
    Publisher Taylor & Francis
    Publishing place Boca Raton
    Document type Book
    ISBN 1574444727 ; 9781574444728
    Database NAL-Catalogue (AGRICOLA)

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