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Artikel ; 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 Band 134, Seite(n) 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-Begriff(e)	Collagen ; Fibronectins ; Hexosamines ; Humans ; Laminin/pharmacology ; Neural Stem Cells/metabolism ; Sulfhydryl Compounds
Chemische Substanzen	Fibronectins ; Hexosamines ; Laminin ; Sulfhydryl Compounds ; Collagen (9007-34-5) ; N-acetylmannosamine (X80PR7P73R)
Sprache	Englisch
Erscheinungsdatum	2022-01-21
Erscheinungsland	Netherlands
Dokumenttyp	Journal Article
ISSN	2772-9508
ISSN (online)	2772-9508
DOI	10.1016/j.msec.2022.112675
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; 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 Band 12, Heft 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-Begriff(e)	Humans ; Adipocytes ; Schwann Cells ; Peripheral Nerves ; Cell Differentiation/physiology ; Stem Cells
Sprache	Englisch
Erscheinungsdatum	2023-04-19
Erscheinungsland	Switzerland
Dokumenttyp	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
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; 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 Band 3, Heft 6, Seite(n) 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-Begriff(e)	Humans ; Polysaccharides/metabolism ; Monosaccharides ; Glycosylation ; Structure-Activity Relationship ; Oligosaccharides
Chemische Substanzen	Polysaccharides ; Monosaccharides ; Oligosaccharides
Sprache	Englisch
Erscheinungsdatum	2023-04-15
Erscheinungsland	United States
Dokumenttyp	Journal Article
ISSN	2691-1299
ISSN (online)	2691-1299
DOI	10.1002/cpz1.822
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; 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 Band 10, Heft 2

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

Abstract	This report describes novel thiol-modified
Mesh-Begriff(e)	Adipocytes/metabolism ; Cell Differentiation/physiology ; Glycoconjugates/metabolism ; Hexosamines/metabolism ; Humans ; N-Acetylneuraminic Acid/metabolism ; Stem Cells/metabolism ; Sulfhydryl Compounds/metabolism
Chemische Substanzen	Glycoconjugates ; Hexosamines ; Sulfhydryl Compounds ; N-Acetylneuraminic Acid (GZP2782OP0) ; N-acetylmannosamine (X80PR7P73R)
Sprache	Englisch
Erscheinungsdatum	2021-02-12
Erscheinungsland	Switzerland
Dokumenttyp	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
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: 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 Band 10, Seite(n) 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
Sprache	Englisch
Erscheinungsdatum	2022-04-13
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article ; Review
ZDB-ID	2711776-5
ISSN	2296-2646
ISSN	2296-2646
DOI	10.3389/fchem.2022.863118
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: 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 Band 3, Heft 10, Seite(n) 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.
Sprache	Englisch
Erscheinungsdatum	2019-09-06
Erscheinungsland	England
Dokumenttyp	Journal Article
ISSN	2397-3358
ISSN	2397-3358
DOI	10.1038/s41570-019-0126-y
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; 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 Band 18, Heft 1, Seite(n) 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-Begriff(e)	Animals ; Biosynthetic Pathways ; Hexosamines/metabolism ; Pancreatic Neoplasms ; Antineoplastic Agents/pharmacology ; Glucose/metabolism ; Uridine Diphosphate/metabolism ; Acetylglucosamine/metabolism ; Pancreatic Neoplasms
Chemische Substanzen	Hexosamines ; Antineoplastic Agents ; Glucose (IY9XDZ35W2) ; Uridine Diphosphate (58-98-0) ; Acetylglucosamine (V956696549)
Sprache	Englisch
Erscheinungsdatum	2023-01-10
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.2c00784
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; 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 Band 14, Heft 1, Seite(n) 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-Begriff(e)	Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/therapeutic use ; Glycosylation ; Immunoglobulin G/chemistry ; Polysaccharides/chemistry
Chemische Substanzen	Antibodies, Monoclonal ; Immunoglobulin G ; Polysaccharides
Sprache	Englisch
Erscheinungsdatum	2022-07-05
Erscheinungsland	United States
Dokumenttyp	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
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: 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 Band 7, Heft 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-
Sprache	Englisch
Erscheinungsdatum	2020-11-10
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article
ZDB-ID	2746191-9
ISSN	2306-5354
ISSN	2306-5354
DOI	10.3390/bioengineering7040144
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Improving Immunotherapy Through Glycodesign.

Buettner, Matthew J / Shah, Sagar R / Saeui, Christopher T / Ariss, Ryan / Yarema, Kevin J

Frontiers in immunology

2018 Band 9, Seite(n) 2485

Abstract: Immunotherapy is revolutionizing health care, with the majority of high impact "drugs" approved in the past decade falling into this category of therapy. Despite considerable success, glycosylation-a key design parameter that ensures safety, optimizes ... ...

Abstract	Immunotherapy is revolutionizing health care, with the majority of high impact "drugs" approved in the past decade falling into this category of therapy. Despite considerable success, glycosylation-a key design parameter that ensures safety, optimizes biological response, and influences the pharmacokinetic properties of an immunotherapeutic-has slowed the development of this class of drugs in the past and remains challenging at present. This article describes how optimizing glycosylation through a variety of glycoengineering strategies provides enticing opportunities to not only avoid past pitfalls, but also to substantially improve immunotherapies including antibodies and recombinant proteins, and cell-based therapies. We cover design principles important for early stage pre-clinical development and also discuss how various glycoengineering strategies can augment the biomanufacturing process to ensure the overall effectiveness of immunotherapeutics.
Mesh-Begriff(e)	Animals ; Antibodies/chemistry ; Antibodies/therapeutic use ; Biological Products/chemistry ; Biological Products/therapeutic use ; Biomedical Engineering/methods ; Drug Design ; Glycosylation ; Humans ; Immunotherapy/methods ; Immunotherapy/trends ; Quality Improvement ; Recombinant Proteins/chemistry ; Recombinant Proteins/therapeutic use
Chemische Substanzen	Antibodies ; Biological Products ; Recombinant Proteins
Sprache	Englisch
Erscheinungsdatum	2018-11-02
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2018.02485
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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