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  1. Article ; Online: The multifaceted role of intracellular glycosylation in cytoprotection and heart disease.

    Umapathi, Priya / Aggarwal, Akanksha / Zahra, Fiddia / Narayanan, Bhargavi / Zachara, Natasha E

    The Journal of biological chemistry

    2024  Volume 300, Issue 6, Page(s) 107296

    Abstract: The modification of nuclear, cytoplasmic, and mitochondrial proteins by O-linked β-N-actylglucosamine (O-GlcNAc) is an essential posttranslational modification that is common in metozoans. O-GlcNAc is cycled on and off proteins in response to ... ...

    Abstract The modification of nuclear, cytoplasmic, and mitochondrial proteins by O-linked β-N-actylglucosamine (O-GlcNAc) is an essential posttranslational modification that is common in metozoans. O-GlcNAc is cycled on and off proteins in response to environmental and physiological stimuli impacting protein function, which, in turn, tunes pathways that include transcription, translation, proteostasis, signal transduction, and metabolism. One class of stimulus that induces rapid and dynamic changes to O-GlcNAc is cellular injury, resulting from environmental stress (for instance, heat shock), hypoxia/reoxygenation injury, ischemia reperfusion injury (heart attack, stroke, trauma hemorrhage), and sepsis. Acute elevation of O-GlcNAc before or after injury reduces apoptosis and necrosis, suggesting that injury-induced changes in O-GlcNAcylation regulate cell fate decisions. However, prolonged elevation or reduction in O-GlcNAc leads to a maladaptive response and is associated with pathologies such as hypertrophy and heart failure. In this review, we discuss the impact of O-GlcNAc in both acute and prolonged models of injury with a focus on the heart and biological mechanisms that underpin cell survival.
    Language English
    Publishing date 2024-04-18
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2024.107296
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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  2. Article ; Online: Differential Detection of O-GlcNAcylated proteins in the heart using antibodies

    Narayanan, Bhargavi / Zahra, Fiddia / Reeves, Russell A. / Aggarwal, Akanksha / O'Meally, Robert N. / Henry, Roger K. / Craven, Megan / Jacobson, Avital / Cole, Robert N. / Kohr, Mark J. / Umapathi, Priya / Zachara, Natasha E.

    Analytical Biochemistry. 2023 Oct., v. 678 p.115262-

    2023  

    Abstract: Thousands of mammalian intracellular proteins are dynamically modified by O-linked β−N-acetylglucosamine (O-GlcNAc). Global changes in O-GlcNAcylation have been associated with the development of cardiomyopathy, heart failure, hypertension, and ... ...

    Abstract Thousands of mammalian intracellular proteins are dynamically modified by O-linked β−N-acetylglucosamine (O-GlcNAc). Global changes in O-GlcNAcylation have been associated with the development of cardiomyopathy, heart failure, hypertension, and neurodegenerative disease. Levels of O-GlcNAc in cells and tissues can be detected using numerous approaches; however, immunoblotting using GlcNAc-specific antibodies and lectins is commonplace. The goal of this study was to optimize the detection of O-GlcNAc in heart lysates by immunoblotting. Using a combination of tissue fractionation, immunoblotting, and galactosyltransferase labeling, as well as hearts from wild-type and O-GlcNAc transferase transgenic mice, we demonstrate that contractile proteins in the heart are differentially detected by two commercially available antibodies (CTD110.6 and RL2). As CTD110.6 displays poor reactivity toward contractile proteins, and as these proteins represent a major fraction of the heart proteome, a better assessment of cardiac O-GlcNAcylation is obtained in total tissue lysates with RL2. The data presented highlight tissue lysis approaches that should aid the assessment of the cardiac O-GlcNAcylation by immunoblotting.
    Keywords cardiomyopathy ; fractionation ; genetically modified organisms ; heart ; heart failure ; hypertension ; immunoblotting ; lectins ; mammals ; neurodegenerative diseases ; proteome ; O-GlcNAc ; Glycosylation ; Antibodies ; Click chemistry
    Language English
    Dates of publication 2023-10
    Publishing place Elsevier Inc.
    Document type Article ; Online
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2023.115262
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  3. Article ; Online: Differential Detection of O-GlcNAcylated proteins in the heart using antibodies.

    Narayanan, Bhargavi / Zahra, Fiddia / Reeves, Russell A / Aggarwal, Akanksha / O'Meally, Robert N / Henry, Roger K / Craven, Megan / Jacobson, Avital / Cole, Robert N / Kohr, Mark J / Umapathi, Priya / Zachara, Natasha E

    Analytical biochemistry

    2023  Volume 678, Page(s) 115262

    Abstract: Thousands of mammalian intracellular proteins are dynamically modified by O-linked β-N-acetylglucosamine (O-GlcNAc). Global changes in O-GlcNAcylation have been associated with the development of cardiomyopathy, heart failure, hypertension, and ... ...

    Abstract Thousands of mammalian intracellular proteins are dynamically modified by O-linked β-N-acetylglucosamine (O-GlcNAc). Global changes in O-GlcNAcylation have been associated with the development of cardiomyopathy, heart failure, hypertension, and neurodegenerative disease. Levels of O-GlcNAc in cells and tissues can be detected using numerous approaches; however, immunoblotting using GlcNAc-specific antibodies and lectins is commonplace. The goal of this study was to optimize the detection of O-GlcNAc in heart lysates by immunoblotting. Using a combination of tissue fractionation, immunoblotting, and galactosyltransferase labeling, as well as hearts from wild-type and O-GlcNAc transferase transgenic mice, we demonstrate that contractile proteins in the heart are differentially detected by two commercially available antibodies (CTD110.6 and RL2). As CTD110.6 displays poor reactivity toward contractile proteins, and as these proteins represent a major fraction of the heart proteome, a better assessment of cardiac O-GlcNAcylation is obtained in total tissue lysates with RL2. The data presented highlight tissue lysis approaches that should aid the assessment of the cardiac O-GlcNAcylation by immunoblotting.
    MeSH term(s) Mice ; Animals ; Neurodegenerative Diseases ; Antibodies/metabolism ; Proteome/metabolism ; Heart ; Contractile Proteins/metabolism ; Acetylglucosamine ; Protein Processing, Post-Translational ; Mammals/metabolism
    Chemical Substances Antibodies ; Proteome ; Contractile Proteins ; Acetylglucosamine (V956696549)
    Language English
    Publishing date 2023-07-27
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2023.115262
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 389: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine.

    Fahie, Kamau / Narayanan, Bhargavi / Zahra, Fiddia / Reeves, Russell / Fernandes, Steve M / Hart, Gerald W / Zachara, Natasha E

    Current protocols

    2021  Volume 1, Issue 5, Page(s) e129

    Abstract: O-GlcNAc is a common post-translational modification of nuclear, mitochondrial, and cytoplasmic proteins that regulates normal physiology and the cell stress response. Dysregulation of O-GlcNAc cycling is implicated in the etiology of type II diabetes, ... ...

    Abstract O-GlcNAc is a common post-translational modification of nuclear, mitochondrial, and cytoplasmic proteins that regulates normal physiology and the cell stress response. Dysregulation of O-GlcNAc cycling is implicated in the etiology of type II diabetes, heart failure, hypertension, and Alzheimer's disease, as well as cardioprotection. These protocols cover simple and comprehensive techniques for detecting proteins modified by O-GlcNAc and studying the enzymes that add or remove O-GlcNAc. © 2021 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Increasing the stoichiometry of O-GlcNAc on proteins before analysis Basic Protocol 2: Detection of proteins modified by O-GlcNAc using antibodies Basic Protocol 3: Detection of proteins modified by O-GlcNAc using the lectin sWGA Support Protocol 1: Control for O-linked glycosylation Basic Protocol 4: Detection and enrichment of proteins using WGA-agarose Support Protocol 2: Digestion of proteins with hexosaminidase Alternate Protocol: Detection of proteins modified by O-GlcNAc using galactosyltransferase Support Protocol 3: Autogalactosylation of galactosyltransferase Support Protocol 4: Assay of galactosyltransferase activity Basic Protocol 5: Characterization of labeled glycans by β-elimination and chromatography Basic Protocol 6: Detection of O-GlcNAc in 96-well plates Basic Protocol 7: Assay for OGT activity Support Protocol 5: Desalting of O-GlcNAc transferase Basic Protocol 8: Assay for O-GlcNAcase activity.
    MeSH term(s) Acetylglucosamine/metabolism ; Cell Nucleus/metabolism ; Diabetes Mellitus, Type 2/metabolism ; Glycosylation ; Humans ; Protein Processing, Post-Translational
    Chemical Substances Acetylglucosamine (V956696549)
    Language English
    Publishing date 2021-05-18
    Publishing country United States
    Document type Journal Article
    ISSN 2691-1299
    ISSN (online) 2691-1299
    DOI 10.1002/cpz1.129
    Database MEDical Literature Analysis and Retrieval System OnLINE

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