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  1. Book ; Conference proceedings: Mitochondria and oxidative stress in neurodegenerative disorders

    Gibson, Gary E.

    [result of a Conference Entitled Mitochondria and Oxidative Stress in Neurodegenerative Disorders, held on September 26 - 29, 2007 at the New York Academy of Sciences]

    (Annals of the New York Academy of Sciences ; 1147)

    2008  

    Event/congress Conference Entitled Mitochondria and Oxidative Stress in Neurodegenerative Disorders (2007, NewYorkNY)
    Author's details ed. by Gary E. Gibson
    Series title Annals of the New York Academy of Sciences ; 1147
    Collection
    Keywords Neurodegenerative Diseases / physiopathology ; Mitochondria / physiology ; Oxidative Stress / physiology
    Language English
    Size XII, 414 S. : Ill., graph. Darst.
    Publisher Blackwell
    Publishing place Boston, Mass
    Publishing country United States
    Document type Book ; Conference proceedings
    HBZ-ID HT015794638
    ISBN 978-1-57331-713-9 ; 1-57331-713-6
    Database Catalogue ZB MED Medicine, Health

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  2. Article ; Online: The α-Ketoglutarate Dehydrogenase Complex as a Hub of Plasticity in Neurodegeneration and Regeneration.

    Hansen, Grace E / Gibson, Gary E

    International journal of molecular sciences

    2022  Volume 23, Issue 20

    Abstract: Abnormal glucose metabolism is central to neurodegeneration, and considerable evidence suggests that abnormalities in key enzymes of the tricarboxylic acid (TCA) cycle underlie the metabolic deficits. Significant recent advances in the role of metabolism ...

    Abstract Abnormal glucose metabolism is central to neurodegeneration, and considerable evidence suggests that abnormalities in key enzymes of the tricarboxylic acid (TCA) cycle underlie the metabolic deficits. Significant recent advances in the role of metabolism in cancer provide new insight that facilitates our understanding of the role of metabolism in neurodegeneration. Research indicates that the rate-limiting step of the TCA cycle, the α-ketoglutarate dehydrogenase complex (KGDHC) and its substrate alpha ketoglutarate (KG), serve as a signaling hub that regulates multiple cellular processes: (1) is the rate-limiting step of the TCA cycle, (2) is sensitive to reactive oxygen species (ROS) and produces ROS, (3) determines whether KG is used for energy or synthesis of compounds to support growth, (4) regulates the cellular responses to hypoxia, (5) controls the post-translational modification of hundreds of cell proteins in the mitochondria, cytosol, and nucleus through succinylation, (6) controls critical aspects of transcription, (7) modulates protein signaling within cells, and (8) modulates cellular calcium. The primary focus of this review is to understand how reductions in KGDHC are translated to pathologically important changes that underlie both neurodegeneration and cancer. An understanding of each role is necessary to develop new therapeutic strategies to treat neurodegenerative disease.
    MeSH term(s) Humans ; Ketoglutarate Dehydrogenase Complex/metabolism ; Neurodegenerative Diseases/metabolism ; Reactive Oxygen Species/metabolism ; Calcium/metabolism ; Ketoglutaric Acids ; Glucose ; Tricarboxylic Acids
    Chemical Substances Ketoglutarate Dehydrogenase Complex (EC 1.2.4.2) ; Reactive Oxygen Species ; Calcium (SY7Q814VUP) ; Ketoglutaric Acids ; Glucose (IY9XDZ35W2) ; Tricarboxylic Acids
    Language English
    Publishing date 2022-10-17
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms232012403
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Succinylation Links Metabolism to Protein Functions.

    Yang, Yun / Gibson, Gary E

    Neurochemical research

    2019  Volume 44, Issue 10, Page(s) 2346–2359

    Abstract: Post-translational modifications (PTMs) are important regulators of protein function, and integrate metabolism with physiological and pathological processes. Phosphorylation and acetylation are particularly well studied PTMs. A relatively recently ... ...

    Abstract Post-translational modifications (PTMs) are important regulators of protein function, and integrate metabolism with physiological and pathological processes. Phosphorylation and acetylation are particularly well studied PTMs. A relatively recently discovered novel PTM is succinylation in which metabolically derived succinyl CoA modifies protein lysine groups. Succinylation causes a protein charge flip from positive to negative and a relatively large increase in mass compared to other PTMs. Hundreds of protein succinylation sites are present in proteins of multiple tissues and species, and the significance is being actively investigated. The few completed studies demonstrate that succinylation alters rates of enzymes and pathways, especially mitochondrial metabolic pathways. Thus, succinylation provides an elegant and efficient mechanism to coordinate metabolism and signaling by utilizing metabolic intermediates as sensors to regulate metabolism. Even though the brain is one of the most metabolically active organs, an understanding of the role succinylation in the nervous system is largely unknown. Data from other tissues and other PTMs suggest that succinylation provides a coupling between metabolism and protein function in the nervous system and in neurological diseases. This review provides a new insight into metabolism in neurological diseases and suggests that the drug development for these diseases requires a better understanding of succinylation and de-succinylation in the brain and other tissues.
    MeSH term(s) Acyl Coenzyme A/metabolism ; Animals ; Humans ; Lysine/metabolism ; Metabolic Networks and Pathways/physiology ; Mitochondria/metabolism ; Protein Processing, Post-Translational/physiology ; Proteome/metabolism
    Chemical Substances Acyl Coenzyme A ; Proteome ; succinyl-coenzyme A (BSI27HW5EQ) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2019-03-22
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 199335-5
    ISSN 1573-6903 ; 0364-3190
    ISSN (online) 1573-6903
    ISSN 0364-3190
    DOI 10.1007/s11064-019-02780-x
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  4. Article: Pharmacological thiamine levels as a therapeutic approach in Alzheimer's disease.

    Gibson, Gary E / Feldman, Howard H / Zhang, Sheng / Flowers, Sarah A / Luchsinger, José A

    Frontiers in medicine

    2022  Volume 9, Page(s) 1033272

    Abstract: of the study. ...

    Abstract of the study.
    Language English
    Publishing date 2022-10-04
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2775999-4
    ISSN 2296-858X
    ISSN 2296-858X
    DOI 10.3389/fmed.2022.1033272
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  5. Article ; Online: Interactions of Mitochondria/Metabolism and Calcium Regulation in Alzheimer's Disease: A Calcinist Point of View.

    Gibson, Gary E / Thakkar, Ankita

    Neurochemical research

    2017  Volume 42, Issue 6, Page(s) 1636–1648

    Abstract: Decades of research suggest that alterations in calcium are central to the pathophysiology of Alzheimer's Disease (AD). Highly reproducible changes in calcium dynamics occur in cells from patients with both genetic and non-genetic forms of AD relative to ...

    Abstract Decades of research suggest that alterations in calcium are central to the pathophysiology of Alzheimer's Disease (AD). Highly reproducible changes in calcium dynamics occur in cells from patients with both genetic and non-genetic forms of AD relative to controls. The most robust change is an exaggerated release of calcium from internal stores. Detailed analysis of these changes in animal and cell models of the AD-causing presenilin mutations reveal robust changes in ryanodine receptors, inositol tris-phosphate receptors, calcium leak channels and store activated calcium entry. Similar anomalies in calcium result when AD-like changes in mitochondrial enzymes or oxidative stress are induced experimentally. The calcium abnormalities can be directly linked to the altered tau phosphorylation, amyloid precursor protein processing and synaptic dysfunction that are defining features of AD. A better understanding of these changes is required before using calcium abnormalities as therapeutic targets.
    MeSH term(s) Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Calcium/physiology ; Calcium Channels/genetics ; Calcium Channels/metabolism ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Humans ; Mitochondria/genetics ; Mitochondria/metabolism ; Oxidative Stress/physiology
    Chemical Substances Calcium Channels ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2017-02-08
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 199335-5
    ISSN 1573-6903 ; 0364-3190
    ISSN (online) 1573-6903
    ISSN 0364-3190
    DOI 10.1007/s11064-017-2182-3
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  6. Article ; Online: Mitochondria/metabolic reprogramming in the formation of neurons from peripheral cells: Cause or consequence and the implications to their utility.

    Gibson, Gary E / Thakkar, Ankita

    Neurochemistry international

    2017  Volume 117, Page(s) 65–76

    Abstract: The induction of pluripotent stem cells (iPSC) from differentiated cells such as fibroblasts and their subsequent conversion to neural progenitor cells (NPC) and finally to neurons is intriguing scientifically, and its potential to medicine is nearly ... ...

    Abstract The induction of pluripotent stem cells (iPSC) from differentiated cells such as fibroblasts and their subsequent conversion to neural progenitor cells (NPC) and finally to neurons is intriguing scientifically, and its potential to medicine is nearly infinite, but unrealized. A better understanding of the changes at each step of the transformation will enable investigators to better model neurological disease. Each step of conversion from a differentiated cell to an iPSC to a NPC to neurons requires large changes in glycolysis including aerobic glycolysis, the pentose shunt, the tricarboxylic acid cycle, the electron transport chain and in the production of reactive oxygen species (ROS). These mitochondrial/metabolic changes are required and their manipulation modifies conversions. These same mitochondrial/metabolic processes are altered in common neurological diseases so that factors related to the disease may alter the cellular transformation at each step including the final phenotype. A lack of understanding of these interactions could compromise the validity of the disease comparisons in iPSC derived neurons. Both the complexity and potential of iPSC derived cells for understanding and treating disease remain great.
    MeSH term(s) Animals ; Cell Differentiation/physiology ; Cellular Reprogramming/physiology ; Humans ; Induced Pluripotent Stem Cells/metabolism ; Mitochondria/metabolism ; Neural Stem Cells/metabolism ; Neurons/metabolism ; Reactive Oxygen Species/metabolism
    Chemical Substances Reactive Oxygen Species
    Language English
    Publishing date 2017-06-13
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 283190-9
    ISSN 1872-9754 ; 0197-0186
    ISSN (online) 1872-9754
    ISSN 0197-0186
    DOI 10.1016/j.neuint.2017.06.007
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  7. Article ; Online: Serum Metabolomic and Lipidomic Profiling Reveals Novel Biomarkers of Efficacy for Benfotiamine in Alzheimer's Disease.

    Bhawal, Ruchika / Fu, Qin / Anderson, Elizabeth T / Gibson, Gary E / Zhang, Sheng

    International journal of molecular sciences

    2021  Volume 22, Issue 24

    Abstract: Serum metabolomics and lipidomics are powerful approaches for discovering unique biomarkers in various diseases and associated therapeutics and for revealing metabolic mechanisms of both. Treatment with Benfotiamine (BFT), a thiamine prodrug, for one ... ...

    Abstract Serum metabolomics and lipidomics are powerful approaches for discovering unique biomarkers in various diseases and associated therapeutics and for revealing metabolic mechanisms of both. Treatment with Benfotiamine (BFT), a thiamine prodrug, for one year produced encouraging results for patients with mild cognitive impairment and mild Alzheimer's disease (AD). In this study, a parallel metabolomics and lipidomics approach was applied for the first exploratory investigation on the serum metabolome and lipidome of patients treated with BFT. A total of 315 unique metabolites and 417 lipids species were confidently identified and relatively quantified. Rigorous statistical analyses revealed significant differences between the placebo and BFT treatment groups in 25 metabolites, including thiamine, tyrosine, tryptophan, lysine, and 22 lipid species, mostly belonging to phosphatidylcholines. Additionally, 10 of 11 metabolites and 14 of 15 lipid species reported in previous literature to follow AD progression changed in the opposite direction to those reported to reflect AD progression. Enrichment and pathway analyses show that significantly altered metabolites by BFT are involved in glucose metabolism and biosynthesis of aromatic amino acids. Our study discovered that multiple novel biomarkers and multiple mechanisms that may underlie the benefit of BFT are potential therapeutic targets in AD and should be validated in studies with larger sample sizes.
    MeSH term(s) Alzheimer Disease/blood ; Alzheimer Disease/drug therapy ; Biomarkers/blood ; Case-Control Studies ; Chromatography, Liquid ; Humans ; Lipids/blood ; Mass Spectrometry ; Metabolic Networks and Pathways ; Metabolomics/methods ; Pilot Projects ; Thiamine/administration & dosage ; Thiamine/analogs & derivatives ; Thiamine/pharmacology
    Chemical Substances Biomarkers ; Lipids ; Thiamine (X66NSO3N35) ; benphothiamine (Y92OUS2H9B)
    Language English
    Publishing date 2021-12-07
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms222413188
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  8. Article: Foreword.

    Gibson, Gary E

    Neurochemical research

    2007  Volume 32, Issue 4-5, Page(s) 533–534

    MeSH term(s) Brain Chemistry ; Dementia/therapy ; Geriatrics/history ; History, 20th Century ; History, 21st Century ; Neurology/history ; United States
    Language English
    Publishing date 2007-04
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article ; Portraits
    ZDB-ID 199335-5
    ISSN 1573-6903 ; 0364-3190
    ISSN (online) 1573-6903
    ISSN 0364-3190
    DOI 10.1007/s11064-007-9298-9
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  9. Article ; Online: The human brain acetylome reveals that decreased acetylation of mitochondrial proteins associates with Alzheimer's disease.

    Sun, Lidan / Bhawal, Ruchika / Xu, Hui / Chen, Huanlian / Anderson, Elizabeth T / Haroutunian, Vahrum / Cross, Abigail C / Zhang, Sheng / Gibson, Gary E

    Journal of neurochemistry

    2021  Volume 158, Issue 2, Page(s) 282–296

    Abstract: Metabolic changes that correlate to cognitive changes are well-known in Alzheimer's disease (AD). Metabolism is often linked to functional changes in proteins by post-translational modifications. The importance of the regulation of transcription by ... ...

    Abstract Metabolic changes that correlate to cognitive changes are well-known in Alzheimer's disease (AD). Metabolism is often linked to functional changes in proteins by post-translational modifications. The importance of the regulation of transcription by acetylation is well documented. Advanced mass spectrometry reveals hundreds of acetylated proteins in multiple tissues, but the acetylome of human brain, its functional significance, and the changes with disease are unknown. Filling this gap is critical for understanding the pathophysiology and development of therapies. To fill this gap, we assessed the human brain acetylome in human brain and its changes with AD. More than 5% of the 4,442 proteins from the human brain global proteome were acetylated. Acetylated proteins were primarily found in the cytosol (148), mitochondria (100), nucleus (91), and plasma membrane (58). The comparison of the brain acetylome in controls to that of patients with AD revealed striking and selective differences in terms of its abundances of acetylated peptides/sites. Acetylation of 18 mitochondrial proteins decreased, while acetylation of two cytosolic proteins, tau and GFAP, increased. Our experiments demonstrate that acetylation at some specific lysine sites alters enzyme function. The results indicate that general activation of de-acetylases (i.e., sirtuins) is not an appropriate therapeutic approach for AD.
    MeSH term(s) Acetylation ; Aged ; Aged, 80 and over ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Brain Chemistry ; Computational Biology ; Female ; Glial Fibrillary Acidic Protein/metabolism ; Humans ; Ketoglutarate Dehydrogenase Complex/metabolism ; Lysine/metabolism ; Male ; Metabolome/genetics ; Mitochondrial Proteins/metabolism ; Protein Processing, Post-Translational ; Pyruvate Dehydrogenase Complex/metabolism ; Subcellular Fractions/metabolism ; tau Proteins/metabolism
    Chemical Substances GFAP protein, human ; Glial Fibrillary Acidic Protein ; MAPT protein, human ; Mitochondrial Proteins ; Pyruvate Dehydrogenase Complex ; tau Proteins ; Ketoglutarate Dehydrogenase Complex (EC 1.2.4.2) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2021-05-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/jnc.15377
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  10. Article ; Online: Up-regulation of the mitochondrial malate dehydrogenase by oxidative stress is mediated by miR-743a.

    Shi, Qingli / Gibson, Gary E

    Journal of neurochemistry

    2011  Volume 118, Issue 3, Page(s) 440–448

    Abstract: These experiments reveal for the first time that microRNAs (miRNAs) mediate oxidant regulated expression of a mitochondrial tricarboxylic acid cycle gene (mdh2). mdh2 encoded malate dehydrogenase (MDH) is elevated by an unknown mechanism in brains of ... ...

    Abstract These experiments reveal for the first time that microRNAs (miRNAs) mediate oxidant regulated expression of a mitochondrial tricarboxylic acid cycle gene (mdh2). mdh2 encoded malate dehydrogenase (MDH) is elevated by an unknown mechanism in brains of patients that died with Alzheimer's disease. Oxidative stress, an early and pervasive event in Alzheimer's disease, increased MDH activity and mRNA level of mdh2 by 19% and 22%, respectively, in a mouse hippocampal cell line (HT22). Post-transcriptional events underlie the change in mRNA because actinomycin D did not block the elevated mdh2 mRNA. Since miRNAs regulate gene expression post-transcriptionally, the expression of miR-743a, a miRNA predicted to target mdh2, was determined and showed a 52% reduction after oxidant treatment. Direct interaction of miR-743a with mdh2 was demonstrated with a luciferase based assay. Over-expression or inhibition of miR-743a led to a respective reduction or increase in endogenous mRNA and MDH activity. The results demonstrate that miR-743a negatively regulates mdh2 at post-transcriptional level by directly targeting the mdh2 3'UTR. The findings are consistent with the suggestion that oxidative stress can elevate the activity of MDH through miR-743a, and provide new insights into possible roles of miRNA in oxidative stress and neurodegeneration.
    MeSH term(s) 3' Untranslated Regions/genetics ; Animals ; Brain Chemistry/physiology ; Cell Line ; Enzyme Activation/drug effects ; Gene Targeting ; Hippocampus/drug effects ; Hippocampus/enzymology ; Hydrogen Peroxide/metabolism ; Luciferases/metabolism ; Malate Dehydrogenase/biosynthesis ; Malate Dehydrogenase/metabolism ; Mice ; Mice, 129 Strain ; MicroRNAs/pharmacology ; Mitochondria/enzymology ; Oxidative Stress/physiology ; Protein Processing, Post-Translational/drug effects ; Protein Processing, Post-Translational/genetics ; Transfection ; Up-Regulation
    Chemical Substances 3' Untranslated Regions ; MicroRNAs ; Mirn743 microRNA, mouse ; Hydrogen Peroxide (BBX060AN9V) ; Malate Dehydrogenase (EC 1.1.1.37) ; Luciferases (EC 1.13.12.-)
    Language English
    Publishing date 2011-06-24
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/j.1471-4159.2011.07333.x
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