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  1. Article ; Online: Nicotinamide pathways as the root cause of sepsis - an evolutionary perspective on macrophage energetic shifts.

    Suchard, Melinda S / Savulescu, Dana M

    The FEBS journal

    2021  Volume 289, Issue 4, Page(s) 955–964

    Abstract: Divergent pathways of macrophage metabolism occur during infection, notably switching between oxidative phosphorylation and aerobic glycolysis (Warburg-like metabolism). Concurrently, macrophages shift between alternate and classical activation. A key ... ...

    Abstract Divergent pathways of macrophage metabolism occur during infection, notably switching between oxidative phosphorylation and aerobic glycolysis (Warburg-like metabolism). Concurrently, macrophages shift between alternate and classical activation. A key enzyme upregulated in alternatively activated macrophages is indoleamine 2,3-dioxygenase, which converts tryptophan to kynurenine for de novo synthesis of nicotinamide. Nicotinamide can be used to replenish cellular NAD
    MeSH term(s) Animals ; Biological Evolution ; COVID-19/complications ; Energy Metabolism ; Humans ; Macrophages/immunology ; Macrophages/metabolism ; Niacinamide/metabolism ; Sepsis/etiology ; Sepsis/metabolism
    Chemical Substances Niacinamide (25X51I8RD4)
    Language English
    Publishing date 2021-03-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.15807
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  2. Article: Nicotinamide pathways as the root cause of sepsis – an evolutionary perspective on macrophage energetic shifts

    Suchard, Melinda S. / Savulescu, Dana M.

    FEBS journal. 2022 Feb., v. 289, no. 4

    2022  

    Abstract: Divergent pathways of macrophage metabolism occur during infection, notably switching between oxidative phosphorylation and aerobic glycolysis (Warburg‐like metabolism). Concurrently, macrophages shift between alternate and classical activation. A key ... ...

    Abstract Divergent pathways of macrophage metabolism occur during infection, notably switching between oxidative phosphorylation and aerobic glycolysis (Warburg‐like metabolism). Concurrently, macrophages shift between alternate and classical activation. A key enzyme upregulated in alternatively activated macrophages is indoleamine 2,3‐dioxygenase, which converts tryptophan to kynurenine for de novo synthesis of nicotinamide. Nicotinamide can be used to replenish cellular NAD⁺ supplies. We hypothesize that an insufficient cellular NAD⁺ supply is the root cause of metabolic shifts in macrophages. We assert that manipulation of nicotinamide pathways may correct deleterious immune responses. We propose evaluation of nicotinamide (Vitamin B3) and analogues, including isoniazid, nicotinamide mononucleotide and nicotinamide riboside, as potential therapy for infectious causes of sepsis, including COVID‐19.
    Keywords COVID-19 infection ; glycolysis ; indoleamine 2,3-dioxygenase ; isoniazid ; kynurenine ; macrophages ; niacin ; nicotinamide ; oxidative phosphorylation ; therapeutics ; tryptophan
    Language English
    Dates of publication 2022-02
    Size p. 955-964.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note REVIEW
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.15807
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  3. Article: Evolutionary Views of Tuberculosis: Indoleamine 2,3‐Dioxygenase Catalyzed Nicotinamide Synthesis Reflects Shifts in Macrophage Metabolism: Indoleamine 2,3‐Dioxygenase Reflects Altered Macrophage Metabolism During Tuberculosis Pathogenesis

    Suchard, Melinda S / Adu‐Gyamfi, Clement G / Cumming, Bridgette M / Savulescu, Dana M

    BioEssays. 2020 May, v. 42, no. 5

    2020  

    Abstract: Indoleamine 2,3‐dioxygenase (IDO) is the rate‐limiting enzyme in conversion of tryptophan to kynurenines, feeding de novo nicotinamide synthesis. IDO orchestrates materno‐foetal tolerance, increasing human reproductive fitness. IDO mediates immune ... ...

    Abstract Indoleamine 2,3‐dioxygenase (IDO) is the rate‐limiting enzyme in conversion of tryptophan to kynurenines, feeding de novo nicotinamide synthesis. IDO orchestrates materno‐foetal tolerance, increasing human reproductive fitness. IDO mediates immune suppression through depletion of tryptophan required by T lymphocytes and other mechanisms. IDO is expressed by alternatively activated macrophages, suspected to play a key role in tuberculosis (TB) pathogenesis. Unlike its human host, Mycobacterium tuberculosis can synthesize tryptophan, suggesting possible benefit to the host from infection with the microbe. Intriguingly, nicotinamide analogues are used to treat TB. In reviewing this field, it is postulated that flux through the nicotinamide synthesis pathway reflects switching between aerobic glycolysis and oxidative phosphorylation in M. tuberculosis‐infected macrophages. The evolutionary cause of such shifts may be ancient mitochondrial behavior related to reproductive fitness. Evolutionary perspectives on the IDO pathway may elucidate why, after centuries of co‐existence with the Tubercle bacillus, humans still remain susceptible to TB disease.
    Keywords Mycobacterium tuberculosis ; glycolysis ; humans ; indoleamine 2,3-dioxygenase ; kynurenine ; macrophages ; mitochondria ; nicotinamide ; oxidative phosphorylation ; pathogenesis ; reproductive fitness ; tryptophan ; tuberculosis
    Language English
    Dates of publication 2020-05
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note NAL-AP-2-clean ; JOURNAL ARTICLE
    ZDB-ID 50140-2
    ISSN 1521-1878 ; 0265-9247
    ISSN (online) 1521-1878
    ISSN 0265-9247
    DOI 10.1002/bies.201900220
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  4. Article ; Online: Evolutionary Views of Tuberculosis: Indoleamine 2,3-Dioxygenase Catalyzed Nicotinamide Synthesis Reflects Shifts in Macrophage Metabolism: Indoleamine 2,3-Dioxygenase Reflects Altered Macrophage Metabolism During Tuberculosis Pathogenesis.

    Suchard, Melinda S / Adu-Gyamfi, Clement G / Cumming, Bridgette M / Savulescu, Dana M

    BioEssays : news and reviews in molecular, cellular and developmental biology

    2020  Volume 42, Issue 5, Page(s) e1900220

    Abstract: Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in conversion of tryptophan to kynurenines, feeding de novo nicotinamide synthesis. IDO orchestrates materno-foetal tolerance, increasing human reproductive fitness. IDO mediates immune ... ...

    Abstract Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in conversion of tryptophan to kynurenines, feeding de novo nicotinamide synthesis. IDO orchestrates materno-foetal tolerance, increasing human reproductive fitness. IDO mediates immune suppression through depletion of tryptophan required by T lymphocytes and other mechanisms. IDO is expressed by alternatively activated macrophages, suspected to play a key role in tuberculosis (TB) pathogenesis. Unlike its human host, Mycobacterium tuberculosis can synthesize tryptophan, suggesting possible benefit to the host from infection with the microbe. Intriguingly, nicotinamide analogues are used to treat TB. In reviewing this field, it is postulated that flux through the nicotinamide synthesis pathway reflects switching between aerobic glycolysis and oxidative phosphorylation in M. tuberculosis-infected macrophages. The evolutionary cause of such shifts may be ancient mitochondrial behavior related to reproductive fitness. Evolutionary perspectives on the IDO pathway may elucidate why, after centuries of co-existence with the Tubercle bacillus, humans still remain susceptible to TB disease.
    MeSH term(s) Catalysis ; Humans ; Indoleamine-Pyrrole 2,3,-Dioxygenase/genetics ; Macrophages ; Niacinamide ; Tuberculosis/genetics
    Chemical Substances Indoleamine-Pyrrole 2,3,-Dioxygenase ; Niacinamide (25X51I8RD4)
    Language English
    Publishing date 2020-06-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 50140-2
    ISSN 1521-1878 ; 0265-9247
    ISSN (online) 1521-1878
    ISSN 0265-9247
    DOI 10.1002/bies.201900220
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2024: Show issues Location:
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    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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  5. Article ; Online: Alloimmunity to Class 2 Human Leucocyte Antigens May Reduce HIV-1 Acquisition - A Nested Case-Control Study in HIV-1 Serodiscordant Couples.

    Suchard, Melinda S / Martinson, Neil / Malfeld, Susan / de Assis Rosa, Debbie / Mackelprang, Romel D / Lingappa, Jairam / Hou, Xuanlin / Rees, Helen / Delany-Moretlwe, Sinead / Goldfein, Hadassa / Ranchod, Heena / Coetzee, David / Otwombe, Kennedy / Morris, Lynn / Tiemessen, Caroline T / Savulescu, Dana M

    Frontiers in immunology

    2022  Volume 13, Page(s) 813412

    Abstract: Enveloped viruses, including the Human Immunodeficiency Virus-1 (HIV), incorporate host proteins such as human leucocyte antigens (HLA) into their envelope. Pre-existing antibodies against HLA, termed HLA antibodies, may bind to these surface proteins ... ...

    Abstract Enveloped viruses, including the Human Immunodeficiency Virus-1 (HIV), incorporate host proteins such as human leucocyte antigens (HLA) into their envelope. Pre-existing antibodies against HLA, termed HLA antibodies, may bind to these surface proteins and reduce viral infectivity. Related evidence includes macaque studies which suggest that xenoimmunization with HLA antigens may protect against simian immunodeficiency virus infection. Since HIV gp120 shows homology with class 2 HLA, including shared affinity for binding to CD4, class 2 HLA antibodies may influence HIV acquisition
    MeSH term(s) Autoantibodies ; Case-Control Studies ; HIV Infections ; HIV-1 ; HLA Antigens ; Humans
    Chemical Substances Autoantibodies ; HLA Antigens
    Language English
    Publishing date 2022-03-24
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2022.813412
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  6. Article ; Online: HLA antibody repertoire in infants suggests selectivity in transplacental crossing.

    Savulescu, Dana M / Groome, Michelle / Malfeld, Susan C K / Madhi, Shabir / Koen, Anthonet / Jones, Stephanie / Duxbury, Vania / Scheuermaier, Karine / De Assis Rosa, Debbie / Suchard, Melinda

    American journal of reproductive immunology (New York, N.Y. : 1989)

    2020  Volume 84, Issue 2, Page(s) e13264

    Abstract: Problem: Late in pregnancy, women produce and transfer high amounts of antibodies to the foetus. During gestation, women produce antibodies against human leukocyte antigens (HLA), including antibodies directed at foetal HLA. There is paucity of data on ... ...

    Abstract Problem: Late in pregnancy, women produce and transfer high amounts of antibodies to the foetus. During gestation, women produce antibodies against human leukocyte antigens (HLA), including antibodies directed at foetal HLA. There is paucity of data on transplacental crossing, specificity and role of HLA antibodies in pregnancy and new-borns.
    Method of study: Using highly sensitive Luminex technology, we measured prevalence of IgG HLA antibodies in 30 mother-infant pairs six weeks post-partum. Additionally, in six pregnant women, we measured HLA antibodies longitudinally and HLA-typed infant DNA to assess whether maternal HLA antibodies were directed at infant specificities.
    Results: Overall, 68% of mothers and 44% of infants expressed HLA-I antibodies and 56% of mothers and 52% of infants expressed HLA-II antibodies. Infants shared up to 78% of antibodies with their mothers, suggesting that the remaining antibodies were self-made. Less than 25% of maternal HLA antibodies were detected in infants, possibly due to selection in transplacental crossing. We detected complement-fixing HLA antibodies in mothers and at low levels in infants. In a third of our pregnant subjects, we detected infant-directed HLA antibodies.
    Conclusion: Our findings raise the possibility of selection in transplacental crossing of HLA antibodies. As HLA antibodies may act as autoantibodies in the neonate, the mechanism of a selective transfer may give important insights into immune tolerance. Findings also suggest that infants start producing their own HLA antibodies in the first weeks of life, which, together with maternally derived antibodies may impact the infant's immune reaction to HLA proteins.
    MeSH term(s) Adult ; Autoantibodies/blood ; Epitopes ; Female ; HLA Antigens/immunology ; Humans ; Immune Tolerance ; Immunity, Maternally-Acquired ; Infant ; Infant, Newborn ; Isoantibodies/blood ; Maternal-Fetal Exchange ; Placental Circulation ; Pregnancy/immunology
    Chemical Substances Autoantibodies ; Epitopes ; HLA Antigens ; Isoantibodies
    Language English
    Publishing date 2020-06-16
    Publishing country Denmark
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 604542-x
    ISSN 1600-0897 ; 0271-7352 ; 8755-8920 ; 1046-7408
    ISSN (online) 1600-0897
    ISSN 0271-7352 ; 8755-8920 ; 1046-7408
    DOI 10.1111/aji.13264
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1653: Show issues Location:
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