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  1. Book ; Online ; E-Book: Peroxiporins

    Medraño-Fernandez, Iria / Bienert, Gerd Patrick / Sitia, Roberto

    redox signal mediators in and between cells

    (Oxidative Stress and Disease Series ; v.50)

    2024  

    Author's details edited by Iria Medraño-Fernandez, Gerd Patrick Bienert, and Roberto Sitia
    Series title Oxidative Stress and Disease Series ; v.50
    Keywords Aquaporins
    Subject code 572.696
    Language English
    Size 1 online resource (245 pages)
    Edition 1st ed.
    Publisher CRC Press
    Publishing place Boca Raton, FL
    Document type Book ; Online ; E-Book
    Note Includes index.
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 1-000-92781-4 ; 9780367749866 ; 978-1-000-92781-8 ; 0367749866
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article ; Online: Transfer of H

    Sorrentino, Ilaria / Galli, Mauro / Medraño-Fernandez, Iria / Sitia, Roberto

    Redox biology

    2022  Volume 55, Page(s) 102410

    Abstract: Some aquaporins (AQPs) can transport ... ...

    Abstract Some aquaporins (AQPs) can transport H
    Language English
    Publishing date 2022-07-16
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2701011-9
    ISSN 2213-2317 ; 2213-2317
    ISSN (online) 2213-2317
    ISSN 2213-2317
    DOI 10.1016/j.redox.2022.102410
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  3. Article ; Online: Neil J. Bulleid (1960-2023), a virtuoso of protein folding and redox biology.

    Braakman, Ineke / High, Stephen / Kadler, Karl / Sitia, Roberto / Tokatlidis, Kostas / Woodman, Philip

    The EMBO journal

    2023  Volume 42, Issue 17, Page(s) e115046

    MeSH term(s) Protein Folding ; Oxidation-Reduction ; Biology
    Language English
    Publishing date 2023-08-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2023115046
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  4. Article ; Online: Evolution, role in inflammation, and redox control of leaderless secretory proteins.

    Sitia, Roberto / Rubartelli, Anna

    The Journal of biological chemistry

    2020  Volume 295, Issue 22, Page(s) 7799–7811

    Abstract: Members of the interleukin (IL)-1 family are key determinants of inflammation. Despite their role as intercellular mediators, most lack the leader peptide typically required for protein secretion. This lack is a characteristic of dozens of other proteins ...

    Abstract Members of the interleukin (IL)-1 family are key determinants of inflammation. Despite their role as intercellular mediators, most lack the leader peptide typically required for protein secretion. This lack is a characteristic of dozens of other proteins that are actively and selectively secreted from living cells independently of the classical endoplasmic reticulum-Golgi exocytic route. These proteins, termed leaderless secretory proteins (LLSPs), comprise proteins directly or indirectly involved in inflammation, including cytokines such as IL-1β and IL-18, growth factors such as fibroblast growth factor 2 (FGF2), redox enzymes such as thioredoxin, and proteins most expressed in the brain, some of which participate in the pathogenesis of neurodegenerative disorders. Despite much effort, motifs that promote LLSP secretion remain to be identified. In this review, we summarize the mechanisms and pathophysiological significance of the unconventional secretory pathways that cells use to release LLSPs. We place special emphasis on redox regulation and inflammation, with a focus on IL-1β, which is secreted after processing of its biologically inactive precursor pro-IL-1β in the cytosol. Although LLSP externalization remains poorly understood, some possible mechanisms have emerged. For example, a common feature of LLSP pathways is that they become more active in response to stress and that they involve several distinct excretion mechanisms, including direct plasma membrane translocation, lysosome exocytosis, exosome formation, membrane vesiculation, autophagy, and pyroptosis. Further investigations of unconventional secretory pathways for LLSP secretion may shed light on their evolution and could help advance therapeutic avenues for managing pathological conditions, such as diseases arising from inflammation.
    MeSH term(s) Animals ; Autophagy ; Evolution, Molecular ; Exocytosis ; Exosomes/genetics ; Exosomes/metabolism ; Exosomes/pathology ; Fibroblast Growth Factor 2/genetics ; Fibroblast Growth Factor 2/metabolism ; Humans ; Inflammation/genetics ; Inflammation/metabolism ; Inflammation/pathology ; Interleukin-18/genetics ; Interleukin-18/metabolism ; Interleukin-1beta/genetics ; Interleukin-1beta/metabolism ; Lysosomes/genetics ; Lysosomes/metabolism ; Lysosomes/pathology ; Protein Processing, Post-Translational ; Pyroptosis ; Secretory Pathway
    Chemical Substances IL18 protein, human ; IL1B protein, human ; Interleukin-18 ; Interleukin-1beta ; Fibroblast Growth Factor 2 (103107-01-3)
    Language English
    Publishing date 2020-04-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.REV119.008907
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Arenaviral infection causes bleeding in mice due to reduced serotonin release from platelets.

    Aiolfi, Roberto / Sitia, Giovanni / Iannacone, Matteo / Brunetta, Ivan / Guidotti, Luca G / Ruggeri, Zaverio M

    Science signaling

    2022  Volume 15, Issue 722, Page(s) eabb0384

    Abstract: Bleeding correlates with disease severity in viral hemorrhagic fevers. We found that the increase in type I interferon (IFN-I) in mice caused by infection with the Armstrong strain of lymphocytic choriomeningitis virus (LCMV; an arenavirus) reduced the ... ...

    Abstract Bleeding correlates with disease severity in viral hemorrhagic fevers. We found that the increase in type I interferon (IFN-I) in mice caused by infection with the Armstrong strain of lymphocytic choriomeningitis virus (LCMV; an arenavirus) reduced the megakaryocytic expression of genes encoding enzymes involved in lipid biosynthesis (
    MeSH term(s) Animals ; Blood Platelets/metabolism ; Hemorrhage/metabolism ; Lymphocytic Choriomeningitis/genetics ; Lymphocytic Choriomeningitis/metabolism ; Lymphocytic choriomeningitis virus/genetics ; Mice ; Serotonin/metabolism
    Chemical Substances Serotonin (333DO1RDJY)
    Language English
    Publishing date 2022-02-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2417226-1
    ISSN 1937-9145 ; 1945-0877
    ISSN (online) 1937-9145
    ISSN 1945-0877
    DOI 10.1126/scisignal.abb0384
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The unconventional secretion of IL-1β: Handling a dangerous weapon to optimize inflammatory responses.

    Sitia, Roberto / Rubartelli, Anna

    Seminars in cell & developmental biology

    2018  Volume 83, Page(s) 12–21

    Abstract: Interleukin 1β (IL-1β) is a major mediator of inflammation, with a causative role in many diseases. Unlike most other cytokines, however, it lacks a secretory signal sequence, raising intriguing mechanistic, functional and evolutionary questions. Despite ...

    Abstract Interleukin 1β (IL-1β) is a major mediator of inflammation, with a causative role in many diseases. Unlike most other cytokines, however, it lacks a secretory signal sequence, raising intriguing mechanistic, functional and evolutionary questions. Despite decades of strenuous efforts in many laboratories, how IL-1β is secreted is still a matter of intense debate. Here, we summarize the different mechanisms and pathways that have been proposed for IL-1β secretion. At least two of them, namely the endolysosomal vesicle-based and gasdermin D-dependent pathways (types III and I in the recent Rabouille's classification of unconventional protein secretion), can be triggered in monocytes, the main source of IL-1β in humans, according to the type and strength of the pro-inflammatory stimuli. As during the escalation of human conflicts, monocytes deploy secretory mechanisms of increasing efficiency and dangerousness, shifting from the specific and controlled type III pathway to the much faster release of type I. Thus, the different mechanisms are activated depending on the severity of the conditions, from the self-limiting type III pathways in response of low pathogen load or small trauma, to the uncontrolled responses that underlie autoinflammatory disorders and sepsis.
    MeSH term(s) Autophagy/physiology ; Humans ; Interleukin-1beta/metabolism ; Lysosomes/metabolism
    Chemical Substances Interleukin-1beta
    Language English
    Publishing date 2018-04-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2018.03.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  7. Article ; Online: Transfer of H2O2 from Mitochondria to the endoplasmic reticulum via Aquaporin-11

    Ilaria Sorrentino / Mauro Galli / Iria Medraño-Fernandez / Roberto Sitia

    Redox Biology, Vol 55, Iss , Pp 102410- (2022)

    2022  

    Abstract: Some aquaporins (AQPs) can transport H2O2 across membranes, allowing redox signals to proceed in and between cells. Unlike other peroxiporins, human AQP11 is an endoplasmic reticulum (ER)-resident that can conduit H2O2 to the cytosol. Here, we show that ... ...

    Abstract Some aquaporins (AQPs) can transport H2O2 across membranes, allowing redox signals to proceed in and between cells. Unlike other peroxiporins, human AQP11 is an endoplasmic reticulum (ER)-resident that can conduit H2O2 to the cytosol. Here, we show that silencing Ero1α, an ER flavoenzyme that generates abundant H2O2 during oxidative folding, causes a paradoxical increase in luminal H2O2 levels. The simultaneous AQP11 downregulation prevents this increase, implying that H2O2 reaches the ER from an external source(s). Pharmacological inhibition of the electron transport chain reveals that Ero1α downregulation activates superoxide production by complex III. In the intermembrane space, superoxide dismutase 1 generates H2O2 that enters the ER channeled by AQP11. Meanwhile, the number of ER-mitochondria contact sites increases as well, irrespective of AQP11 expression. Taken together, our findings identify a novel interorganellar redox response that is activated upon Ero1α downregulation and transfers H2O2 from mitochondria to the ER via AQP11.
    Keywords Hydrogen peroxide ; Redox homeostasis ; Interorganellar crosstalk/ peroxiporin ; Complex III ; Mitochondrial-associated membranes ; Medicine (General) ; R5-920 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-09-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Correction: Role of the early secretory pathway in SARS-CoV-2 infection.

    Sicari, Daria / Chatziioannou, Aristotelis / Koutsandreas, Theodoros / Sitia, Roberto / Chevet, Eric

    The Journal of cell biology

    2020  Volume 219, Issue 9

    Keywords covid19
    Language English
    Publishing date 2020-08-25
    Publishing country United States
    Document type Journal Article ; Published Erratum
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.20200600508132020c
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  9. Article ; Online: Role of the early secretory pathway in SARS-CoV-2 infection.

    Sicari, Daria / Chatziioannou, Aristotelis / Koutsandreas, Theodoros / Sitia, Roberto / Chevet, Eric

    The Journal of cell biology

    2020  Volume 219, Issue 9

    Abstract: Similar to other RNA viruses, SARS-CoV-2 must (1) enter a target/host cell, (2) reprogram it to ensure its replication, (3) exit the host cell, and (4) repeat this cycle for exponential growth. During the exit step, the virus hijacks the sophisticated ... ...

    Abstract Similar to other RNA viruses, SARS-CoV-2 must (1) enter a target/host cell, (2) reprogram it to ensure its replication, (3) exit the host cell, and (4) repeat this cycle for exponential growth. During the exit step, the virus hijacks the sophisticated machineries that host cells employ to correctly fold, assemble, and transport proteins along the exocytic pathway. Therefore, secretory pathway-mediated assemblage and excretion of infective particles represent appealing targets to reduce the efficacy of virus biogenesis, if not to block it completely. Here, we analyze and discuss the contribution of the molecular machines operating in the early secretory pathway in the biogenesis of SARS-CoV-2 and their relevance for potential antiviral targeting. The fact that these molecular machines are conserved throughout evolution, together with the redundancy and tissue specificity of their components, provides opportunities in the search for unique proteins essential for SARS-CoV-2 biology that could also be targeted with therapeutic objectives. Finally, we provide an overview of recent evidence implicating proteins of the early secretory pathway as potential antiviral targets with effective therapeutic applications.
    MeSH term(s) Antiviral Agents/therapeutic use ; Betacoronavirus/drug effects ; Betacoronavirus/pathogenicity ; COVID-19 ; Coronavirus Infections/drug therapy ; Coronavirus Infections/virology ; Humans ; Pandemics ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/virology ; SARS-CoV-2 ; Secretory Pathway/drug effects ; Secretory Pathway/physiology ; Virus Replication/drug effects ; Virus Replication/physiology
    Chemical Substances Antiviral Agents
    Keywords covid19
    Language English
    Publishing date 2020-07-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202006005
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  10. Article ; Online: Molecular Evaluation of Endoplasmic Reticulum Homeostasis Meets Humoral Immunity.

    van Anken, Eelco / Bakunts, Anush / Hu, Chih-Chi Andrew / Janssens, Sophie / Sitia, Roberto

    Trends in cell biology

    2021  Volume 31, Issue 7, Page(s) 529–541

    Abstract: The biosynthesis of about one third of the human proteome, including membrane receptors and secreted proteins, occurs in the endoplasmic reticulum (ER). Conditions that perturb ER homeostasis activate the unfolded protein response (UPR). An 'optimistic' ... ...

    Abstract The biosynthesis of about one third of the human proteome, including membrane receptors and secreted proteins, occurs in the endoplasmic reticulum (ER). Conditions that perturb ER homeostasis activate the unfolded protein response (UPR). An 'optimistic' UPR output aims at restoring homeostasis by reinforcement of machineries that guarantee efficiency and fidelity of protein biogenesis in the ER. Yet, once the UPR 'deems' that ER homeostatic readjustment fails, it transitions to a 'pessimistic' output, which, depending on the cell type, will result in apoptosis. In this article, we discuss emerging concepts on how the UPR 'evaluates' ER stress, how the UPR is repurposed, in particular in B cells, and how UPR-driven counter-selection of cells undergoing homeostatic failure serves organismal homeostasis and humoral immunity.
    MeSH term(s) Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress ; Homeostasis ; Humans ; Immunity, Humoral ; Unfolded Protein Response
    Language English
    Publishing date 2021-03-05
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2021.02.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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