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  1. Article ; Online: Xenobiotic Exposure and Migraine-Associated Signaling: A Multimethod Experimental Study Exploring Cellular Assays in Combination with

    Rasmussen, Rikke H / Christensen, Sarah L / Calloe, Kirstine / Nielsen, Brian Skriver / Rehfeld, Anders / Taylor-Clark, Thomas E / Haanes, Kristian A / Taboureau, Olivier / Audouze, Karine / Klaerke, Dan A / Olesen, Jes / Kristensen, David M

    Environmental health perspectives

    2023  Volume 131, Issue 11, Page(s) 117003

    Abstract: Background: Mechanisms for how environmental chemicals might influence pain has received little attention. Epidemiological studies suggest that environmental factors such as pollutants might play a role in migraine prevalence. Potential targets for ... ...

    Abstract Background: Mechanisms for how environmental chemicals might influence pain has received little attention. Epidemiological studies suggest that environmental factors such as pollutants might play a role in migraine prevalence. Potential targets for pollutants are the transient receptor potential (TRP) channels ankyrin 1 (TRPA1) and vanilloid 1 (TRPV1), which on activation release pain-inducing neuropeptide calcitonin gene-related peptide (CGRP).
    Objective: In this study, we aimed to examine the hypothesis that environmental pollutants via TRP channel signaling and subsequent CGRP release trigger migraine signaling and pain.
    Methods: A calcium imaging-based screen of environmental chemicals was used to investigate activation of migraine pain-associated TRP channels TRPA1 and TRPV1. Based on this screen, whole-cell patch clamp and
    Results: A total of 16 out of the 52 screened environmental chemicals activated TRPA1 at 10 or
    Discussion: Here we show that multiple environmental pollutants interact with the TRPA1-CGRP migraine pain pathway. The data provide valuable insights into how environmental chemicals can interact with neurobiology and provide a potential mechanism for putative increases in migraine prevalence over the last decades. https://doi.org/10.1289/EHP12413.
    MeSH term(s) Mice ; Animals ; TRPA1 Cation Channel/physiology ; Calcitonin Gene-Related Peptide/metabolism ; Calcium/metabolism ; Xenobiotics ; Transient Receptor Potential Channels/metabolism ; Migraine Disorders/metabolism ; Pain ; Environmental Pollutants/toxicity
    Chemical Substances TRPA1 Cation Channel ; Calcitonin Gene-Related Peptide (JHB2QIZ69Z) ; Calcium (SY7Q814VUP) ; Xenobiotics ; Transient Receptor Potential Channels ; Environmental Pollutants
    Language English
    Publishing date 2023-11-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 195189-0
    ISSN 1552-9924 ; 0091-6765 ; 1078-0475
    ISSN (online) 1552-9924
    ISSN 0091-6765 ; 1078-0475
    DOI 10.1289/EHP12413
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Structural determinants underlying permeant discrimination of the Cx43 hemichannel.

    Nielsen, Brian Skriver / Zonta, Francesco / Farkas, Thomas / Litman, Thomas / Nielsen, Morten Schak / MacAulay, Nanna

    The Journal of biological chemistry

    2019  Volume 294, Issue 45, Page(s) 16789–16803

    Abstract: Connexin (Cx) gap junction channels comprise two hemichannels in neighboring cells, and their permeability is well-described, but permeabilities of the single Cx hemichannel remain largely unresolved. Moreover, determination of isoform-specific Cx ... ...

    Abstract Connexin (Cx) gap junction channels comprise two hemichannels in neighboring cells, and their permeability is well-described, but permeabilities of the single Cx hemichannel remain largely unresolved. Moreover, determination of isoform-specific Cx hemichannel permeability is challenging because of concurrent expression of other channels with similar permeability profiles and inhibitor sensitivities. The mammalian Cx hemichannels Cx30 and Cx43 are gated by extracellular divalent cations, removal of which promotes fluorescent dye uptake in both channels but atomic ion conductance only through Cx30. To determine the molecular determinants of this difference, here we employed chimeras and mutagenesis of predicted pore-lining residues in Cx43. We expressed the mutated channels in
    MeSH term(s) Amino Acid Sequence ; Cell Membrane/metabolism ; Connexin 43/chemistry ; Connexin 43/metabolism ; Electrophysiological Phenomena ; Molecular Dynamics Simulation ; Permeability ; Porosity ; Protein Conformation ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism ; Substrate Specificity
    Chemical Substances Connexin 43 ; Protein Isoforms
    Language English
    Publishing date 2019-09-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA119.007732
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Pannexin 1 activation and inhibition is permeant-selective.

    Nielsen, Brian Skriver / Toft-Bertelsen, Trine Lisberg / Lolansen, Sara Diana / Anderson, Connor L / Nielsen, Morten Schak / Thompson, Roger J / MacAulay, Nanna

    The Journal of physiology

    2020  Volume 598, Issue 2, Page(s) 361–379

    Abstract: Key points: The large-pore channel pannexin 1 (Panx1) is expressed in many cell types and can open upon different, yet not fully established, stimuli. Panx1 permeability is often inferred from channel permeability to fluorescent dyes, but it is ... ...

    Abstract Key points: The large-pore channel pannexin 1 (Panx1) is expressed in many cell types and can open upon different, yet not fully established, stimuli. Panx1 permeability is often inferred from channel permeability to fluorescent dyes, but it is currently unknown whether dye permeability translates to permeability to other molecules. Cell shrinkage and C-terminal cleavage led to a Panx1 open-state with increased permeability to atomic ions (current), but did not alter ethidium uptake. Panx1 inhibitors affected Panx1-mediated ion conduction differently from ethidium permeability, and inhibitor efficiency towards a given molecule therefore cannot be extrapolated to its effects on the permeability of another. We conclude that ethidium permeability does not reflect equal permeation of other molecules and thus is no measure of general Panx1 activity.
    Abstract: Pannexin 1 (Panx1) is a large-pore membrane channel connecting the extracellular milieu with the cell interior. While several activation regimes activate Panx1 in a variety of cell types, the selective permeability of an open Panx1 channel remains unresolved: does a given activation paradigm increase Panx1's permeability towards all permeants equally and does fluorescent dye flux serve as a proxy for biological permeation through an open channel? To explore permeant-selectivity of Panx1 activation and inhibition, we employed Panx1-expressing Xenopus laevis oocytes and HEK293T cells. We report that different mechanisms of activation of Panx1 differentially affected ethidium and atomic ion permeation. Most notably, C-terminal truncation or cell shrinkage elevated Panx1-mediated ion conductance, but had no effect on ethidium permeability. In contrast, extracellular pH changes predominantly affected ethidium permeability but not ionic conductance. High [K
    MeSH term(s) Animals ; Connexins/physiology ; Fluorescent Dyes ; Glutamic Acid ; HEK293 Cells ; Humans ; Ion Channels/physiology ; Lactic Acid ; Nerve Tissue Proteins/physiology ; Oocytes ; Xenopus laevis
    Chemical Substances Connexins ; Fluorescent Dyes ; Ion Channels ; Nerve Tissue Proteins ; PANX1 protein, human ; Lactic Acid (33X04XA5AT) ; Glutamic Acid (3KX376GY7L)
    Language English
    Publishing date 2020-01-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3115-x
    ISSN 1469-7793 ; 0022-3751
    ISSN (online) 1469-7793
    ISSN 0022-3751
    DOI 10.1113/JP278759
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Permeant-specific gating of connexin 30 hemichannels.

    Nielsen, Brian Skriver / Alstrom, Jette Skov / Nicholson, Bruce J / Nielsen, Morten Schak / MacAulay, Nanna

    The Journal of biological chemistry

    2017  Volume 292, Issue 49, Page(s) 19999–20009

    Abstract: Gap junctions confer interconnectivity of the cytoplasm in neighboring cells via docking of two connexons expressed in each of the adjacent membranes. Undocked connexons, referred to as hemichannels, may open and connect the cytoplasm with the ... ...

    Abstract Gap junctions confer interconnectivity of the cytoplasm in neighboring cells via docking of two connexons expressed in each of the adjacent membranes. Undocked connexons, referred to as hemichannels, may open and connect the cytoplasm with the extracellular fluid. The hemichannel configuration of connexins (Cxs) displays isoform-specific permeability profiles that are not directly determined by the size and charge of the permeant. To further explore Ca
    MeSH term(s) Amino Acid Substitution ; Animals ; Calcium Channels ; Connexin 30/genetics ; Connexin 30/metabolism ; Ethidium/metabolism ; Gap Junctions/physiology ; Humans ; Ion Channel Gating ; Ions/metabolism ; Permeability ; Xenopus laevis/genetics
    Chemical Substances Calcium Channels ; Connexin 30 ; Ions ; Ethidium (EN464416SI)
    Language English
    Publishing date 2017-10-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M117.805986
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Connexin Hemichannels in Astrocytes: An Assessment of Controversies Regarding Their Functional Characteristics.

    Nielsen, Brian Skriver / Hansen, Daniel Bloch / Ransom, Bruce R / Nielsen, Morten Schak / MacAulay, Nanna

    Neurochemical research

    2017  Volume 42, Issue 9, Page(s) 2537–2550

    Abstract: Astrocytes in the mammalian central nervous system are interconnected by gap junctions made from connexins of the subtypes Cx30 and Cx43. These proteins may exist as hemichannels in the plasma membrane in the absence of a 'docked' counterpart on the ... ...

    Abstract Astrocytes in the mammalian central nervous system are interconnected by gap junctions made from connexins of the subtypes Cx30 and Cx43. These proteins may exist as hemichannels in the plasma membrane in the absence of a 'docked' counterpart on the neighboring cell. A variety of stimuli are reported to open the hemichannels and thereby create a permeation pathway through the plasma membrane. Cx30 and Cx43 have, in their hemichannel configuration, been proposed to act as ion channels and membrane pathways for different molecules, such as fluorescent dyes, ATP, prostaglandins, and glutamate. Published studies about astrocyte hemichannel behavior, however, have been highly variable and/or contradictory. The field of connexin hemichannel research has been complicated by great variability in the experimental preparations employed, a lack of highly specific pharmacological inhibitors and by confounding changes associated with genetically modified animal models. This review attempts to critically assess the gating, inhibition and permeability of astrocytic connexin hemichannels and proposes that connexins in their hemichannel configuration act as gated pores with isoform-specific permeant selectivity. We expect that some, or all, of the controversies discussed here will be resolved by future research and sincerely hope that this review serves to motivate such clarifying investigations.
    MeSH term(s) Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/pharmacology ; Animals ; Astrocytes/drug effects ; Astrocytes/metabolism ; Cell Membrane/drug effects ; Cell Membrane/metabolism ; Connexins/agonists ; Connexins/antagonists & inhibitors ; Connexins/physiology ; Fluorescent Dyes/metabolism ; Fluorescent Dyes/pharmacology ; Humans ; Ion Channel Gating/drug effects ; Ion Channel Gating/physiology ; Peptide Fragments/metabolism ; Peptide Fragments/pharmacology
    Chemical Substances Amyloid beta-Peptides ; Connexins ; Fluorescent Dyes ; Peptide Fragments ; amyloid beta-protein (25-35)
    Language English
    Publishing date 2017-09
    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/s11064-017-2243-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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