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  1. 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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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: Isoform-specific phosphorylation-dependent regulation of connexin hemichannels.

    Alstrøm, Jette Skov / Hansen, Daniel Bloch / Nielsen, Morten Schak / MacAulay, Nanna

    Journal of neurophysiology

    2015  Volume 114, Issue 5, Page(s) 3014–3022

    Abstract: Connexins form gap junction channels made up of two connexons (hemichannels) from adjacent cells. Unopposed hemichannels may open toward the extracellular space upon stimulation by, e.g., removal of divalent cations from the extracellular solution and ... ...

    Abstract Connexins form gap junction channels made up of two connexons (hemichannels) from adjacent cells. Unopposed hemichannels may open toward the extracellular space upon stimulation by, e.g., removal of divalent cations from the extracellular solution and allow isoform-specific transmembrane flux of fluorescent dyes and physiologically relevant molecules, such as ATP and ions. Connexin (Cx)43 and Cx30 are the major astrocytic connexins. Protein kinase C (PKC) regulates Cx43 in its cell-cell gap junction configuration and may also act to keep Cx43 hemichannels closed. In contrast, the regulation of Cx30 hemichannels by PKC is unexplored. To determine phosphorylation-dependent regulation of Cx30 and Cx43 hemichannels, these were heterologously expressed in Xenopus laevis oocytes and opened with divalent cation-free solution. Inhibition of PKC activity did not affect hemichannel opening of either connexin. PKC activation had no effect on Cx43-mediated hemichannel activity, whereas both dye uptake and current through Cx30 hemichannels were reduced. We detected no PKC-induced connexin internalization from the plasma membrane, indicating that PKC reduced Cx30 hemichannel activity by channel closure. In an attempt to resolve the PKC phosphorylation site(s) on Cx30, alanine mutations of putative cytoplasmic PKC consensus sites were created to prevent phosphorylation (T5A, T8A, T102A, S222A, S225A, S239A, and S258A). These Cx30 mutants responded to PKC activation, suggesting that Cx30 hemichannels are not regulated by phosphorylation of a single site. In conclusion, Cx30, but not Cx43, hemichannels close upon PKC activation, illustrating that connexin hemichannels display not only isoform-specific permeability profiles but also isoform-specific regulation by PKC.
    MeSH term(s) Animals ; Benzophenanthridines/pharmacology ; Connexin 30 ; Connexin 43/metabolism ; Connexins/metabolism ; Indoles/pharmacology ; Maleimides/pharmacology ; Membrane Potentials ; Mice ; Phosphorylation ; Protein Isoforms/metabolism ; Protein Kinase C/antagonists & inhibitors ; Protein Kinase C/metabolism ; Rats ; Xenopus laevis
    Chemical Substances Benzophenanthridines ; Connexin 30 ; Connexin 43 ; Connexins ; Gja1 protein, rat ; Gjb6 protein, mouse ; Indoles ; Maleimides ; Protein Isoforms ; bisindolylmaleimide II ; chelerythrine (E3B045W6X0) ; Protein Kinase C (EC 2.7.11.13)
    Language English
    Publishing date 2015-09-23
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80161-6
    ISSN 1522-1598 ; 0022-3077
    ISSN (online) 1522-1598
    ISSN 0022-3077
    DOI 10.1152/jn.00575.2015
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels.

    Alstrom, Jette Skov / Stroemlund, Line Waring / Nielsen, Morten Schak / MacAulay, Nanna

    Biochemical Society transactions

    2015  Volume 43, Issue 3, Page(s) 519–523

    Abstract: Connexin43 (Cx43) generates intercellular gap junction channels involved in, among others, cardiac and brain function. Gap junctions are formed by the docking of two hemichannels from neighbouring cells. Undocked Cx43 hemichannels can upon different ... ...

    Abstract Connexin43 (Cx43) generates intercellular gap junction channels involved in, among others, cardiac and brain function. Gap junctions are formed by the docking of two hemichannels from neighbouring cells. Undocked Cx43 hemichannels can upon different stimuli open towards the extracellular matrix and allow transport of molecules such as fluorescent dyes and ATP. A range of phosphorylated amino acids have been detected in the C-terminus of Cx43 and their physiological role has been intensively studied both in the gap junctional form of Cx43 and in its hemichannel configuration. We present the current knowledge of protein kinase C (PKC)-dependent regulation of Cx43 and discuss the divergent results.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Biological Transport/genetics ; Brain/physiology ; Connexin 43/biosynthesis ; Connexin 43/genetics ; Gap Junctions/genetics ; Gap Junctions/metabolism ; Gap Junctions/physiology ; Gene Expression Regulation ; Heart/physiology ; Humans ; Phosphorylation ; Protein Kinase C/genetics ; Protein Kinase C/metabolism
    Chemical Substances Connexin 43 ; Adenosine Triphosphate (8L70Q75FXE) ; Protein Kinase C (EC 2.7.11.13)
    Language English
    Publishing date 2015-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20150040
    Database MEDical Literature Analysis and Retrieval System OnLINE

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