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  1. Article ; Online: Chromophore-Assisted Light Inactivation of Mitochondrial Electron Transport Chain Complex II in Caenorhabditis elegans.

    Wojtovich, Andrew P / Wei, Alicia Y / Sherman, Teresa A / Foster, Thomas H / Nehrke, Keith

    Scientific reports

    2016  Volume 6, Page(s) 29695

    Abstract: Mitochondria play critical roles in meeting cellular energy demand, in cell death, and in reactive oxygen species (ROS) and stress signaling. Most Caenorhabditis elegans loss-of-function (lf) mutants in nuclear-encoded components of the respiratory chain ...

    Abstract Mitochondria play critical roles in meeting cellular energy demand, in cell death, and in reactive oxygen species (ROS) and stress signaling. Most Caenorhabditis elegans loss-of-function (lf) mutants in nuclear-encoded components of the respiratory chain are non-viable, emphasizing the importance of respiratory function. Chromophore-Assisted Light Inactivation (CALI) using genetically-encoded photosensitizers provides an opportunity to determine how individual respiratory chain components contribute to physiology following acute lf. As proof-of-concept, we expressed the 'singlet oxygen generator' miniSOG as a fusion with the SDHC subunit of respiratory complex II, encoded by mev-1 in C. elegans, using Mos1-mediated Single Copy Insertion. The resulting mev-1::miniSOG transgene complemented mev-1 mutant phenotypes in kn1 missense and tm1081(lf) deletion mutants. Complex II activity was inactivated by blue light in mitochondria from strains expressing active miniSOG fusions, but not those from inactive fusions. Moreover, light-inducible phenotypes in vivo demonstrated that complex II activity is important under conditions of high energy demand, and that specific cell types are uniquely susceptible to loss of complex II. In conclusion, miniSOG-mediated CALI is a novel genetic platform for acute inactivation of respiratory chain components. Spatio-temporally controlled ROS generation will expand our understanding of how the respiratory chain and mitochondrial ROS influence whole organism physiology.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/growth & development ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Chromophore-Assisted Light Inactivation ; Clutch Size ; Electron Transport Complex II/genetics ; Electron Transport Complex II/metabolism ; Gene Knockdown Techniques ; Genetic Complementation Test ; Larva/genetics ; Larva/growth & development ; Larva/metabolism ; Mitochondria/metabolism ; Mutation, Missense ; Optogenetics
    Chemical Substances Caenorhabditis elegans Proteins ; respiratory complex II ; Electron Transport Complex II (EC 1.3.5.1)
    Language English
    Publishing date 2016-07-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep29695
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Identification of a nuclear carbonic anhydrase in Caenorhabditis elegans

    Sherman, Teresa A / Rongali, Sharath C / Matthews, Tori A / Pfeiffer, Jason / Nehrke, Keith

    Biochimica et biophysica acta. Molecular cell research. 2012 Apr., v. 1823, no. 4

    2012  

    Abstract: BACKGROUND: Carbonic anhydrases (CA) catalyze the inter-conversion of CO2 with HCO3 and H+, and are involved in a wide variety of physiologic processes such as anion transport, pH regulation, and water balance. In mammals there are sixteen members of the ...

    Abstract BACKGROUND: Carbonic anhydrases (CA) catalyze the inter-conversion of CO2 with HCO3 and H+, and are involved in a wide variety of physiologic processes such as anion transport, pH regulation, and water balance. In mammals there are sixteen members of the classical α-type CA family, while the simple genetic model organism Caenorhabditis elegans codes for six αCA isoforms (cah-1 through cah-6). METHODS: Fluorescent reporter constructs were used to analyze gene promoter usage, splice variation, and protein localization in transgenic worms. Catalytic activity of recombinant CA proteins was assessed using Hansson's histochemistry. CA's ability to regulate pH as a function of CO2 and HCO3 was measured using dynamic fluorescent imaging of genetically-targeted biosensors. RESULTS: Each of the six CA genes was found to be expressed in a distinct repertoire of cell types. Surprisingly, worms also expressed a catalytically-active CA splice variant, cah-4a, in which an alternative first exon targeted the protein to the nucleus. Cah-4a expression was restricted mainly to the nervous system, where it was found in nearly all neurons, and recombinant CAH-4A protein could regulate pH in the nucleus. CONCLUSIONS: In addition to establishing C. elegans as a platform for studying αCA function, this is the first example of a nuclear-targeted αCA in any organism to date. GENERAL SIGNIFICANCE: A classical αCA isoform is targeted exclusively to the nucleus where its activity may impact nuclear physiologic and pathophysiologic responses.
    Keywords carbon dioxide ; carbonate dehydratase ; genetically modified organisms ; image analysis ; neurons ; proteins ; fluorescence ; histochemistry ; pH ; exons ; mammals ; protons ; catalytic activity ; Caenorhabditis elegans ; biosensors
    Language English
    Dates of publication 2012-04
    Size p. 808-817.
    Publishing place Elsevier B.V.
    Document type Article
    Note 2019-12-06
    ZDB-ID 283444-3
    ISSN 0167-4889
    ISSN 0167-4889
    DOI 10.1016/j.bbamcr.2011.12.014
    Database NAL-Catalogue (AGRICOLA)

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  3. Article: Identification of a nuclear carbonic anhydrase in Caenorhabditis elegans.

    Sherman, Teresa A / Rongali, Sharath C / Matthews, Tori A / Pfeiffer, Jason / Nehrke, Keith

    Biochimica et biophysica acta

    2012  Volume 1823, Issue 4, Page(s) 808–817

    Abstract: Background: Carbonic anhydrases (CA) catalyze the inter-conversion of CO(2) with HCO(3) and H(+), and are involved in a wide variety of physiologic processes such as anion transport, pH regulation, and water balance. In mammals there are sixteen members ...

    Abstract Background: Carbonic anhydrases (CA) catalyze the inter-conversion of CO(2) with HCO(3) and H(+), and are involved in a wide variety of physiologic processes such as anion transport, pH regulation, and water balance. In mammals there are sixteen members of the classical α-type CA family, while the simple genetic model organism Caenorhabditis elegans codes for six αCA isoforms (cah-1 through cah-6).
    Methods: Fluorescent reporter constructs were used to analyze gene promoter usage, splice variation, and protein localization in transgenic worms. Catalytic activity of recombinant CA proteins was assessed using Hansson's histochemistry. CA's ability to regulate pH as a function of CO(2) and HCO(3) was measured using dynamic fluorescent imaging of genetically-targeted biosensors.
    Results: Each of the six CA genes was found to be expressed in a distinct repertoire of cell types. Surprisingly, worms also expressed a catalytically-active CA splice variant, cah-4a, in which an alternative first exon targeted the protein to the nucleus. Cah-4a expression was restricted mainly to the nervous system, where it was found in nearly all neurons, and recombinant CAH-4A protein could regulate pH in the nucleus.
    Conclusions: In addition to establishing C. elegans as a platform for studying αCA function, this is the first example of a nuclear-targeted αCA in any organism to date.
    General significance: A classical αCA isoform is targeted exclusively to the nucleus where its activity may impact nuclear physiologic and pathophysiologic responses.
    MeSH term(s) Animals ; Bicarbonates/pharmacology ; Biocatalysis/drug effects ; Caenorhabditis elegans/drug effects ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Carbonic Anhydrases/genetics ; Carbonic Anhydrases/metabolism ; Cell Nucleus/drug effects ; Cell Nucleus/enzymology ; Exons/genetics ; Gene Expression Regulation, Enzymologic/drug effects ; Genome, Helminth/genetics ; Hydrogen-Ion Concentration/drug effects ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Multigene Family ; Protein Transport/drug effects ; Recombinant Proteins/metabolism
    Chemical Substances Bicarbonates ; Caenorhabditis elegans Proteins ; Isoenzymes ; Recombinant Proteins ; Carbonic Anhydrases (EC 4.2.1.1)
    Language English
    Publishing date 2012-01-05
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2011.12.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: The C. elegans mitochondrial K+(ATP) channel: a potential target for preconditioning.

    Wojtovich, Andrew P / Burwell, Lindsay S / Sherman, Teresa A / Nehrke, Keith W / Brookes, Paul S

    Biochemical and biophysical research communications

    2008  Volume 376, Issue 3, Page(s) 625–628

    Abstract: Ischemic preconditioning (IPC) is an evolutionarily conserved endogenous mechanism whereby short periods of non-lethal exposure to hypoxia alleviate damage caused by subsequent ischemia reperfusion (IR). Pharmacologic targeting has suggested that the ... ...

    Abstract Ischemic preconditioning (IPC) is an evolutionarily conserved endogenous mechanism whereby short periods of non-lethal exposure to hypoxia alleviate damage caused by subsequent ischemia reperfusion (IR). Pharmacologic targeting has suggested that the mitochondrial ATP-sensitive potassium channel (mK(ATP)) is central to IPC signaling, despite its lack of molecular identity. Here, we report that isolated Caenorhabditis elegans mitochondria have a K(ATP) channel with the same physiologic and pharmacologic characteristics as the vertebrate channel. Since C. elegans also exhibit IPC, our observations provide a framework to study the role of mK(ATP) in IR injury in a genetic model organism.
    MeSH term(s) Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Ischemic Preconditioning ; Mitochondria/metabolism ; Models, Animal ; Potassium Channels/agonists ; Potassium Channels/drug effects ; Potassium Channels/metabolism ; Reperfusion Injury/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Potassium Channels ; mitochondrial K(ATP) channel
    Language English
    Publishing date 2008-11-21
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2008.09.043
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    Zs.A 116: Show issues Location:
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  5. Article ; Online: SLO-2 is cytoprotective and contributes to mitochondrial potassium transport.

    Wojtovich, Andrew P / Sherman, Teresa A / Nadtochiy, Sergiy M / Urciuoli, William R / Brookes, Paul S / Nehrke, Keith

    PloS one

    2011  Volume 6, Issue 12, Page(s) e28287

    Abstract: Mitochondrial potassium channels are important mediators of cell protection against stress. The mitochondrial large-conductance "big" K(+) channel (mBK) mediates the evolutionarily-conserved process of anesthetic preconditioning (APC), wherein exposure ... ...

    Abstract Mitochondrial potassium channels are important mediators of cell protection against stress. The mitochondrial large-conductance "big" K(+) channel (mBK) mediates the evolutionarily-conserved process of anesthetic preconditioning (APC), wherein exposure to volatile anesthetics initiates protection against ischemic injury. Despite the role of the mBK in cardioprotection, the molecular identity of the channel remains unknown. We investigated the attributes of the mBK using C. elegans and mouse genetic models coupled with measurements of mitochondrial K(+) transport and APC. The canonical Ca(2+)-activated BK (or "maxi-K") channel SLO1 was dispensable for both mitochondrial K(+) transport and APC in both organisms. Instead, we found that the related but physiologically-distinct K(+) channel SLO2 was required, and that SLO2-dependent mitochondrial K(+) transport was triggered directly by volatile anesthetics. In addition, a SLO2 channel activator mimicked the protective effects of volatile anesthetics. These findings suggest that SLO2 contributes to protection from hypoxic injury by increasing the permeability of the mitochondrial inner membrane to K(+).
    MeSH term(s) Anesthetics, Inhalation ; Animals ; Caenorhabditis elegans Proteins/antagonists & inhibitors ; Caenorhabditis elegans Proteins/physiology ; Cytoprotection ; Hypoxia/prevention & control ; Immunoblotting ; Indoles/pharmacology ; Ion Transport ; Ischemic Preconditioning, Myocardial ; Large-Conductance Calcium-Activated Potassium Channel alpha Subunits/antagonists & inhibitors ; Large-Conductance Calcium-Activated Potassium Channel alpha Subunits/physiology ; Male ; Membrane Potential, Mitochondrial/drug effects ; Membrane Transport Proteins/physiology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mitochondria/metabolism ; Potassium Channel Blockers/pharmacology
    Chemical Substances Anesthetics, Inhalation ; Caenorhabditis elegans Proteins ; Indoles ; Kcnma1 protein, mouse ; Large-Conductance Calcium-Activated Potassium Channel alpha Subunits ; Membrane Transport Proteins ; Potassium Channel Blockers ; SLO-2 protein, C elegans ; paxilline (3T9U9Z96L7)
    Language English
    Publishing date 2011-12-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0028287
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