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  1. Article ; Online: Renal peroxiredoxin 6 interacts with anion exchanger 1 and plays a novel role in pH homeostasis.

    Sorrell, Sara L / Golder, Zoe J / Johnstone, Duncan B / Frankl, Fiona E Karet

    Kidney international

    2016  Volume 89, Issue 1, Page(s) 105–112

    Abstract: Peroxiredoxin 6 (PRDX6) is one of the six members of the PRDX family, which have peroxidase and antioxidant activity. PRDX6 is unique, containing only one conserved cysteine residue (C47) rather than the two found in other PRDXs. A yeast two-hybrid ... ...

    Abstract Peroxiredoxin 6 (PRDX6) is one of the six members of the PRDX family, which have peroxidase and antioxidant activity. PRDX6 is unique, containing only one conserved cysteine residue (C47) rather than the two found in other PRDXs. A yeast two-hybrid screen found PRDX6 to be a potential binding partner of the C-terminal tail of anion exchanger 1 (AE1), a Cl(-)/HCO(3)(-) exchanger basolaterally expressed in renal α-intercalated cells. PRDX6 immunostaining in human kidney was both cytoplasmic and peripheral and colocalized with AE1. Analysis of native protein showed that it was largely monomeric, whereas expressed tagged protein was more dimeric. Two methionine oxidation sites were identified. In vitro and ex vivo pull-downs and immunoprecipitation assays confirmed interaction with AE1, but mutation of the conserved cysteine resulted in loss of interaction. Prdx6 knockout mice had a baseline acidosis with a major respiratory component and greater AE1 expression than wild-type animals. After an oral acid challenge, PRDX6 expression increased in wild-type mice, with preservation of AE1. However, AE1 expression was significantly decreased in knockout animals. Kidneys from acidified mice showed widespread proximal tubular vacuolation in wild-type but not knockout animals. Knockdown of PRDX6 by siRNA in mammalian cells reduced both total and cell membrane AE1 levels. Thus, PRDX6-AE1 interaction contributes to the maintenance of AE1 during cellular stress such as during metabolic acidosis.
    MeSH term(s) Acidosis/metabolism ; Animals ; Anion Exchange Protein 1, Erythrocyte/chemistry ; Anion Exchange Protein 1, Erythrocyte/metabolism ; Homeostasis ; Humans ; Hydrogen-Ion Concentration ; Immunohistochemistry ; Immunoprecipitation ; Kidney/metabolism ; Kidney/pathology ; Mice ; Mice, Knockout ; Peroxiredoxin VI/chemistry ; Peroxiredoxin VI/genetics ; Peroxiredoxin VI/metabolism
    Chemical Substances Anion Exchange Protein 1, Erythrocyte ; Peroxiredoxin VI (EC 1.11.1.15)
    Language English
    Publishing date 2016-01-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120573-0
    ISSN 1523-1755 ; 0085-2538
    ISSN (online) 1523-1755
    ISSN 0085-2538
    DOI 10.1038/ki.2015.277
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 797: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  2. Article: The d subunit plays a central role in human vacuolar H(+)-ATPases.

    Smith, Annabel N / Francis, Richard W / Sorrell, Sara L / Karet, Fiona E

    Journal of bioenergetics and biomembranes

    2008  Volume 40, Issue 4, Page(s) 371–380

    Abstract: The multi-subunit vacuolar-type H(+)-ATPase consists of a V(1) domain (A-H subunits) catalyzing ATP hydrolysis and a V(0) domain (a, c, c', c", d, e) responsible for H(+) translocation. The mammalian V(0) d subunit is one of the least-well characterized, ...

    Abstract The multi-subunit vacuolar-type H(+)-ATPase consists of a V(1) domain (A-H subunits) catalyzing ATP hydrolysis and a V(0) domain (a, c, c', c", d, e) responsible for H(+) translocation. The mammalian V(0) d subunit is one of the least-well characterized, and its function and position within the pump are still unclear. It has two different forms encoded by separate genes, d1 being ubiquitous while d2 is predominantly expressed at the cell surface in kidney and osteoclast. To determine whether it forms part of the pump's central stalk as suggested by bacterial A-ATPase studies, or is peripheral as hypothesized from a yeast model, we investigated both human d subunit isoforms. In silico structural modelling demonstrated that human d1 and d2 are structural orthologues of bacterial subunit C, despite poor sequence identity. Expression studies of d1 and d2 showed that each can pull down the central stalk's D and F subunits from human kidney membrane, and in vitro studies using D and F further showed that the interactions between these proteins and the d subunit is direct. These data indicate that the d subunit in man is centrally located within the pump and is thus important in its rotary mechanism.
    MeSH term(s) Binding Sites ; Computer Simulation ; Enzyme Activation ; Enzyme Stability ; Humans ; Kidney/enzymology ; Models, Chemical ; Models, Molecular ; Protein Binding ; Protein Subunits ; Proton-Translocating ATPases/chemistry ; Proton-Translocating ATPases/metabolism ; Proton-Translocating ATPases/ultrastructure ; Structure-Activity Relationship ; Vacuoles/enzymology
    Chemical Substances Protein Subunits ; Proton-Translocating ATPases (EC 3.6.3.14)
    Language English
    Publishing date 2008-08-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 198499-8
    ISSN 1573-6881 ; 0145-479X ; 0449-5705
    ISSN (online) 1573-6881
    ISSN 0145-479X ; 0449-5705
    DOI 10.1007/s10863-008-9161-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1005: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  3. Article: The d subunit plays a central role in human vacuolar H⁺-ATPases

    Smith, Annabel N / Francis, Richard W / Sorrell, Sara L / Karet, Fiona E

    Journal of bioenergetics and biomembranes. 2008 Aug., v. 40, no. 4

    2008  

    Abstract: The multi-subunit vacuolar-type H⁺-ATPase consists of a V₁ domain (A-H subunits) catalyzing ATP hydrolysis and a V₀ domain (a, c, c′, c″, d, e) responsible for H⁺ translocation. The mammalian V₀ d subunit is one of the least-well characterized, and its ... ...

    Abstract The multi-subunit vacuolar-type H⁺-ATPase consists of a V₁ domain (A-H subunits) catalyzing ATP hydrolysis and a V₀ domain (a, c, c′, c″, d, e) responsible for H⁺ translocation. The mammalian V₀ d subunit is one of the least-well characterized, and its function and position within the pump are still unclear. It has two different forms encoded by separate genes, d1 being ubiquitous while d2 is predominantly expressed at the cell surface in kidney and osteoclast. To determine whether it forms part of the pump's central stalk as suggested by bacterial A-ATPase studies, or is peripheral as hypothesized from a yeast model, we investigated both human d subunit isoforms. In silico structural modelling demonstrated that human d1 and d2 are structural orthologues of bacterial subunit C, despite poor sequence identity. Expression studies of d1 and d2 showed that each can pull down the central stalk's D and F subunits from human kidney membrane, and in vitro studies using D and F further showed that the interactions between these proteins and the d subunit is direct. These data indicate that the d subunit in man is centrally located within the pump and is thus important in its rotary mechanism.
    Keywords humans ; proton pump
    Language English
    Dates of publication 2008-08
    Size p. 371-380.
    Publisher Springer US
    Publishing place Boston
    Document type Article
    ZDB-ID 198499-8
    ISSN 1573-6881 ; 0145-479X ; 0449-5705
    ISSN (online) 1573-6881
    ISSN 0145-479X ; 0449-5705
    DOI 10.1007/s10863-008-9161-y
    Database NAL-Catalogue (AGRICOLA)

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    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1005: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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