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  1. Article: The Na+/H+ exchanger gene family.

    Burckhardt, Gerhard / Di Sole, Francesca / Helmle-Kolb, Corinna

    Journal of nephrology

    2002  Volume 15 Suppl 5, Page(s) S3–21

    Abstract: Na+/H+ exchangers (NHEs) extrude protons from, and take up sodium ions into cells. Six isoforms, NHE-1 - NHE-6, have been cloned. NHE proteins are composed of an N-terminal domain, which most likely crosses the cell membrane 12 times and constitutes the ... ...

    Abstract Na+/H+ exchangers (NHEs) extrude protons from, and take up sodium ions into cells. Six isoforms, NHE-1 - NHE-6, have been cloned. NHE proteins are composed of an N-terminal domain, which most likely crosses the cell membrane 12 times and constitutes the cation exchange machinery, and a C-terminal tail, which modulates the exchanger by interacting with protein kinases and regulatory factors. The "house-keeping" NHE-1 is located at the basolateral membrane of most renal tubule cells; NHE-2 is located apically in selected nephron segments. As suggested from data with NHE-1 and NHE-2 deficient mice, both isoforms play a minor role in renal salt and water handling. NHE-3 is located at the apical membrane of proximal tubule and thick ascending limb cells, is involved in Na+ absorption, and is responsible for the majority of bicarbonate absorption. NHE-3 is modulated by the NHE regulating factor, which interacts with further proteins, protein kinases, and the cytoskeleton. Downregulation of NHE-3 by parathyroid hormone, dopamine, and by an increase in blood pressure leads to saluresis/diuresis. The failure of dopamine to downregulate NHE-3 may cause hypertension through renal salt and water retention. NHE-3 knockouts are hypotonic and can not survive on low salt diet. In chronic acidosis, NHE-3 is upregulated possibly through increased local endothelin production. NHE4 has been found mostly in renal medulla. The precise function of this isoform, which is activated by hypertonicity and can perform K+/H+ exchange, is not clear. The segmental location and function of NHE-5 and NHE-6 in the kidney are unknown at present.
    MeSH term(s) Absorption ; Animals ; Bicarbonates/metabolism ; Humans ; Kidney/physiology ; Multigene Family/physiology ; Sodium-Hydrogen Exchangers/genetics ; Tissue Distribution
    Chemical Substances Bicarbonates ; Sodium-Hydrogen Exchangers
    Language English
    Publishing date 2002-03
    Publishing country Italy
    Document type Journal Article ; Review
    ZDB-ID 1093991-x
    ISSN 1724-6059 ; 1121-8428 ; 1120-3625
    ISSN (online) 1724-6059
    ISSN 1121-8428 ; 1120-3625
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3369: Show issues Location:
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  2. Article: Bimodal acute effects of A1 adenosine receptor activation on Na+/H+ exchanger 3 in opossum kidney cells.

    Di Sole, Francesca / Cerull, Robert / Petzke, Soeren / Casavola, Valeria / Burckhardt, Gerhard / Helmle-Kolb, Corinna

    Journal of the American Society of Nephrology : JASN

    2003  Volume 14, Issue 7, Page(s) 1720–1730

    Abstract: Regulation of renal apical Na+/H+ exchanger 3 (NHE3) activity by adenosine has been suggested to contribute to acute control of mammalian Na(+) homeostasis. The mechanism by which adenosine controls NHE3 activity in a renal cell line was examined. The ... ...

    Abstract Regulation of renal apical Na+/H+ exchanger 3 (NHE3) activity by adenosine has been suggested to contribute to acute control of mammalian Na(+) homeostasis. The mechanism by which adenosine controls NHE3 activity in a renal cell line was examined. The adenosine analog, N(6)-cyclopentyladenosine (CPA) exerts a bimodal effect on NHE3: CPA concentrations >10(-8) M inactivate NHE3, whereas concentrations <10(-8) M stimulate NHE3 activity. Acute CPA-induced control of NHE3 was blocked by antagonists of A1 adenosine receptors and inhibition of phospholipase C, pretreatment with BAPTA-AM (chelator of cellular calcium), and exposure to pertussis toxin. Stimulatory and to some extent also inhibitory CPA concentrations attenuated 8-bromo-cAMP and dopamine-mediated inhibition of NHE3. BAPTA eliminated the ability of a stimulatory dose of CPA to attenuate 8-bromo-cAMP-induced suppression of NHE3 activity. Upon inhibition of protein kinase C, CPA at an inhibitory dose provoked activation of NHE3, which is partially reverted by 8-bromo-cAMP and suppressed by pre-incubation with BAPTA-AM. Cytochalasin B, an actin-modifying agent, selectively prevented downregulation but did not affect upregulation of NHE3 activity by CPA. In conclusion, these observations demonstrate that (1) CPA modulates NHE3 activity by elevation of cellular Ca(2+) exerting a negative control on adenylate cyclase activity, (2) protein kinase C is the determining factor leading to CPA-induced downregulation of NHE3 activity, and (3) alterations of surface NHE3 abundance may contribute to A1 adenosine receptor-dependent inhibition of NHE3 activity.
    MeSH term(s) Adenosine/analogs & derivatives ; Adenosine/metabolism ; Adenosine/pharmacology ; Animals ; Calcium/metabolism ; Chelating Agents/pharmacology ; Cytochalasin B/pharmacology ; DNA, Complementary/metabolism ; Dose-Response Relationship, Drug ; Down-Regulation ; Egtazic Acid/analogs & derivatives ; Egtazic Acid/pharmacology ; Kidney/cytology ; Kidney/metabolism ; Opossums ; Pertussis Toxin/pharmacology ; Protein Kinase C/antagonists & inhibitors ; Protein Structure, Tertiary ; Receptors, Purinergic P1/metabolism ; Signal Transduction ; Sodium/metabolism ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers/metabolism ; Time Factors ; Up-Regulation
    Chemical Substances Chelating Agents ; DNA, Complementary ; Receptors, Purinergic P1 ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers ; 1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester (139890-68-9) ; Cytochalasin B (3CHI920QS7) ; N(6)-cyclopentyladenosine (41552-82-3) ; Egtazic Acid (526U7A2651) ; Sodium (9NEZ333N27) ; Pertussis Toxin (EC 2.4.2.31) ; Protein Kinase C (EC 2.7.11.13) ; Adenosine (K72T3FS567) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2003-06-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1085942-1
    ISSN 1533-3450 ; 1046-6673
    ISSN (online) 1533-3450
    ISSN 1046-6673
    DOI 10.1097/01.asn.0000072743.97583.db
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3344: Show issues Location:
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  3. Article: Molecular aspects of acute inhibition of Na(+)-H(+) exchanger NHE3 by A(2)-adenosine receptor agonists.

    Di Sole, Francesca / Cerull, Robert / Casavola, Valeria / Moe, Orson W / Burckhardt, Gerhard / Helmle-Kolb, Corinna

    The Journal of physiology

    2002  Volume 541, Issue Pt 2, Page(s) 529–543

    Abstract: Adenosine regulates Na(+) homeostasis by its acute effects on renal Na(+) transport. We have shown in heterologously transfected A6/C1 cells (renal cell line from Xenopus laevis) that adenosine-induced natriuresis may be effected partly via A(2) ... ...

    Abstract Adenosine regulates Na(+) homeostasis by its acute effects on renal Na(+) transport. We have shown in heterologously transfected A6/C1 cells (renal cell line from Xenopus laevis) that adenosine-induced natriuresis may be effected partly via A(2) adenosine receptor-mediated inactivation of the renal brush border membrane Na(+)-H(+) exchanger NHE3. In this study we utilized A6/C1 cells stably expressing wild-type as well as mutated forms of NHE3 to assess the molecular mechanism underlying A(2)-dependent control of NHE3 function. Cell surface biotinylation combined with immunoprecipitation revealed that NHE3 is targeted exclusively to the apical domain and that the endogenous Xenopus NHE is located entirely on the basolateral side of A6/C1 transfectants. Stimulation of A(2)-adenosine receptors located on the basolateral side for 15 min with CPA (N6-cyclopentyladenosine) acutely decreased NHE3 activity (microspectrofluorimety). This effect was mimicked by 8-bromo-cAMP and entirely blocked by pharmacological inhibition of PKA (with H89) or singular substitution of two PKA target sites (serine 552 and serine 605) on NHE3. Downregulation of NHE3 activity by CPA was attributable to a reduction of NHE3 intrinsic transport activity without change in surface NHE3 protein at 15 min. At 30 min, the decrease in transport activity was associated with a decrease in apical membrane NHE3 antigen. In conclusion, two highly conserved target serine sites on NHE3 determine NHE3 modulation upon A(2)-receptor activation and NHE3 inactivation by adenosine proceeds via two phases with distinct mechanisms.
    MeSH term(s) 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Adenosine/analogs & derivatives ; Adenosine/pharmacology ; Animals ; Biological Transport, Active/physiology ; Blotting, Western ; Cell Line ; Culture Media ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Down-Regulation/drug effects ; Enzyme Activation/physiology ; Enzyme Inhibitors/pharmacology ; Mice ; Purinergic P1 Receptor Agonists ; RNA, Messenger/biosynthesis ; RNA, Messenger/genetics ; Reverse Transcriptase Polymerase Chain Reaction ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers/antagonists & inhibitors ; Sodium-Hydrogen Exchangers/metabolism ; Transfection
    Chemical Substances Culture Media ; Enzyme Inhibitors ; Purinergic P1 Receptor Agonists ; RNA, Messenger ; Slc9a3 protein, mouse ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers ; 8-Bromo Cyclic Adenosine Monophosphate (23583-48-4) ; N(6)-cyclopentyladenosine (41552-82-3) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Adenosine (K72T3FS567)
    Language English
    Publishing date 2002-06-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 3115-x
    ISSN 1469-7793 ; 0022-3751
    ISSN (online) 1469-7793
    ISSN 0022-3751
    DOI 10.1113/jphysiol.2001.013438
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Acute regulation of Na/H exchanger NHE3 by adenosine A(1) receptors is mediated by calcineurin homologous protein.

    Di Sole, Francesca / Cerull, Robert / Babich, Victor / Quiñones, Henry / Gisler, Serge M / Biber, Jürg / Murer, Heini / Burckhardt, Gerhard / Helmle-Kolb, Corinna / Moe, Orson W

    The Journal of biological chemistry

    2003  Volume 279, Issue 4, Page(s) 2962–2974

    Abstract: Adenosine is an autacoid that regulates renal Na(+) transport. Activation of adenosine A(1) receptor (A(1)R) by N(6)-cyclopentidyladenosine (CPA) inhibits the Na(+)/H(+) exchanger 3 (NHE3) via phospholipase C/Ca(2+)/protein kinase C (PKC) signaling ... ...

    Abstract Adenosine is an autacoid that regulates renal Na(+) transport. Activation of adenosine A(1) receptor (A(1)R) by N(6)-cyclopentidyladenosine (CPA) inhibits the Na(+)/H(+) exchanger 3 (NHE3) via phospholipase C/Ca(2+)/protein kinase C (PKC) signaling pathway. Mutation of PKC phosphorylation sites on NHE3 does not affected regulation of NHE3 by CPA, but amino acid residues 462 and 552 are essential for A(1)R-dependent control of NHE3 activity. One binding partner of the NHE family is calcineurin homologous protein (CHP). We tested the role of NHE3-CHP interaction in mediating CPA-induced inhibition of NHE3 in opossum kidney (OK) and Xenopus laevis uroepithelial (A6) cells. Both native and transfected NHE3 and CHP are present in the same immuno-complex by co-immunoprecipitation. CPA (10(-6) M) increases CHP-NHE3 interaction by 30 - 60% (native and transfected proteins). Direct CHP-NHE3 interaction is evident by yeast two-hybrid assay (bait, NHE3(C terminus); prey, CHP); the minimal interacting region is localized to the juxtamembrane region of NHE3(C terminus) (amino acids 462-552 of opossum NHE3). The yeast data were confirmed in OK cells where truncated NHE3 (NHE3(delta552)) still shows CPA-stimulated CHP interaction. Overexpression of the polypeptide from the CHP binding region (NHE3(462-552)) interferes with the ability of CPA to inhibit NHE3 activity and to increase CHPNHE3(Full-length) interaction. Reduction of native CHP expression by small interference RNA abolishes the ability of CPA to inhibit NHE3 activity. We conclude that CHPNHE3 interaction is regulated by A(1)R activation and this interaction is a necessary and integral part of the signaling pathway between adenosine and NHE3.
    MeSH term(s) Adenosine/metabolism ; Amino Acid Sequence ; Animals ; Calcium-Binding Proteins/genetics ; Calcium-Binding Proteins/metabolism ; Cell Line ; Intracellular Space/metabolism ; Molecular Sequence Data ; Protein Transport ; Receptor, Adenosine A1/metabolism ; Saccharomyces cerevisiae ; Sequence Alignment ; Signal Transduction ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers/genetics ; Sodium-Hydrogen Exchangers/metabolism
    Chemical Substances Calcium-Binding Proteins ; Receptor, Adenosine A1 ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers ; Adenosine (K72T3FS567)
    Language English
    Publishing date 2003-10-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M306838200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.108: Show issues Location:
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