Acute regulation of Na/H exchanger NHE3 by adenosine A(1) receptors is mediated by calcineurin homologous protein. 2004

Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
Department of Internal Medicine, University of Texas Southwestern, Dallas, Texas 75390-8856, USA. Francesca.DiSole@UTsouthwestern.edu

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.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D002135 Calcium-Binding Proteins Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS. Calcium Binding Protein,Calcium-Binding Protein,Calcium Binding Proteins,Binding Protein, Calcium,Binding Proteins, Calcium,Protein, Calcium Binding,Protein, Calcium-Binding
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D000074083 Sodium-Hydrogen Exchanger 3 A sodium-hydrogen antiporter expressed primarily by EPITHELIAL CELLS in the kidneys, it localizes to the apical membrane of the PROXIMAL KIDNEY TUBULE, where it functions in sodium and water reabsorption and possibly calcium homeostasis. It also is expressed in heart, brain, and lung tissues and is resistant to AMILORIDE inhibition. NHE-3 Protein,Na(+)-H(+) Exchanger 3,SLC9A3 Protein,Solute Carrier Family 9 Member 3,NHE 3 Protein,Sodium Hydrogen Exchanger 3
D000241 Adenosine A nucleoside that is composed of ADENINE and D-RIBOSE. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter. Adenocard,Adenoscan
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker
D015398 Signal Transduction The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway. Cell Signaling,Receptor-Mediated Signal Transduction,Signal Pathways,Receptor Mediated Signal Transduction,Signal Transduction Pathways,Signal Transduction Systems,Pathway, Signal,Pathway, Signal Transduction,Pathways, Signal,Pathways, Signal Transduction,Receptor-Mediated Signal Transductions,Signal Pathway,Signal Transduction Pathway,Signal Transduction System,Signal Transduction, Receptor-Mediated,Signal Transductions,Signal Transductions, Receptor-Mediated,System, Signal Transduction,Systems, Signal Transduction,Transduction, Signal,Transductions, Signal
D016415 Sequence Alignment The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms. Sequence Homology Determination,Determination, Sequence Homology,Alignment, Sequence,Alignments, Sequence,Determinations, Sequence Homology,Sequence Alignments,Sequence Homology Determinations

Related Publications

Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
May 1999, The American journal of physiology,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
January 2002, Nephrologie,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
May 2010, American journal of physiology. Renal physiology,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
August 2011, American journal of physiology. Cell physiology,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
August 2009, Journal of the American Society of Nephrology : JASN,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
October 2000, The Journal of biological chemistry,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
March 2006, American journal of physiology. Cell physiology,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
December 1999, The Journal of biological chemistry,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
February 2007, American journal of physiology. Renal physiology,
Francesca Di Sole, and Robert Cerull, and Victor Babich, and Henry Quiñones, and Serge M Gisler, and Jürg Biber, and Heini Murer, and Gerhard Burckhardt, and Corinna Helmle-Kolb, and Orson W Moe
April 2006, Biochimica et biophysica acta,
Copied contents to your clipboard!