Source:http://linkedlifedata.com/resource/pubmed/id/20810915
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
2010-12-1
|
pubmed:abstractText |
Rhbg is a membrane glycoprotein that is involved in NH(3)/NH(4)(+) transport. Several models have been proposed to describe Rhbg, including an electroneutral NH(4)(+)/H(+) exchanger, a uniporter, an NH(4)(+) channel, or even a gas channel. In this study, we characterized the pH sensitivity of Rhbg expressed in Xenopus oocytes. We used two-electrode voltage clamp and ion-selective microelectrodes to measure NH(4)(+)-induced [and methyl ammonium (MA(+))] currents and changes in intracellular pH (pH(i)), respectively. In oocytes expressing Rhbg, 5 mM NH(4)Cl (NH(3)/NH(4)(+)) at extracellular pH (pH(o)) of 7.5 induced an inward current, decreased pH(i), and depolarized the cell. Raising pH(o) to 8.2 significantly enhanced the NH(4)(+)-induced current and pH(i) changes, whereas decreasing bath pH to 6.5 inhibited these changes. Lowering pH(i) (decreased by butyrate) also inhibited the NH(4)(+)-induced current and pH(i) decrease. In oocytes expressing Rhbg, 5 mM methyl amine hydrochloride (MA/MA(+)), often used as an NH(4)Cl substitute, induced an inward current, a pH(i) increase (not a decrease), and depolarization of the cell. Exposing the oocyte to MA/MA(+) at alkaline bath pH (8.2) enhanced the MA(+)-induced current, whereas lowering bath pH to 6.5 inhibited the MA(+) current completely. Exposing the oocyte to MA/MA(+) at low pH(i) abolished the MA(+)-induced current and depolarization; however, pH(i) still increased. These data indicate that 1) transport of NH(4)(+) and MA/MA(+) by Rhbg is pH sensitive; 2) electrogenic NH(4)(+) and MA(+) transport are stimulated by alkaline pH(o) but inhibited by acidic pH(i) or pH(o); and 3) electroneutral transport of MA by Rhbg is likely but is less sensitive to pH changes.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Butyrates,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Methylamines,
http://linkedlifedata.com/resource/pubmed/chemical/Quaternary Ammonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/RhBG protein, mouse
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
1522-1563
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
299
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
C1386-97
|
pubmed:dateRevised |
2011-2-14
|
pubmed:meshHeading |
pubmed-meshheading:20810915-Animals,
pubmed-meshheading:20810915-Butyrates,
pubmed-meshheading:20810915-Glycoproteins,
pubmed-meshheading:20810915-Hydrogen-Ion Concentration,
pubmed-meshheading:20810915-Membrane Potentials,
pubmed-meshheading:20810915-Membrane Transport Proteins,
pubmed-meshheading:20810915-Methylamines,
pubmed-meshheading:20810915-Mice,
pubmed-meshheading:20810915-Quaternary Ammonium Compounds
|
pubmed:year |
2010
|
pubmed:articleTitle |
pH sensitivity of ammonium transport by Rhbg.
|
pubmed:affiliation |
Section of Nephrology, Department of Medicine, Tulane Hypertension and Renal Center of Excellence, Tulane University School of Medicine, New Orleans, Louisiana 70112, USA. nakhoul@tulane.edu
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|