Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2006-4-24
pubmed:abstractText
The recently cloned, non-erythrocyte Rh glycoproteins (Rhbg and Rhcg) are expressed in the intercalated cells of the renal collecting duct. The apical Rhcg and the basolateral Rhbg are likely involved in NH3 and/or NH4+ transport, yet the characteristics of this transport are not yet certain. In this study we investigated the mechanism of NH4+ transport by Rhbg and Rhcg expressed in Xenopus oocytes. We used a two-electrode voltage-clamp and ion-selective microelectrodes to measure NH4+-induced currents (I(NH4)) and changes in pHi, respectively. In oocytes expressing Rhcg, exposure to bath [NH4+] of 2.5-20 mM induced inward currents that were slightly more than those in H2O-injected (control) oocytes. I-V plots in the presence of NH4+ showed a small increase in slope conductance only at positive potentials. On the other hand, in oocytes expressing Rhbg, 5 mM NH4+ induced an inward I(NH4) of -79 nA, decreased pHi (DeltapHi) by 0.13 at a rate (dpHi/dt) of -2 7 x 10(-4) pH/s and depolarized the cell by 45 mV. These changes were significantly more than those in control oocytes. I-V plots in the presence of NH4+ showed substantial increase in conductance. Amiloride (1 mM) inhibited I(NH4), DeltapHi and dpHi/dt in oocytes expressing Rhbg but not in control oocytes. Raising bath [NH4+] in increments from 1 to 20 mM elicited a faster dpHi/dt, a larger decrease in pHi and a larger depolarization. Net NH4+ flux by Rhbg (estimated from dpHi/dt) was proportional to [NH4+] gradient and followed saturation kinetics with an apparent Km of 2.3 mM. Methyl ammonium (5 mM) induced a current of -63 nA in Rhbg oocytes but did not cause any change in control oocytes. These data indicate that: 1) Rhbg transport of NH4+ is electrogenic. 2) Methyl ammonium is transported by Rhbg. 3) NH4+ transport by Rhbg is saturated at high concentrations with Michaelis-Menten kinetics.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amiloride, http://linkedlifedata.com/resource/pubmed/chemical/Ammonia, http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane 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/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RhBG protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Rhcg protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Channel Blockers, http://linkedlifedata.com/resource/pubmed/chemical/methylamine
pubmed:status
MEDLINE
pubmed:issn
1246-7820
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
147-53
pubmed:meshHeading
pubmed-meshheading:16580864-Amiloride, pubmed-meshheading:16580864-Ammonia, pubmed-meshheading:16580864-Animals, pubmed-meshheading:16580864-Biological Transport, pubmed-meshheading:16580864-Cation Transport Proteins, pubmed-meshheading:16580864-Female, pubmed-meshheading:16580864-Glycoproteins, pubmed-meshheading:16580864-Hydrogen-Ion Concentration, pubmed-meshheading:16580864-Ion Transport, pubmed-meshheading:16580864-Kidney, pubmed-meshheading:16580864-Kinetics, pubmed-meshheading:16580864-Membrane Glycoproteins, pubmed-meshheading:16580864-Membrane Transport Proteins, pubmed-meshheading:16580864-Methylamines, pubmed-meshheading:16580864-Mice, pubmed-meshheading:16580864-Oocytes, pubmed-meshheading:16580864-Osmolar Concentration, pubmed-meshheading:16580864-Patch-Clamp Techniques, pubmed-meshheading:16580864-Quaternary Ammonium Compounds, pubmed-meshheading:16580864-Recombinant Fusion Proteins, pubmed-meshheading:16580864-Sodium Channel Blockers, pubmed-meshheading:16580864-Transfection, pubmed-meshheading:16580864-Xenopus laevis
pubmed:articleTitle
Electrogenic ammonium transport by renal Rhbg.
pubmed:affiliation
Department of Medicine, Section of Nephrology, SL-45, Tulane University School of Medicine, 1430 Tulane Avenue, New Orleans, LA 70112, USA. nakhoul@tulane.edu
pubmed:publicationType
Journal Article