Apical ammonia transport by the mouse inner medullary collecting duct cell (mIMCD-3)

Am J Physiol Renal Physiol. 2005 Aug;289(2):F347-58. doi: 10.1152/ajprenal.00253.2004. Epub 2005 Mar 29.

Abstract

The collecting duct is the primary site of urinary ammonia secretion; the current study determines whether apical ammonia transport in the mouse inner medullary collecting duct cell (mIMCD-3) occurs via nonionic diffusion or a transporter-mediated process and, if the latter, presents the characteristics of this apical ammonia transport. We used confluent cells on permeable support membranes and examined apical uptake of the ammonia analog [(14)C]methylammonia ([(14)C]MA). mIMCD-3 cells exhibited both diffusive and saturable, transporter-mediated, nondiffusive apical [(14)C]MA transport. Transporter-mediated [(14)C]MA uptake had a K(m) of 7.0 +/- 1.5 mM and was competitively inhibited by ammonia with a K(i) of 4.3 +/- 2.0 mM. Transport activity was stimulated by both intracellular acidification and extracellular alkalinization, and it was unaltered by changes in membrane voltage, thereby functionally identifying an apical, electroneutral NH(4)(+)/H(+) exchange activity. Transport was bidirectional, consistent with a role in ammonia secretion. In addition, transport was not altered by Na(+) or K(+) removal, not inhibited by luminal K(+), and not mediated by apical H(+)-K(+)-ATPase, Na(+)-K(+)-ATPase, or Na(+)/H(+) exchange. Finally, mIMCD-3 cells express the recently identified ammonia transporter family member Rh C glycoprotein (RhCG) at its apical membrane. These studies indicate that the renal collecting duct cell mIMCD-3 has a novel apical, electroneutral Na(+)- and K(+)-independent NH(4)(+)/H(+) exchange activity, possibly mediated by RhCG, that is likely to mediate important components of collecting duct ammonia secretion.

Publication types

  • Research Support, N.I.H., Extramural
  • 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.

MeSH terms

  • Acids / pharmacology
  • Algorithms
  • Ammonia / metabolism*
  • Animals
  • Binding, Competitive / drug effects
  • Biological Transport, Active
  • Biotin / metabolism
  • Carrier Proteins / metabolism
  • Cation Transport Proteins / metabolism
  • Cell Line
  • H(+)-K(+)-Exchanging ATPase / metabolism
  • Hydrogen-Ion Concentration
  • Immunoblotting
  • Kidney Medulla / metabolism*
  • Kidney Tubules, Collecting / metabolism*
  • Membrane Glycoproteins / metabolism
  • Membrane Potentials / physiology
  • Membranes / metabolism
  • Methylamines / metabolism
  • Mice
  • Microscopy, Fluorescence
  • Models, Statistical
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sodium-Hydrogen Exchanger 3
  • Sodium-Hydrogen Exchangers / metabolism

Substances

  • Acids
  • Carrier Proteins
  • Cation Transport Proteins
  • Membrane Glycoproteins
  • Methylamines
  • Rhcg protein, mouse
  • Sodium-Hydrogen Exchanger 3
  • Sodium-Hydrogen Exchangers
  • Biotin
  • Ammonia
  • methylamine
  • H(+)-K(+)-Exchanging ATPase