Evidence for involvement of the putative first extracellular loop in differential volume sensitivity of the Na+/H+ exchangers NHE1 and NHE2

Biochemistry. 2003 Feb 4;42(4):1086-94. doi: 10.1021/bi020427d.

Abstract

We studied hyperosmolarity-induced changes in cell volume and cytoplasmic pH in PS120 cells expressing Na(+)/H(+) exchanger (NHE) isoforms and their mutants. Change in cell volume was estimated by measuring change in cell height by means of confocal microscopy. Regulatory volume increase (RVI) and cytoplasmic alkalinization were observed in cells expressing NHE1 but not in cells expressing NHE2 or NHE3. Studies using chimeric exchangers revealed that the membrane domain of the exchanger is responsible for the difference in volume sensitivity between NHE1 and NHE2. Although deletion or point mutation within the first extracellular loop of NHE1 did not affect RVI and alkalinization, point mutations within the corresponding region of NHE2, particularly a region containing aa 41-53, as well as replacement of the N-terminus of NHE2 with the corresponding region of NHE1, rendered NHE2 responsive to the activating effect of cell shrinkage. Thus, the membrane domain plays an important role in the response of the exchanger to cell shrinkage. The data suggest that the putative first extracellular loop of NHE2, but not that of NHE1, may exert an inhibitory influence on hyperosmolarity-induced activation of the exchanger and thereby block RVI.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Adhesion / genetics
  • Cell Adhesion / physiology
  • Cell Line
  • Cell Size / genetics
  • Cell Size / physiology
  • Cricetinae
  • Extracellular Space / chemistry*
  • Extracellular Space / physiology*
  • Humans
  • Hydrogen-Ion Concentration
  • Intracellular Fluid / chemistry
  • Intracellular Fluid / physiology
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Osmotic Pressure
  • Protein Isoforms / biosynthesis
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / physiology
  • Protein Structure, Tertiary / genetics
  • Rats
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / genetics
  • Sodium-Hydrogen Exchangers / biosynthesis
  • Sodium-Hydrogen Exchangers / chemistry*
  • Sodium-Hydrogen Exchangers / genetics
  • Sodium-Hydrogen Exchangers / physiology*
  • Transfection

Substances

  • Protein Isoforms
  • Recombinant Fusion Proteins
  • SLC9A2 protein, human
  • Slc9a2 protein, rat
  • Sodium-Hydrogen Exchangers
  • growth factor-activatable Na-H exchanger NHE-1