Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD

C Sardet1, L Counillon, A Franchi

  • 1Centre de Biochimie-CNRS, Nice, France.

Science (New York, N.Y.)
|February 9, 1990
PubMed

Insights

The study identified the Na+/H+ antiporter as a phosphorylated glycoprotein. Its phosphorylation increases with mitogenic stimulation, suggesting a role in regulating intracellular pH.

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Biology

Background:

  • The Na+/H+ antiporter regulates intracellular pH in all cells.
  • Its activity is rapidly altered by mitogenic and oncogene activation, but the mechanism is unknown.

Purpose of the Study:

  • To investigate the molecular mechanism of Na+/H+ antiporter activation.

Main Methods:

  • Expressed a Na+/H+ antiporter cDNA fragment in E. coli as a fusion protein.
  • Developed a specific antibody against the fusion protein.
  • Utilized the antibody to detect and characterize the antiporter in mammalian cells.

Main Results:

  • Identified the Na+/H+ antiporter as a 110-kilodalton glycoprotein.
  • Demonstrated that the antiporter is phosphorylated in growing cells.
  • Showed that mitogenic activation stimulates antiporter phosphorylation, correlating with increased intracellular pH.

Conclusions:

  • The Na+/H+ antiporter is a glycoprotein whose phosphorylation is modulated by mitogenic signals.
  • This phosphorylation likely plays a role in the rapid changes in antiporter activity observed upon stimulation.

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