Molecular cloning of NHE1 from winter flounder RBCs: Activation by osmotic shrinkage, cAMP, and calyculin A

Stine F. Pedersen, Scott A. King, Robert R. Rigor, Zhenpeng Zhuang, Jaimie M. Warren, Peter M Cala

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

In this report, we describe the cloning, cellular localization, and functional characteristics of Na+/H+ exchanger 1 (NHE1) from red blood cells of the winter flounder Pseudopleuronectes americanus (paNHE1). The paNHE1 protein localizes primarily to the marginal band and exhibits a 74% similarity to the trout β-NHE, and 65% to the human NHE1 (hNHE1). Functionally, paNHE1 shares characteristics of both β-NHE and hNHE1 in that it is activated both by manipulations that increase cAMP and by cell shrinkage, respectively. In accordance, the paNHE1 protein exhibits both protein kinase A consensus sites as in β-NHE and a region of high homology to that required for shrinkagedependent activation of hNHE1. After shrinkage-dependent activation of paNHE1 and resulting activation of a Cl-/ HCO3 - exchanger, their parallel operation results in net uptake of NaCl and osmotically obliged water. Activation of paNHE1 by cAMP is at least additive to that elicited by osmotic shrinkage, suggesting that these stimuli regulate paNHE1 by distinct mechanisms. Finally, exposure to the serine/threonine phosphatase inhibitor calyculin A potently activates paNHE1, and this activation is also additive to that induced by shrinkage or cAMP.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Cell Physiology
Volume284
Issue number6 53-6
StatePublished - Jun 1 2003

Keywords

  • β-Na/H exchanger
  • Protein kinase A
  • Protein kinase C
  • Protein phosphatases
  • Red blood cells
  • Sodium-proton antiport

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology

Fingerprint Dive into the research topics of 'Molecular cloning of NHE1 from winter flounder RBCs: Activation by osmotic shrinkage, cAMP, and calyculin A'. Together they form a unique fingerprint.

  • Cite this