The links between cellular Ca2+ and Na+/H+ exchange in the pathophysiology of essential hypertension

Research output: Contribution to journalReview article

25 Citations (Scopus)

Abstract

This review focuses on the mechanisms whereby the cytosolic Ca2+ regulates the ubiquitous Na+/H+ exchanger (NHE-1) and how these regulatory processes might modify the behavior of NHE-1 in essential hypertension. The pH setpoint for activation of the Na+/H+ exchanger is controlled by two interrelated and Ca2+-dependent pathways, namely, the protein kinase/phosphatase cascade and Ca2+/calmodulin. The cytoplasmic domain of NHE-1 contains elements responsive to serine/theorine kinases and a high affinity binding site to Ca2+/calmodulin. Phosphorylation of NHE-1 or the binding of the Ca2+/calmodulin complex to its binding site promotes an alkaline shift in the pH setpoint for the exchanger. It is suggested that, in essential hypertension, an increased cellular Ca2+ load or an enhanced external Ca2+ entry stimulate the NHE-1 through protein kinase/phosphatase and Ca2+/calmodulin systems, thereby increasing its activity.

Original languageEnglish (US)
Pages (from-to)703-707
Number of pages5
JournalAmerican journal of hypertension
Volume9
Issue number7
DOIs
StatePublished - Jan 1 1996

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Calmodulin
Sodium-Hydrogen Antiporter
Phosphoprotein Phosphatases
Protein Kinases
Binding Sites
Protein-Serine-Threonine Kinases
Phosphorylation
Essential Hypertension

All Science Journal Classification (ASJC) codes

  • Internal Medicine

Keywords

  • Calcium
  • calmodulin
  • hypertension
  • pH
  • serine/theorine kinase
  • sodium-hydrogen exchanger

Cite this

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abstract = "This review focuses on the mechanisms whereby the cytosolic Ca2+ regulates the ubiquitous Na+/H+ exchanger (NHE-1) and how these regulatory processes might modify the behavior of NHE-1 in essential hypertension. The pH setpoint for activation of the Na+/H+ exchanger is controlled by two interrelated and Ca2+-dependent pathways, namely, the protein kinase/phosphatase cascade and Ca2+/calmodulin. The cytoplasmic domain of NHE-1 contains elements responsive to serine/theorine kinases and a high affinity binding site to Ca2+/calmodulin. Phosphorylation of NHE-1 or the binding of the Ca2+/calmodulin complex to its binding site promotes an alkaline shift in the pH setpoint for the exchanger. It is suggested that, in essential hypertension, an increased cellular Ca2+ load or an enhanced external Ca2+ entry stimulate the NHE-1 through protein kinase/phosphatase and Ca2+/calmodulin systems, thereby increasing its activity.",
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The links between cellular Ca2+ and Na+/H+ exchange in the pathophysiology of essential hypertension. / Aviv, Abraham.

In: American journal of hypertension, Vol. 9, No. 7, 01.01.1996, p. 703-707.

Research output: Contribution to journalReview article

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