Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA)

Anastasia Pyriochou, Antonis Tsarbopoulos, Andreas Papapetropoulos

Research output: Contribution to journalArticle

Abstract

Soluble guanylyl cyclase (sGC) has been shown to be regulated by transcriptional, post-transcriptional and post-translational mechanisms. Post-translationally sGC activity and subcellular localization is regulated by both phosphorylation and protein-protein interactions. The aim of the present study was to determine whether sGC is a cAMP-dependent protein kinase (PKA) substrate. We provide evidence that both of and β1 sGC can be phosphorylated by PKA.

Original languageEnglish (US)
Pages (from-to)311-313
Number of pages3
JournalReview of Clinical Pharmacology and Pharmacokinetics, International Edition
Volume20
Issue number2
StatePublished - Jun 6 2006
Externally publishedYes

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Cyclic AMP-Dependent Protein Kinases
Phosphorylation
Protein Kinases
Proteins
Soluble Guanylyl Cyclase

Keywords

  • cAMP-dependent protein kinase
  • cGMP
  • Phosphorylation
  • Soluble guanylyl cyclase

ASJC Scopus subject areas

  • Pharmacology (medical)

Cite this

Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA). / Pyriochou, Anastasia; Tsarbopoulos, Antonis; Papapetropoulos, Andreas.

In: Review of Clinical Pharmacology and Pharmacokinetics, International Edition, Vol. 20, No. 2, 06.06.2006, p. 311-313.

Research output: Contribution to journalArticle

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