| Title | Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA) | |
| Author | Anastasia Pyriochou, Antonis Tsarbopoulos and Andreas Papapetropoulos
Department of Pharmacy, University of Patras, Patras, Greece |
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| Citation | Pyriochou, A., Tsarbopoulos, A., Papapetropoulos, A.: Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA), Epitheorese Klin. Farmakol. Farmakokinet. 20(2): 311-313 (2006) | |
| Publication Date | Accepted for publication: 19-20 May 2006 | |
| Full Text Language | English | |
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| Keywords | Soluble guanylyl cyclase, phosphorylation, cAMP-dependent protein kinase, cGMP. | |
| Other Terms | review article | |
| Summary | 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 α1 and β1 sGC can be phosphorylated by PKA. | |
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| Relative Papers |
Online ISSN 1011-6575
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Articles published in this Journal are Indexed or Abstracted in: • Chemical Abstracts • Elsevier’s Bibliographic Databases: Scopus, EMBASE, EMBiology, Elsevier BIOBASE SCImago Journal and Country Rank Factor
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