Interaction of the catalytic subunit of protein kinase A with the lung type V cyclic GMP phosphodiesterase: modulation of non-catalytic binding sites

F Burns, N J Pyne

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20 Citations (Scopus)

Abstract

We have previously demonstrated that the catalytic sub-unit of protein kinase A can catalyse a potent activation of partially purified Type V cyclic GMP-specific phosphodiesterase activity (Burns et al., 1992, Biochem. J. 283, 487-491). We now demonstrate that this phosphodiesterase most likely has a sub-unit mass of 90kDa, based upon 32P-cyclic GMP photo-affinity labelling, that activation of the phosphodiesterase does not require the prior binding of cyclic GMP to the phosphodiesterase, and that alkaline phosphatase can reverse the protein kinase A-dependent activation of phosphodiesterase activity. Zaprinast is a mixed inhibitor of non-activated cyclic GMP phosphodiesterase activity. However, inhibition of the protein kinase A-activated phosphodiesterase is competitive. These results suggest that protein kinase A can modulate the inhibitory effects of zaprinast via perturbations of a non-catalytic binding site.
Original languageEnglish
Pages (from-to)1389-1396
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume189
Issue number3
DOIs
Publication statusPublished - 30 Dec 1992

Keywords

  • 3',5'-cyclic-GMP phosphodiesterases
  • alkaline phosphatase
  • animals
  • cyclic GMP
  • enzyme activation
  • guinea pigs
  • isoenzymes
  • kinetics
  • lung
  • macromolecular substances
  • protein kinases
  • purinones
  • pyrazines
  • pyrrolidinones
  • rolipram

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