Lung phosphodiesterase isoenzymes

N J Pyne, F Burns

Research output: Contribution to journalLiterature review

7 Citations (Scopus)

Abstract

The distinct phosphodiesterase isoenzyme activities in guinea-pig lung were identified and characterised. We demonstrate that protein kinase A catalyses the activation of lung Type V cyclic GMP phosphodiesterase. This occurs via a marked change in the Vmax for cyclic GMP hydrolysis. The sensitivity of the activated PDE to inhibition by zaprinast is also markedly reduced (zaprinast inhibits in PDE activity via a mixed mechanism). We suggest that activation of the PDE by protein kinase A involves a mechanism that leads to alteration in the regulatory action of a non-catalytic cyclic GMP binding site.
Original languageEnglish
Pages (from-to)35-49
Number of pages15
JournalAgents and actions. Supplements
Volume43
Publication statusPublished - 1993

Keywords

  • 3',5'-Cyclic-GMP Phosphodiesterases
  • animals
  • catalysis
  • enzyme activation
  • Guinea Pigs
  • isoenzymes
  • lung
  • muscle
  • perfusion
  • phosphoric diester hydrolases
  • purinones
  • pyrazines

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