Lung phosphodiesterase isoenzymes

Pyne, N J and Burns, F (1993) Lung phosphodiesterase isoenzymes. Agents and actions. Supplements, 43. pp. 35-49. ISSN 0379-0363

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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.

ORCID iDs

Pyne, N J ORCID logoORCID: https://orcid.org/0000-0002-5657-4578 and Burns, F;
CORE (COnnecting REpositories)