Pyne, N J and Burns, F (1993) Lung phosphodiesterase isoenzymes. Agents and actions. Supplements, 43. pp. 35-49. ISSN 0379-0363Full text not available in this repository. (Request a copy from the Strathclyde author)
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.
|Keywords:||3',5'-Cyclic-GMP Phosphodiesterases, animals, catalysis, enzyme activation, Guinea Pigs, isoenzymes, lung, muscle, perfusion, phosphoric diester hydrolases, purinones, pyrazines, Therapeutics. Pharmacology, Pharmacology (medical)|
|Subjects:||Medicine > Therapeutics. Pharmacology|
|Department:||Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences|
|Depositing user:||Pure Administrator|
|Date Deposited:||15 Nov 2011 05:18|
|Last modified:||06 Jan 2017 10:14|