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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.

Item type: Article
ID code: 34911
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
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    Depositing user: Pure Administrator
    Date Deposited: 15 Nov 2011 05:18
    Last modified: 01 Oct 2014 16:57
    URI: http://strathprints.strath.ac.uk/id/eprint/34911

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