Pyne, N J and Burns, F (1993) Lung phosphodiesterase isoenzymes. Agents and actions. Supplements, 43. pp. 35-49. ISSN 0379-0363
Full text not available in this repository. (Request a copy from the Strathclyde author)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 |
| Subjects: | Medicine > Therapeutics. Pharmacology |
| Department: | Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences |
| Related URLs: | |
| Depositing user: | Pure Administrator |
| Date Deposited: | 15 Nov 2011 05:18 |
| Last modified: | 12 Mar 2012 11:37 |
| URI: | http://strathprints.strath.ac.uk/id/eprint/34911 |
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