Burns, F and Pyne, N J (1992) Interaction of the catalytic subunit of protein kinase A with the lung type V cyclic GMP phosphodiesterase : modulation of non-catalytic binding sites. Biochemical and Biophysical Research Communications, 189 (3). pp. 1389-1396. ISSN 1090-2104Full text not available in this repository. (Request a copy from the Strathclyde author)
We have previously demonstrated that the catalytic sub-unit of protein kinase A can catalyse a potent activation of partially purified Type V cyclic GMP-specific phosphodiesterase activity (Burns et al., 1992, Biochem. J. 283, 487-491). We now demonstrate that this phosphodiesterase most likely has a sub-unit mass of 90kDa, based upon 32P-cyclic GMP photo-affinity labelling, that activation of the phosphodiesterase does not require the prior binding of cyclic GMP to the phosphodiesterase, and that alkaline phosphatase can reverse the protein kinase A-dependent activation of phosphodiesterase activity. Zaprinast is a mixed inhibitor of non-activated cyclic GMP phosphodiesterase activity. However, inhibition of the protein kinase A-activated phosphodiesterase is competitive. These results suggest that protein kinase A can modulate the inhibitory effects of zaprinast via perturbations of a non-catalytic binding site.
|Keywords:||3',5'-cyclic-GMP phosphodiesterases, alkaline phosphatase, animals, cyclic GMP, enzyme activation, guinea pigs, isoenzymes, kinetics, lung, macromolecular substances, protein kinases, purinones, pyrazines, pyrrolidinones, rolipram, Pharmacy and materia medica, Biochemistry, Cell Biology, Molecular Biology, Biophysics|
|Subjects:||Medicine > Pharmacy and materia medica|
|Department:||Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences|
|Depositing user:||Pure Administrator|
|Date Deposited:||15 Nov 2011 05:18|
|Last modified:||04 May 2016 20:21|