cGMP-dependent protein kinase protects cGMP from hydrolysis by phosphodiesterase-5.
作者： Jun KOTERA , Kennard A. GRIMES , Jackie D. CORBIN , Sharron H. FRANCIS
DOI: 10.1042/BJ20030107
关键词:
摘要: The physiological effects of cGMP are largely determined by the activities intracellular receptors, including cGMP-dependent protein kinase (PKG) and cGMP-binding cyclic nucleotide phosphodiesterases (PDEs), distribution among these receptors dictates activity signalling pathway. In present study, PKG-Ialpha or PKG-Ibeta on rate hydrolysis isolated PDE5 catalytic domain were examined. strongly inhibited with an IC(50) value 217 nM, which is similar to concentration PKG in pig coronary artery reported previously. By contrast, PKG-Ibeta, has lower affinity for than does PKG-Ialpha, approx. 1 microM. Inhibition was more effective that consistent their relative affinities cGMP. Autophosphorylation PKGs increased inhibitory its potency 10-fold compared a 2-fold increase upon autophosphorylation PKG-Ialpha. results indicate bound allosteric sites protected from persistent protection either non-phosphorylated autophosphorylated may be positive-feedback control sustain signalling.
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