Characterization of cyclic nucleotide phosphodiesterases from cultured bovine aortic endothelial cells.

摘要: Abstract Experiments were carried out in order to isolate and characterize the cyclic nucleotide phosphodiesterase activities primary low passages of cultured bovine aortic endothelial cells. The subcellular characterization hydrolytic activity showed that both cAMP cGMP predominant cytosolic rather than particulate fraction cell homogenate. At a substrate concentration (0.25 μM), major was for while at high (20 μM) it cGMP. Both insensitive calmodulin. Cytosolic resolved into two distinct forms using HPLC. first eluted form designated cGS-PDE: hydrolysed its markedly enhanced by presence second cAMP-PDE: selectively cAMP. cAMP-PDE inhibited micromolar concentrations inhibitors such as trequinsin, rolipram, dipyridamole or papaverine. cGS-PDE papaverine except hydrolysis which range. relatively selective cGMP-PDE inhibitor, zaprinast about 750-fold less potent on PDEs smooth muscle cGMP-PDE. identification specific PDE different may allow better understanding regulation role nucleotides