[Ca2+-dependent regulation of cGMP-stimulated phosphodiesterase from the soluble fraction of the human brain].
Two forms of phosphodiesterase (F1 and F2) with different regulatory properties have been isolated from the soluble fraction of human brain cortex. F1 is the Ca(2+)-calmodulin-dependent phosphodiesterase and its activity is inhibited by calmodulin antagonists (W-7, TFP, tamoxifen) via a mechanism typical for the majority of Ca(2+)-calmodulin-dependent enzymes. F2 is activated by micromolar concentrations of cGMP (7-14-fold) and by Ca2+ ions (1.5-3-fold) in the absence of exogenous calmodulin. F2 contains a tightly bound Ca(2+)-binding component (apparently calmodulin) which does not dissociate from the enzyme in the presence of EGTA. The mechanism of calmodulin antagonists action on F2 is different from that for F1.
Medvedeva
M V
MV
Bobruskin
I D
ID
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism; D002540:Cerebral Cortex / Q000201:enzymology*; D004789:Enzyme Activation; D006801:Humans
D002147:Calmodulin; D015106:3',5'-Cyclic-GMP Phosphodiesterases; D002118:Calcium
Ca2+-zavisimaia reguliatsiia cGMP-stimuliruemoĭ fosfodiésterazy iz rastvorimoĭ fraktsii mozga cheloveka.