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A variety of phosphodiesterases hydrolyze and terminate the effects of the intracellular second messenger 3',5'-cyclic adenosine monophosphate (cAMP). Phosphodiesterase subtype 4 (PDE4) is particularly abundant in the brain and has been imaged with (11)C-(R)-rolipram, a selective inhibitor of PDE4. We sought to measure in vivo both the binding site density (B(max)) and the radioligand affinity (1/K(D)) of (11)C-(R)-rolipram in the rat brain. We also studied 2 critical factors in small-animal PET scans: the influence of anesthesia and the difference in binding under in vivo and in vitro conditions.

the journal of nuclear medicine

PET Measurement of the In Vivo Affinity of <sup>11</sup>C-(<i>R</i>)-Rolipram and the Density of Its Target, Phosphodiesterase-4, in the Brains of Conscious and Anesthetized Rats

PET Measurement of the In Vivo Affinity of 11C-(R)-Rolipram and the Density of Its Target, Phosphodiesterase-4, in the Brains of Conscious and Anesthetized Rats

PET Measurement of the In Vivo Affinity of ¹¹C-(R)-Rolipram and the Density of Its Target, Phosphodiesterase-4, in the Brains of Conscious and Anesthetized Rats