Identification of novel catecholamine absorbing proteins in the central nervous system
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Several pharmacologically active catecholamines have been shown to react covalently with CNS proteins, namely species of 47, 40, 22, and 20 kDa. Of these, the 47-kDa protein showed the greatest incorporation of tritium following treatment with [3H]dopamine, [3H]ADTN, or [3H]N-propyl-norapomorphine. Labeling was accomplished by incubating the tritiated ligands with crude membrane preparations in the absence of reducing agents. These proteins displayed several unique characteristics: 1. The proteins are distributed throughout the CNS, but no evidence was found for their presence in other tissues; 2. The proteins have a unique pharmacological profile, interacting with dopamine, ADTN, N-propyl-norapomorphine, and apomorphine, but not with ligands specific for other proteins known to interact with these compounds; 3. The labeling of these proteins is not inhibited by several similar catecholamines and other catechols, suggesting specific structural requirements; and 4. These proteins exhibited stereoselectivity with respect to this labeling. These results demonstrate the existence of novel CNS proteins capable of covalently absorbing several physiologically important catecholamines in vitro.