Summary
Catecholamine inactivating enzymes in red blood cells are preferentially localized in the reticulocytes and not in mature erythrocytes: catechol-O-methyltransferase (COMT) activity in erythrocyte ghost preparations from reticulocyte-rich blood of rats pretreated with acetyl-phenylhydrazine was found to be 5 times higher than in ghosts from reticulocyte-poor blood. In the respective 12000×g supernates of the haemolysates, COMT activity in reticulocyte-rich preparations was not significantly enhanced. Significant monoamine oxidase (MAO) activity was only found in ghosts from reticulocyte-rich blood prepared by centrifugation at 12000×g. MAO activity was inhibited in vitro by pargyline concentrations<10−6 M.
These results are in agreement with earlier findings which have shown that rat reticulocytes contain a complete adrenergic β-receptor-effector system.
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Quiring, K., Kaiser, G., Gauger, D. et al. Catecholamine-inactivating enzymes in rat reticulocytes. Naunyn-Schmiedeberg's Arch. Pharmacol. 279, 93–97 (1973). https://doi.org/10.1007/BF00502072
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DOI: https://doi.org/10.1007/BF00502072