Monoclonal antibodies specific for monoamine oxidase (MAO) A and MAO B, respectively, were used to localize these enzymes in primate brain. The reagents recognized different populations of neurons: those that recognized MAO A were located in cell groups containing catecholamines, including the substantia nigra, nucleus locus coeruleus, nucleus subcoeruleus, and the periventricular region of the hypothalamus, whereas those that recognized MAO B were observed in serotonin regions, including the nucleus raphe dorsalis and nucleus centralis superior. These data illustrate the physiological independence of MAO A and B and show that neurons may be specialized for their degradative as well as their synthetic functions.

Monoamine oxidase (EC 1

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Tyrosine hydroxylase (TH, tyrosine 3-monooxygenase; EC 1.14.16.2) activity in crude extracts of rat pheochromocytoma, rat brain, and bovine adrenal medulla can be immunoprecipitated in an indirect assay by monoclonal antibodies prepared against partially purified rat pheochromocytoma TH. One of these monoclonal antibodies, TH-2D8-2, can be used for immunocytochemical localization of TH in cell bodies, dendrites, and axons in catecholaminergic neurons (e.g., cells in the substantia nigra) of rat brain and in the cell body, neurites, and growth cones of rat pheochromocytoma cells after treatment with nerve growth factor. When linked to Affi-gel 10, this monoclonal antibody can also be used for immunoaffinity purification of rat and bovine TH. These results suggest that TH-2D8-2 is a valuable reagent with which to investigate the localization, physiological regulation, and function of this important enzyme.

No abstract