Abstract
In 1928, Mary Hare isolated a new enzyme which catalyzed the oxidative deamination of tyramine (Hare 1928). She called it tyramine oxidase and speculated that it “may be protective and present for the purpose of rapid detoxification of excessive amounts of tyramine absorbed from the intestine.” Later Blashko and coworkers showed that this same enzyme also oxidized catecholamines (Blaschko et al. 1937). To reflect this more general reactivity, Zeller (1938) proposed the general name monoamine oxidase (MAO). In the years that followed its discovery, MAO was further characterized along with its role in the regulation of chemical neurotransmitters and as a target for therapeutic drugs and toxic substances. More recently its genetics have been studied. This chapter will focus on general aspects of MAO, on the development of radiotracers for imaging MAO A and MAO B, and on PET studies of MAO in the human brain.
Reprinted from Methods, vol. 27, Fowler JS, Logan J, Volkow ND, Wang GJ, MacGregor RR, Ding YS, Monoamine oxidase: radiotracer development and human studies, pp. 263-277, 2002, with permission of Elsevier Science
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Fowler, J.S., Logan, J., Volkow, N.D., Wang, GJ., MacGregor, R.R., Ding, YS. (2003). Monoamine Oxidase: Radiotracer Development and Human Studies. In: Feinendegen, L.E., Shreeve, W.W., Eckelman, W.C., Bahk, YW., Wagner, H.N. (eds) Molecular Nuclear Medicine. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-55539-8_20
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