Sulfation of N-Acyl Dopamines in Rat Tissues

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M. G. Akimov^*, I. V. Nazimov, N. M. Gretskaya, G. N. Zinchenko, and V. V. Bezuglov

Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia; fax: (495) 335-7103; E-mail: vvbez@mx.ibch.ru

^* To whom correspondence should be addressed.

Received November 11, 2008; Revision received December 8, 2008

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Sulfation of N-acyl dopamines has been shown for the first time in cytosolic fractions of rat liver and nervous system. Sulfation of dopamine amides of docosahexaenoic and oleic acids occurred in all tissues studied, N-arachidonoyl dopamine was sulfated in the liver and spinal cord, and N-stearoyl dopamine was sulfated only in the liver. Depending on the substrate and tissue, the sulfation activity varied from 0.5 to 3.5 nmol/min per mg total protein. Kinetic parameters of N-docosahexaenoyl dopamine sulfation in the brain were determined. The findings characterize the sulfation system as the most productive metabolic pathway of N-acyl dopamines, but the role of this system in the body is unclear because of high K_m value.

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KEY WORDS: aryl sulfotransferase, neurolipins, metabolism, liver, nervous system

DOI: 10.1134/S0006297909060133

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