Transport of S-adenosylmethionine in isolated rat liver mitochondria.

Horne DW, Holloway RS, Wagner C
Arch Biochem Biophys. 1997 343 (2): 201-6

PMID: 9224731 · DOI:10.1006/abbi.1997.0167

Mitochondria do not have the enzyme, methionine adenosyltransferase (ATP: L-methionine S-adenosyltransferase, EC, necessary for the biosynthesis of S-adenosylmethionine. Nevertheless, about 30% of total hepatic S-adenosylmethionine resides in the mitochondria and radiolabeled S-adenosylmethionine may be isolated from the mitochondria after administration of radiolabeled methionine. This leads to the hypothesis that a carrier-mediated system is responsible for S-adenosylmethionine transport from the cytosol into the mitochondria. We have characterized such a system in isolated rat liver mitochondria. Uptake of S-adenosylmethionine consisted of two components. One component was incorporation of the methyl group into phospholipids as shown by thin-layer chromatography. The second component represented uptake into the mitochondria since addition of excess unlabeled S-adenosylmethionine resulted in efflux of labeled substrate. This countertransport is characteristic of a carrier-mediated transport system. Uptake (corrected for incorporation into phospholipids) was saturable with an apparent Km = 8.9 microM and Vmax = 54.3 pmol x mg protein(-1) x min(-1). Uptake was not inhibited by methionine, adenosine, 5'-methylthioadenosine, carnitine, choline, betaine, quinine, or hemicholinium-3. Uptake was inhibited by sinefungin and by S-adenosylhomocysteine (Ki = 53.4 microM). Uptake of S-adenosylmethionine was not dependent on the electrical potential across the mitochondrial membrane. These results indicate that S-adenosylmethionine is taken up into mitochondria via a specific, carrier-mediated system.

MeSH Terms (11)

Animals Biological Transport Carrier Proteins Kinetics Methionine Mitochondria, Liver Phospholipids Rats Rats, Sprague-Dawley S-Adenosylhomocysteine S-Adenosylmethionine

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