Abstract
Thyroid hormones enter isolated white adipocytes largely by a System L1-type amino acid transporter en route to exerting genomic actions. Differentiated 3T3-L1 mouse adipocytes in culture express mRNA for LAT1 (the catalytic subunit of high-affinity System L1). L-[125I]-T3 uptake into 3T3-L1 adipocytes included a substantial saturable component inhibited by leucine. L-[3H]phenylalanine uptake into 3T3-L1 cells was saturable (K m of 31 μM), competitively inhibited by T3 (K i of 1.2 μM) and blocked by leucine, BCH, and rT3 as expected for substrate interactions of System L1. Efflux of preloaded L-[3H]phenylalanine from 3T3-L1 adipocytes was trans stimulated by external leucine, demonstrating the obligatory exchange mechanism of System L1 transport. T3 (10 μM) did not significantly trans stimulate L-[3H]phenylalanine efflux, but did competitively inhibit the trans stimulatory effect of 10 μM leucine. The results highlight strong competitive interactions between iodothyronines (T3, rT3) and amino acids for transport by System L1 in adipocytes, which may impact cellular iodothyronine exchanges during altered states of protein nutrition.
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