Affiliation:
1. Department of Anatomy and Physiology, University of Dundee, Scotland,United Kingdom.
Abstract
We have identified both N-ethylmaleimide (NEM)-resistant (system T) and NEM-sensitive (system L1) L-[3H]tryptophan transporters in sinusoidal membrane vesicles (SMVs) from euthyroid, hypothyroid (propylthiouracil-treated), and hyperthyroid [L-3,5,3'-triiodothyronine (L-T3)-injected] rats. L-[125I]T3 associates with SMVs largely by surface binding. Kinetic characteristics of tryptophan uptake and T3 binding (transporter or receptor abundance and substrate affinity) are not significantly affected by thyroid status. T3 and thyroxine (T4) inhibit NEM-resistant tryptophan uptake in SMVs to an extent dependent on the thyroid status of the donor rat, increasing in the order hypothyroid < euthyroid < hyperthyroid; the inhibitor constant for this inhibition (0.3 microM T3) is equal to the dissociation constant for T3 binding. Both T3 binding and T3 inhibition of tryptophan transport in SMVs are markedly reduced by treatments (Triton X-100 or trypsin) that do not significantly affect vesicle integrity or transport of tryptophan and glucose. T3 and/or T4 transport at the liver-plasma interface may be facilitated by direct interactions between hormone receptors and system T transporter proteins. Modulation of such interactions may be important for control of hepatic T4 and/or T3 turnover and aromatic amino acid metabolism during altered thyroid status.
Publisher
American Physiological Society
Subject
Physiology (medical),Physiology,Endocrinology, Diabetes and Metabolism
Cited by
14 articles.
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