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Isoform Selectivity of 3-¹²⁵I-Iodo--Methyl-L-Tyrosine Membrane Transport in Human L-Type Amino Acid Transporters

¹ Department of Radiological Sciences, Ibaraki Prefectural University of Health Sciences, Ibaraki, Japan
² Department of Pharmacology and Toxicology, Kyorin University School of Medicine, Tokyo, Japan
³ School of Health Sciences, Faculty of Medicine, Kanazawa University, Kanazawa, Japan

ABSTRACT

3-¹²³I-Iodo--methyl-L-tyrosine (¹²³I-IMT) has been developed for SPECT of amino acid transport imaging. We examined the isoform selectivity of ¹²⁵I-IMT transport of the 2 human L-type amino acid transporters, hLAT1 and hLAT2, with human 4F2hc-coexpressed Xenopus laevis oocytes. Methods: An uptake study of ¹²⁵I-IMT was performed using transporter-expressed X. laevis oocytes. Oocytes were injected with 17.6 ng of hLAT1 or hLAT2 complementary RNA (cRNA) and 7.4 ng of h4F2hc cRNA in a molar ratio of 1:1. Two days after injection, the uptake of ¹²⁵I-IMT was measured in the Na⁺-free uptake solution containing 18.5 kBq of noncarrier-added ¹²⁵I-IMT. After incubation for 30 min at room temperature, radioactivity of the oocytes was determined. Results: Of the 2 hLAT isoforms and h4F2hc-coexpressed X. laevis oocytes, ¹²⁵I-IMT uptake via hLAT1 was 5.95-fold higher than that via hLAT2 (P < 0.005). Conclusion: ¹²⁵I-IMT transport was hLAT1 selective. Investigations on the isoform selectivity of ¹²⁵I-IMT transport with other transporters are anticipated.

Key Words: membrane transport • 3-¹²⁵I-iodo--methyl-L-tyrosine • human L-type amino acid transporter family • human 4F2hc • Xenopus laevis oocyte

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