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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

View larger version (29K): [in a new window]   FIGURE 1. Expected structure of functional unit of L-type amino acid transporter. Human 4F2 heavy chain (CD98; h4F2hc), type II membrane glycoprotein, has molecular weight of approximately 80 kDa. This protein facilitates transport of 125I-IMT by forming heterodimer by disulfide bond with light chain. Light chain has molecular weight of approximately 40 kDa. Human LAT1 and hLAT2 (light chains) have putative 12 transmembrane domains. Complementary DNAs of these transporters have been cloned.

View larger version (30K): [in a new window]   FIGURE 2. Comparison of isoform selectivity of 125I-IMT transport (A) and L-14C(U)-Tyr (B) in hLAT1 or hLAT2 and h4F2hc-coexpressing X. laevis oocytes (water-injected oocytes acted as control). Uptake of radiolabeled amino acids was measured in Na+-free uptake solution containing 18.5 kBq 125I-IMT or L-14C(U)-Tyr. 125I-IMT transport showed hLAT1-h4F2hc selectivity. *P < 0.05; **P < 0.005.