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Titolo:
Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters
Autore:
Kim, DK; Kanai, Y; Chairoungdua, A; Matsuo, H; Cha, SH; Endou, H;
Indirizzi:
Kyorin Univ, Sch Med, Dept Pharmacol & Toxicol, Mitaka, Tokyo 1818611, Japan Kyorin Univ Mitaka Tokyo Japan 1818611 icol, Mitaka, Tokyo 1818611, Japan Natl Def Med Coll, Dept Physiol 1, Tokorozawa, Saitama 3598513, Japan NatlDef Med Coll Tokorozawa Saitama Japan 3598513 Saitama 3598513, Japan Japan Sci & Technol Corp, PRESTO, Mitaka, Tokyo 1818611, Japan Japan Sci &Technol Corp Mitaka Tokyo Japan 1818611 Tokyo 1818611, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 20, volume: 276, anno: 2001,
pagine: 17221 - 17228
SICI:
0021-9258(20010518)276:20<17221:ECOANA>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
XENOPUS-LAEVIS OOCYTES; AFFINITY GLUTAMATE TRANSPORTER; RAT SMALL-INTESTINE; 4F2 HEAVY-CHAIN; MONOCARBOXYLATE TRANSPORTER; FUNCTIONAL-CHARACTERIZATION; SUBSTRATE SELECTIVITY; TRYPTOPHAN TRANSPORT; PEPTIDE TRANSPORTER; MOLECULAR-BIOLOGY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Kanai, Y Kyorin Univ, Sch Med, Dept Pharmacol & Toxicol, 6-20-2 Shinkawa, Mitaka, Tokyo 1818611, Japan Kyorin Univ 6-20-2 Shinkawa Mitaka Tokyo Japan1818611 611, Japan
Citazione:
D.K. Kim et al., "Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters", J BIOL CHEM, 276(20), 2001, pp. 17221-17228

Abstract

A cDNA was isolated from rat small intestine by expression cloning which encodes a novel Na+-independent transporter for aromatic amino acids. When expressed in Xenopus oocytes, the encoded protein designated as TAT1 (T-typeamino acid transporter I) exhibited Na+-independent and low-affinity transport of aromatic amino acids such as tryptophan, tyrosine, and phenylalanine (K-m values: similar to5 mM), consistent with the properties of classicalamino acid transport system T, TATI accepted some variations of aromatic side chains because it interacted with amino acid-related compounds such as L-DOPA and 3-O-methyl-DOPA. Because TAT1 accepted N-methyl- and N-acetyl-derivatives of aromatic amino acids but did not accept their methylesters, itis proposed that TAT1 recognizes amino acid substrates as anions, Consistent with this, TAT1 exhibited sequence similarity (similar to 30% identity at the amino acid level) to H+/monocarboxylate transporters. Distinct from H/monocarboxylate transporters, however, TAT1 was not coupled with the H+ transport but it mediated an electroneutral facilitated diffusion. TATI mRNAwas strongly expressed in intestine, placenta, and liver. In rat small intestine TAT1 immunoreactivity was detected in the basolateral membrane of the epithelial cells suggesting its role in the transepithelial transport of aromatic amino acids. The identification of the amino acid transporter withdistinct structural and functional characteristics will not only facilitate the expansion of amino acid transporter families but also provide new insights into the mechanisms of substrate recognition of organic solute transporters.

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Documento generato il 08/04/20 alle ore 12:03:24