Human LAT1, a subunit of system L amino acid transporter

Molecular cloning and transport function

Puttur D Prasad, Haiping Wang, Wei Huang, Ramesh Kekuda, Deva P. Rajan, Frederick H. Leibach, Vadivel Ganapathy

Research output: Contribution to journalArticle

166 Citations (Scopus)

Abstract

We report here on the cloning and functional characterization of human LAT1, a subunit of the amino acid transport system L. The hLAT1 cDNA, obtained from a human placental cDNA library, codes for a protein of 507 amino acids. When functionally expressed in mammalian cells together with the heavy chain of the rat 4F2 antigen (r4F2hc), hLAT1 induces the transport of neutral amino acids. When expressed independently, neither hLAT1 nor r4F2hc was capable of amino acid transport to any significant extent. Thus, the hLAT1-r4F2hc heterodimeric complex is responsible for the observed amino acid transport. The transport process induced by the heterodimer is Na+ independent and is not influenced by pH. It recognizes exclusively neutral amino acids with high affinity. LAT1-specific mRNA is expressed in most human tissues with the notable exception of the intestine.

Original languageEnglish (US)
Pages (from-to)283-288
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume255
Issue number2
DOIs
StatePublished - Feb 16 1999

Fingerprint

Amino Acid Transport Systems
Cloning
Molecular Cloning
Neutral Amino Acids
Amino Acids
CD98 Heavy Chain Antigens
CD98 Antigens
Amino Acid Transport System L
Gene Library
Intestines
Rats
Organism Cloning
Complementary DNA
Cells
Tissue
Messenger RNA
Proteins

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Human LAT1, a subunit of system L amino acid transporter : Molecular cloning and transport function. / Prasad, Puttur D; Wang, Haiping; Huang, Wei; Kekuda, Ramesh; Rajan, Deva P.; Leibach, Frederick H.; Ganapathy, Vadivel.

In: Biochemical and Biophysical Research Communications, Vol. 255, No. 2, 16.02.1999, p. 283-288.

Research output: Contribution to journalArticle

Prasad, Puttur D ; Wang, Haiping ; Huang, Wei ; Kekuda, Ramesh ; Rajan, Deva P. ; Leibach, Frederick H. ; Ganapathy, Vadivel. / Human LAT1, a subunit of system L amino acid transporter : Molecular cloning and transport function. In: Biochemical and Biophysical Research Communications. 1999 ; Vol. 255, No. 2. pp. 283-288.
@article{f9a8c02523374a4b8b15a684c3eed0f2,
title = "Human LAT1, a subunit of system L amino acid transporter: Molecular cloning and transport function",
abstract = "We report here on the cloning and functional characterization of human LAT1, a subunit of the amino acid transport system L. The hLAT1 cDNA, obtained from a human placental cDNA library, codes for a protein of 507 amino acids. When functionally expressed in mammalian cells together with the heavy chain of the rat 4F2 antigen (r4F2hc), hLAT1 induces the transport of neutral amino acids. When expressed independently, neither hLAT1 nor r4F2hc was capable of amino acid transport to any significant extent. Thus, the hLAT1-r4F2hc heterodimeric complex is responsible for the observed amino acid transport. The transport process induced by the heterodimer is Na+ independent and is not influenced by pH. It recognizes exclusively neutral amino acids with high affinity. LAT1-specific mRNA is expressed in most human tissues with the notable exception of the intestine.",
author = "Prasad, {Puttur D} and Haiping Wang and Wei Huang and Ramesh Kekuda and Rajan, {Deva P.} and Leibach, {Frederick H.} and Vadivel Ganapathy",
year = "1999",
month = "2",
day = "16",
doi = "10.1006/bbrc.1999.0206",
language = "English (US)",
volume = "255",
pages = "283--288",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Human LAT1, a subunit of system L amino acid transporter

T2 - Molecular cloning and transport function

AU - Prasad, Puttur D

AU - Wang, Haiping

AU - Huang, Wei

AU - Kekuda, Ramesh

AU - Rajan, Deva P.

AU - Leibach, Frederick H.

AU - Ganapathy, Vadivel

PY - 1999/2/16

Y1 - 1999/2/16

N2 - We report here on the cloning and functional characterization of human LAT1, a subunit of the amino acid transport system L. The hLAT1 cDNA, obtained from a human placental cDNA library, codes for a protein of 507 amino acids. When functionally expressed in mammalian cells together with the heavy chain of the rat 4F2 antigen (r4F2hc), hLAT1 induces the transport of neutral amino acids. When expressed independently, neither hLAT1 nor r4F2hc was capable of amino acid transport to any significant extent. Thus, the hLAT1-r4F2hc heterodimeric complex is responsible for the observed amino acid transport. The transport process induced by the heterodimer is Na+ independent and is not influenced by pH. It recognizes exclusively neutral amino acids with high affinity. LAT1-specific mRNA is expressed in most human tissues with the notable exception of the intestine.

AB - We report here on the cloning and functional characterization of human LAT1, a subunit of the amino acid transport system L. The hLAT1 cDNA, obtained from a human placental cDNA library, codes for a protein of 507 amino acids. When functionally expressed in mammalian cells together with the heavy chain of the rat 4F2 antigen (r4F2hc), hLAT1 induces the transport of neutral amino acids. When expressed independently, neither hLAT1 nor r4F2hc was capable of amino acid transport to any significant extent. Thus, the hLAT1-r4F2hc heterodimeric complex is responsible for the observed amino acid transport. The transport process induced by the heterodimer is Na+ independent and is not influenced by pH. It recognizes exclusively neutral amino acids with high affinity. LAT1-specific mRNA is expressed in most human tissues with the notable exception of the intestine.

UR - http://www.scopus.com/inward/record.url?scp=0033573892&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033573892&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1999.0206

DO - 10.1006/bbrc.1999.0206

M3 - Article

VL - 255

SP - 283

EP - 288

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -