Cloning and functional characterization of a new subtype of the amino acid transport system N

Takeo Nakanishi, Ramesh Kekuda, You Jun Fei, Takahiro Hatanaka, Mitsuru Sugawara, Robert G. Martindale, Frederick H. Leibach, Puttur D Prasad, Vadivel Ganapathy

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

We have cloned a new subtype of the amino acid transport system N2 (SN2 or second subtype of system N) from rat brain. Rat SN2 consists of 471 amino acids and belongs to the recently identified glutamine transporter gene family that consists of system N and system A. Rat SN2 exhibits 63% identity with rat SN1. It also shows considerable sequence identity (50-56%) with the members of the amino acid transporter A subfamily. In the rat, SN2 mRNA is most abundant in the liver but is detectable in the brain, lung, stomach, kidney, testis, and spleen. When expressed in Xenopus laevis oocytes and in mammalian cells, rat SN2 mediates Na+-dependent transport of several neutral amino acids, including glycine, asparagine, alanine, serine, glutamine, and histidine. The transport process is electrogenic, Li+ tolerant, and pH sensitive. The transport mechanism involves the influx of Na+ and amino acids coupled to the efflux of H+, resulting in intracellular alkalization. Proline, α-(methylamino)isobutyric acid, and anionic and cationic amino acids are not recognized by rat SN2.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Cell Physiology
Volume281
Issue number6 50-6
StatePublished - Dec 1 2001

Fingerprint

Amino Acid Transport Systems
Organism Cloning
Glutamine
Amino Acids
Amino Acid Transport System A
Neutral Amino Acids
Asparagine
Xenopus laevis
Brain
Histidine
Proline
Alanine
Glycine
Serine
Oocytes
Testis
Stomach
Spleen
Kidney
Lung

Keywords

  • Electrogenicity
  • Glutamine transporter family
  • Proton transport
  • System N2

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Nakanishi, T., Kekuda, R., Fei, Y. J., Hatanaka, T., Sugawara, M., Martindale, R. G., ... Ganapathy, V. (2001). Cloning and functional characterization of a new subtype of the amino acid transport system N. American Journal of Physiology - Cell Physiology, 281(6 50-6).

Cloning and functional characterization of a new subtype of the amino acid transport system N. / Nakanishi, Takeo; Kekuda, Ramesh; Fei, You Jun; Hatanaka, Takahiro; Sugawara, Mitsuru; Martindale, Robert G.; Leibach, Frederick H.; Prasad, Puttur D; Ganapathy, Vadivel.

In: American Journal of Physiology - Cell Physiology, Vol. 281, No. 6 50-6, 01.12.2001.

Research output: Contribution to journalArticle

Nakanishi, T, Kekuda, R, Fei, YJ, Hatanaka, T, Sugawara, M, Martindale, RG, Leibach, FH, Prasad, PD & Ganapathy, V 2001, 'Cloning and functional characterization of a new subtype of the amino acid transport system N', American Journal of Physiology - Cell Physiology, vol. 281, no. 6 50-6.
Nakanishi T, Kekuda R, Fei YJ, Hatanaka T, Sugawara M, Martindale RG et al. Cloning and functional characterization of a new subtype of the amino acid transport system N. American Journal of Physiology - Cell Physiology. 2001 Dec 1;281(6 50-6).
Nakanishi, Takeo ; Kekuda, Ramesh ; Fei, You Jun ; Hatanaka, Takahiro ; Sugawara, Mitsuru ; Martindale, Robert G. ; Leibach, Frederick H. ; Prasad, Puttur D ; Ganapathy, Vadivel. / Cloning and functional characterization of a new subtype of the amino acid transport system N. In: American Journal of Physiology - Cell Physiology. 2001 ; Vol. 281, No. 6 50-6.
@article{6070e245428a453883da28aca2e5207b,
title = "Cloning and functional characterization of a new subtype of the amino acid transport system N",
abstract = "We have cloned a new subtype of the amino acid transport system N2 (SN2 or second subtype of system N) from rat brain. Rat SN2 consists of 471 amino acids and belongs to the recently identified glutamine transporter gene family that consists of system N and system A. Rat SN2 exhibits 63{\%} identity with rat SN1. It also shows considerable sequence identity (50-56{\%}) with the members of the amino acid transporter A subfamily. In the rat, SN2 mRNA is most abundant in the liver but is detectable in the brain, lung, stomach, kidney, testis, and spleen. When expressed in Xenopus laevis oocytes and in mammalian cells, rat SN2 mediates Na+-dependent transport of several neutral amino acids, including glycine, asparagine, alanine, serine, glutamine, and histidine. The transport process is electrogenic, Li+ tolerant, and pH sensitive. The transport mechanism involves the influx of Na+ and amino acids coupled to the efflux of H+, resulting in intracellular alkalization. Proline, α-(methylamino)isobutyric acid, and anionic and cationic amino acids are not recognized by rat SN2.",
keywords = "Electrogenicity, Glutamine transporter family, Proton transport, System N2",
author = "Takeo Nakanishi and Ramesh Kekuda and Fei, {You Jun} and Takahiro Hatanaka and Mitsuru Sugawara and Martindale, {Robert G.} and Leibach, {Frederick H.} and Prasad, {Puttur D} and Vadivel Ganapathy",
year = "2001",
month = "12",
day = "1",
language = "English (US)",
volume = "281",
journal = "American Journal of Physiology - Heart and Circulatory Physiology",
issn = "0363-6135",
publisher = "American Physiological Society",
number = "6 50-6",

}

TY - JOUR

T1 - Cloning and functional characterization of a new subtype of the amino acid transport system N

AU - Nakanishi, Takeo

AU - Kekuda, Ramesh

AU - Fei, You Jun

AU - Hatanaka, Takahiro

AU - Sugawara, Mitsuru

AU - Martindale, Robert G.

AU - Leibach, Frederick H.

AU - Prasad, Puttur D

AU - Ganapathy, Vadivel

PY - 2001/12/1

Y1 - 2001/12/1

N2 - We have cloned a new subtype of the amino acid transport system N2 (SN2 or second subtype of system N) from rat brain. Rat SN2 consists of 471 amino acids and belongs to the recently identified glutamine transporter gene family that consists of system N and system A. Rat SN2 exhibits 63% identity with rat SN1. It also shows considerable sequence identity (50-56%) with the members of the amino acid transporter A subfamily. In the rat, SN2 mRNA is most abundant in the liver but is detectable in the brain, lung, stomach, kidney, testis, and spleen. When expressed in Xenopus laevis oocytes and in mammalian cells, rat SN2 mediates Na+-dependent transport of several neutral amino acids, including glycine, asparagine, alanine, serine, glutamine, and histidine. The transport process is electrogenic, Li+ tolerant, and pH sensitive. The transport mechanism involves the influx of Na+ and amino acids coupled to the efflux of H+, resulting in intracellular alkalization. Proline, α-(methylamino)isobutyric acid, and anionic and cationic amino acids are not recognized by rat SN2.

AB - We have cloned a new subtype of the amino acid transport system N2 (SN2 or second subtype of system N) from rat brain. Rat SN2 consists of 471 amino acids and belongs to the recently identified glutamine transporter gene family that consists of system N and system A. Rat SN2 exhibits 63% identity with rat SN1. It also shows considerable sequence identity (50-56%) with the members of the amino acid transporter A subfamily. In the rat, SN2 mRNA is most abundant in the liver but is detectable in the brain, lung, stomach, kidney, testis, and spleen. When expressed in Xenopus laevis oocytes and in mammalian cells, rat SN2 mediates Na+-dependent transport of several neutral amino acids, including glycine, asparagine, alanine, serine, glutamine, and histidine. The transport process is electrogenic, Li+ tolerant, and pH sensitive. The transport mechanism involves the influx of Na+ and amino acids coupled to the efflux of H+, resulting in intracellular alkalization. Proline, α-(methylamino)isobutyric acid, and anionic and cationic amino acids are not recognized by rat SN2.

KW - Electrogenicity

KW - Glutamine transporter family

KW - Proton transport

KW - System N2

UR - http://www.scopus.com/inward/record.url?scp=0035664859&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035664859&partnerID=8YFLogxK

M3 - Article

C2 - 11698233

AN - SCOPUS:0035664859

VL - 281

JO - American Journal of Physiology - Heart and Circulatory Physiology

JF - American Journal of Physiology - Heart and Circulatory Physiology

SN - 0363-6135

IS - 6 50-6

ER -