The orphan transporter v7-3 (slc6a15) is a Na+-dependent neutral amino acid transporter (B0AT2)
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The orphan transporter v7-3 (slc6a15) is a Na+-dependent neutral amino acid transporter (B0AT2). / Bröer, Angelika; Tietze, Nadine; Kowalczuk, Sonja; Chubb, Sarah; Munzinger, Michael; Bak, Lasse K; Bröer, Stefan.
In: Biochemical Journal, Vol. 393, No. Pt 1, 01.01.2006, p. 421-30.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The orphan transporter v7-3 (slc6a15) is a Na+-dependent neutral amino acid transporter (B0AT2)
AU - Bröer, Angelika
AU - Tietze, Nadine
AU - Kowalczuk, Sonja
AU - Chubb, Sarah
AU - Munzinger, Michael
AU - Bak, Lasse K
AU - Bröer, Stefan
PY - 2006/1/1
Y1 - 2006/1/1
N2 - Transporters of the SLC6 (solute carrier 6) family play an important role in the removal of neurotransmitters in brain tissue and in amino acid transport in epithelial cells. In the present study, we demonstrate that mouse v7-3 (slc6a15) encodes a transporter for neutral amino acids. The transporter is functionally and sequence related to B(0)AT1 (slc6a19) and was hence named B(0)AT2. Leucine, isoleucine, valine, proline and methionine were recognized by the transporter, with values of K(0.5) (half-saturation constant) ranging from 40 to 200 microM. Alanine, glutamine and phenylalanine were low-affinity substrates of the transporter, with K(0.5) values in the millimolar range. Transport of neutral amino acids via B(0)AT2 was Na+-dependent, Cl--independent and electrogenic. Superfusion of mouse B(0)AT2-expressing oocytes with amino acid substrates generated robust inward currents. Na+-activation kinetics of proline transport and uptake under voltage clamp suggested a 1:1 Na+/amino acid co-transport stoichiometry. Susbtrate and co-substrate influenced each other's K(0.5) values, suggesting that they share the same binding site. A mouse B(0)AT2-like transport activity was detected in synaptosomes and cultured neurons. A potential role of B(0)AT2 in transporting neurotransmitter precursors and neuromodulators is proposed.
AB - Transporters of the SLC6 (solute carrier 6) family play an important role in the removal of neurotransmitters in brain tissue and in amino acid transport in epithelial cells. In the present study, we demonstrate that mouse v7-3 (slc6a15) encodes a transporter for neutral amino acids. The transporter is functionally and sequence related to B(0)AT1 (slc6a19) and was hence named B(0)AT2. Leucine, isoleucine, valine, proline and methionine were recognized by the transporter, with values of K(0.5) (half-saturation constant) ranging from 40 to 200 microM. Alanine, glutamine and phenylalanine were low-affinity substrates of the transporter, with K(0.5) values in the millimolar range. Transport of neutral amino acids via B(0)AT2 was Na+-dependent, Cl--independent and electrogenic. Superfusion of mouse B(0)AT2-expressing oocytes with amino acid substrates generated robust inward currents. Na+-activation kinetics of proline transport and uptake under voltage clamp suggested a 1:1 Na+/amino acid co-transport stoichiometry. Susbtrate and co-substrate influenced each other's K(0.5) values, suggesting that they share the same binding site. A mouse B(0)AT2-like transport activity was detected in synaptosomes and cultured neurons. A potential role of B(0)AT2 in transporting neurotransmitter precursors and neuromodulators is proposed.
KW - Amino Acid Sequence
KW - Amino Acid Transport Systems, Neutral
KW - Amino Acids, Neutral
KW - Animals
KW - Biological Transport
KW - Cloning, Molecular
KW - Kinetics
KW - Mice
KW - Molecular Sequence Data
KW - Neurons
KW - Proline
KW - Protein Conformation
KW - Sodium
KW - Substrate Specificity
KW - Synaptosomes
U2 - 10.1042/BJ20051273
DO - 10.1042/BJ20051273
M3 - Journal article
C2 - 16185194
VL - 393
SP - 421
EP - 430
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - Pt 1
ER -
ID: 152061131