Characterization of the high-affinity monocarboxylate transporter MCT2 in Xenopus laevis oocytes.
- S. Bröer, A. Bröer, H. Schneider, C. Stegen, A. Halestrap, J. Deitmer
- BiologyBiochemical Journal
- 1 August 1999
It is suggested that cells which express MCT2 preferentially use lactate and ketone bodies as energy sources, and could be inhibited by alpha-cyano-4-hydroxycinnamate, anion-channel inhibitors and flavonoids.
Characterization of the monocarboxylate transporter 1 expressed in Xenopus laevis oocytes by changes in cytosolic pH.
- S. Bröer, H. Schneider, A. Bröer, B. Rahman, B. Hamprecht, J. Deitmer
- BiologyBiochemical Journal
- 1 July 1998
The basic kinetic properties of lactate transport in MCT1-expressing oocytes were determined by analysing the rates of intracellular pH changes under different conditions and were in agreement with the known properties of the transporter.
The orphan transporter v7-3 (slc6a15) is a Na+-dependent neutral amino acid transporter (B0AT2).
It is demonstrated that mouse v7-3 (slc6a15) encodes a transporter for neutral amino acids and was hence named B(0)AT2, which was Na+-dependent, Cl--independent and electrogenic, and a potential role in transporting neurotransmitter precursors and neuromodulators is proposed.
Molecular Cloning of Mouse Amino Acid Transport System B0, a Neutral Amino Acid Transporter Related to Hartnup Disorder*
- A. Bröer, K. Klingel, S. Kowalczuk, J. Rasko, J. Cavanaugh, S. Bröer
- BiologyJournal of Biological Chemistry
- 4 June 2004
A novel member of the Na+-dependent neurotransmitter transporter family (B0AT1) isolated from mouse kidney shows all properties of system B0, and the human homologue of this transporter is an excellent functional and positional candidate for Hartnup disorder.
The Astroglial ASCT2 Amino Acid Transporter as a Mediator of Glutamine Efflux
It is shown here that ASCT2, a variant of transport system ASC, is strongly expressed in rat astroglia-rich primary cultures but not in neuron-richPrimary cultures, and suggest a significant role of AS CT2 in glutamine efflux from astrocytes by obligatory exchange with extracellular amino acids.
The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine efflux in exchange with glutamine.
Results indicated that arginine has the highest affinity for the intracellular binding site and that arkinine release may be the main physiological function of this transporter.
Deletion of Amino Acid Transporter ASCT2 (SLC1A5) Reveals an Essential Role for Transporters SNAT1 (SLC38A1) and SNAT2 (SLC38A2) to Sustain Glutaminolysis in Cancer Cells*
It is shown that HeLa epithelial cervical cancer cells and 143B osteosarcoma cells express a set of glutamine transporters including SNAT1, SNAT2,SNAT2 (SLC38A2), SNAT4, LAT1, and ASCT2, and a combined targeted approach would inhibit growth of glutamines-dependent cancer cells.
Neutral amino acid transporter ASCT2 displays substrate-induced Na+ exchange and a substrate-gated anion conductance.
The neutral amino acid transporter ASCT2 mediates electroneutral obligatory antiport but at the same time requires Na(+) for its function, and was expressed in Xenopus laevis oocytes and transport was analysed by flux studies and two-electrode voltage clamp recordings.
Molecular cloning of the mouse IMINO system: an Na+- and Cl--dependent proline transporter.
- S. Kowalczuk, A. Bröer, M. Munzinger, N. Tietze, K. Klingel, S. Bröer
- BiologyThe Biochemical journal
- 15 March 2005
It is demonstrated that the mouse homologue of slc6a20 has all properties of the long-sought IMINO system, and the two homologues corresponding to the single human SLC6A20 gene are named XT3 and XT3s1 to indicate the tissue expression of the two genes.
Amino acid homeostasis and signalling in mammalian cells and organisms
The CNS appears to generate a protein-specific response upon amino acid depletion, resulting in avoidance of an inadequate diet, and reduction in protein synthesis and amino acid oxidation are the only two measures to reduce amino acid demand.