ArticleThe Biochemical journal1998
Discrimination of two amino acid transport activities in 4F2 heavy chain- expressing Xenopus laevis oocytes.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Consumption and Metabolism of Extracellular Pyruvate by Cultured Rat Brain Astrocytes.Neurochemical research · 2023Article
- Do Amino Acid Antiporters Have Asymmetric Substrate Specificity?Biomolecules · 2023Article
- Quantifying the relative contributions of different solute carriers to aggregate substrate transport.Scientific reports · 2017Article
- Involvement of the L-Type Amino Acid Transporter Lat2 in the Transport of 3,3'-Diiodothyronine across the Plasma Membrane.European thyroid journal · 2015Article
- Heterodimeric amino acid transporter glycoprotein domains determining functional subunit association.The Biochemical journal · 2005Article
- Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains.The Biochemical journal · 2001Article
- The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine efflux in exchange with glutamine.The Biochemical journal · 2000Article
- The heterodimeric amino acid transporter 4F2hc/LAT1 is associated in Xenopus oocytes with a non-selective cation channel that is regulated by the serine/threonine kinase sgk-1.The Journal of physiology · 2000Article
- Heterodimeric amino acid transporters: expression of heavy but not light chains of CD98 correlates with induction of amino acid transport systems in human placental trophoblast.The Journal of physiology · 2000Article
- Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family.The EMBO journal · 1999Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Expression of the type II membrane proteins of the rbAT/4F2hc family in Xenopus laevis oocytes results in the induction of amino acid transport activity. To elucidate the mechanism of action, amino acid transport was investigated in oocytes expressing the surface antigen 4F2hc. Leucine transport was mediated by a Na+-independent and a Na+-dependent transport mechanism. Both systems could be further discriminated by their stereochemical constraints. Isoleucine, with a branch at the beta-position, shared only the Na+-independent transport system with leucine. Both transport systems were sensitive to inhibition by arginine, but only the Na+-independent system was sensitive to inhibition by 2-aminobicyclo[2,2,1]heptane-2-carboxylic acid. When compared with known transport systems the two transport activities could be described as similar to, but not identical with, mammalian systems b0,+ and y+L. The Na+-independent b0,+-like transport system was found both in rbAT and 4F2hc expressing oocytes, indicating that both proteins act in a similar way.
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