Characterization of a novel Na+-independent amino acid transporter in horse erythrocytes.
Abstract: Horse erythrocytes are polymorphic with respect to L-alanine permeability. The present investigation compared the specificity, kinetics and cation-dependence of erythrocyte amino acid transport in two groups of thoroughbred horses, those with erythrocyte L-alanine permeabilities in the range 5-15 mumol/h per litre of cells (0.2 mM extracellular L-alanine, 37 degrees C) (transport-negative type) and those with L-alanine permeabilities in the range 450-700 mumol/h per litre of cells (transport-positive type). Transport-positive cells are shown to possess a novel high-affinity, stereospecific, Na+-independent transporter selective for neutral amino acids of intermediate size. This carrier system (provisional designation asc) operates preferentially in an exchange mode and is functionally absent from erythrocytes of transport-negative-type horses.
Publication Date: 1985-04-01 PubMed ID: 3994678PubMed Central: PMC1144803DOI: 10.1042/bj2270013Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study explores a new type of amino acid transporter found in horse red blood cells, which operates independently of sodium and is particularly active in horses presenting high permeability for L-alanine.
Objective of the Study
- The focus of the research was to investigate the variation in amino acid transport, specifically L-alanine, in the red blood cells of thoroughbred horses. The researchers divided the horses into two groups based on their erythrocyte (red blood cell) L-alanine permeabilities.
Types of Horses in the Study
- The first group had L-alanine permeabilities ranging from 5-15 micromoles per hour per litre of cells, labeled as the “transport-negative type”.
- The second group had L-alanine permeabilities ranging 450-700 micromoles per hour per litre of cells, described as the “transport-positive type”.
Discovery of the Novel Transporter
- The study discovered a previously unidentified high-affinity amino acid transporter in the erythrocytes of the transport-positive type horses.
- This transporter, labeled as the asc system, is selective for neutral amino acids of intermediate size.
- The transporter operates in an exchange mode, meaning it carries one substance into the cell as it transports another substance out.
- Importantly, this transporter operates independently of sodium. This aspect contrasts with many other types of cellular transporters, which require the presence of ions like sodium to function.
- The asc system was found to be absent from the red blood cells of the transport-negative type horses.
Implications of Study
- Understanding these differences in amino acid transporters could have significant implications for equine health and disease management. For instance, if this transporter’s activity is linked to certain diseases, identifying its presence could help diagnose or manage these conditions.
- The study’s findings also provide further context about biological variations in not just horses, but potentially other species as well. The discovery of the asc system brings new insights regarding the diversity of cellular transportation mechanisms.
Cite This Article
APA
Fincham DA, Mason DK, Young JD.
(1985).
Characterization of a novel Na+-independent amino acid transporter in horse erythrocytes.
Biochem J, 227(1), 13-20.
https://doi.org/10.1042/bj2270013 Publication
Researcher Affiliations
MeSH Terms
- Alanine / metabolism
- Amino Acids / blood
- Animals
- Biological Transport / drug effects
- Cations, Monovalent / pharmacology
- Cysteine / pharmacology
- Erythrocytes / drug effects
- Erythrocytes / metabolism
- Horses
- Sodium / pharmacology
- Substrate Specificity
References
This article includes 20 references
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Citations
This article has been cited 9 times.- Soriano-García JF, Torras-Llort M, Ferrer R, Moreto M. Multiple pathways for L-methionine transport in brush-border membrane vesicles from chicken jejunum. J Physiol 1998 Jun 1;509 ( Pt 2)(Pt 2):527-39.
- Peter GJ, Davidson IG, Ahmed A, McIlroy L, Forrester AR, Taylor PM. Multiple components of arginine and phenylalanine transport induced in neutral and basic amino acid transporter-cRNA-injected Xenopus oocytes. Biochem J 1996 Sep 15;318 ( Pt 3)(Pt 3):915-22.
- Gallardo MA, Sánchez J. Glycine uptake by trout (Salmo trutta) red blood cells. J Membr Biol 1993 Jun;134(3):251-9.
- Albi JL, Canals P, Gallardo MA, Sánchez J. Na(+)-independent L-alanine uptake by trout cells. Evidence for the existence of at least two functionally different acs systems. J Membr Biol 1994 Jun;140(3):189-96.
- Christensen HN. On the strategy of kinetic discrimination of amino acid transport systems. J Membr Biol 1985;84(2):97-103.
- Fincham DA, Mason DK, Paterson JY, Young JD. Heterogeneity of amino acid transport in horse erythrocytes: a detailed kinetic analysis of inherited transport variation. J Physiol 1987 Aug;389:385-409.
- Norman PS, Mann GE. Ionic dependence of amino-acid transport in the exocrine pancreatic epithelium: calcium dependence of insulin action. J Membr Biol 1987;96(2):153-63.
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- Mann GE, Norman PS, Smith IC. Amino acid efflux in the isolated perfused rat pancreas: trans-stimulation by extracellular amino acids. J Physiol 1989 Sep;416:485-502.
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