Characterization of a novel variant of amino acid transport system asc in erythrocytes from Przewalski’s horse (Equus przewalskii).
Abstract: In thoroughbred horses, red blood cell amino acid transport activity is Na(+)-independent and controlled by three codominant genetic alleles (h, l, s), coding for high-affinity system asc1 (L-alanine apparent Km for influx at 37 degrees C congruent to 0.35 mM), low-affinity system asc2 (L-alanine Km congruent to 14 mM), and transport deficiency, respectively. The present study investigated amino acid transport mechanisms in red cells from four wild species: Przewalski's horse (Equus przewalskii), Hartmann's zebra (Zebra hartmannae), Grevy's zebra (Zebra grevyi), and onager (Equus hemonius). Red blood cell samples from different Przewalski's horses exhibited uniformly high rates of L-alanine uptake, mediated by a high-affinity asc1-type transport system. Mean apparent Km and Vmax values (+/- SE) for L-alanine influx at 37 degrees C in red cells from 10 individual animals were 0.373 +/- 0.068 mM and 2.27 +/- 0.11 mmol (L cells.h), respectively. As in thoroughbreds, the Przewalski's horse transporter interacted with dibasic as well as neutral amino acids. However, the Przewalski asc1 isoform transported L-lysine with a substantially (6.4-fold) higher apparent affinity than its thoroughbred counterpart (Km for influx 1.4 mM at 37 degrees C) and was also less prone to trans-stimulation effects. The novel high apparent affinity of the Przewalski's horse transporter for L-lysine provides additional key evidence of functional and possible structural similarities between asc and the classical Na(+)-dependent system ASC and between these systems and the Na(+)-independent dibasic amino acid transport system y+. Unlike Przewalski's horse, zebra red cells were polymorphic with respect to L-alanine transport activity, showing high-affinity or low-affinity saturable mechanisms of L-alanine uptake. Onager red cells transported this amino acid with intermediate affinity (apparent Km for influx 3.0 mM at 37 degrees C). Radiation inactivation analysis was used to estimate the target size of system asc in red cells from Przewalski's horse. The transporter's in situ apparent molecular weight was 158,000 +/- 2500 (SE).
Publication Date: 1992-08-01 PubMed ID: 1473044DOI: 10.1139/y92-155Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study explores the amino acid transport system, specifically the asc1-type transport system, in the red blood cells of several species of wild horses and zebras. The researchers discovered a new variant with a high affinity for the amino acid L-lysine in Przewalski’s horse. Unlike zebras, Przewalski’s horse red blood cells showed consistently high rates of L-alanine uptake, suggesting unique differences in the transport mechanisms across different species.
Key Findings
- The research focused on the asc1-type transport system, responsible for transporting amino acids into cells, in the red blood cells of different wild horse species: Przewalski’s horse, Hartmann’s zebra, Grevy’s zebra, and onager.
- In particular, the Przewalski’s horse showed uniformly high rates of an amino acid called L-alanine uptake, mediated by the asc1-type transport system, which means it was efficient in transporting L-alanine to the blood cells.
- Notably, the Przewalski’s horse asc1 isoform showed a significantly higher affinity (6.4 times more) for another amino acid, L-lysine, than its thoroughbred counterpart. This high affinity for L-lysine demonstrates functional and possibly structural similarities between asc and the classical Na(+)-dependent system ASC, and the Na(+)-independent dibasic amino acid transport system y+.
- However, the rate of L-alanine uptake in the red blood cells of the zebra species showed variety, indicating differences in their transport mechanisms compared to the Przewalski’s horse.
Methodology
- The study involved an examination of the L-alanine amino acid uptake in red blood cells from 10 individual Przewalski’s horses. The uptake rate was measured at 37 degrees Celsius, a standard body temperature for mammals.
- They then performed similar tests on different species of wild zebras and onagers, at the same temperature, for comparison.
- Using radiation inactivation analysis, they estimated the target size of the asc transporter in Przewalski’s horse red blood cells, obtaining an in situ apparent molecular weight of 158,000 +/- 2500 (SE).
Implications
- The high apparent affinity exhibited by the Przewalski’s horse for the transport of L-lysine is a key discovery as it suggests a unique variant of the asc1-type transport system that could be structurally and functionally similar to other established transport systems.
- This finding could potentially bring about a greater understanding of the sophisticated control of amino acid transport in different species, and how such mechanisms have evolved and diversified in different equine populations to facilitate their particular needs or environments.
Cite This Article
APA
Fincham DA, Ellory JC, Young JD.
(1992).
Characterization of a novel variant of amino acid transport system asc in erythrocytes from Przewalski’s horse (Equus przewalskii).
Can J Physiol Pharmacol, 70(8), 1117-1127.
https://doi.org/10.1139/y92-155 Publication
Researcher Affiliations
- School of Applied Sciences, Wolverhampton Polytechnic, United Kingdom.
MeSH Terms
- Alanine / blood
- Alanine / pharmacokinetics
- Amino Acids / blood
- Amino Acids / pharmacology
- Animals
- Biological Transport, Active
- Erythrocytes / metabolism
- Female
- Glucosephosphate Dehydrogenase / blood
- Horses / blood
- Kinetics
- Lysine / blood
- Lysine / pharmacokinetics
- Male
- Molecular Weight
- Perissodactyla / metabolism
- Sodium / pharmacokinetics
- Sodium / physiology
Citations
This article has been cited 2 times.- Stevens BR, Ellory JC, Preston RL. B(0)AT1 Amino Acid Transporter Complexed With SARS-CoV-2 Receptor ACE2 Forms a Heterodimer Functional Unit: In Situ Conformation Using Radiation Inactivation Analysis.. Function (Oxf) 2021;2(4):zqab027.
- 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.
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