ArticlePflugers Archiv : European journal of physiology2012
Temperature effects on the kinetic properties of the rabbit intestinal oligopeptide cotransporter PepT1.
Article in Pflugers Archiv : European journal of physiology, 2012. 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, 14 citations in OpenAlex.
- Temperature regulated nutrient sensing and metabolism of amino acids in juvenile turbot (Marine life science & technology · 2025Article
- Molecular Fingerprint of Cold Adaptation in Antarctic Icefish PepT1 (Biomolecules · 2025Article
- The "www" ofMembranes · 2022Review
- Functional characterization of Atlantic salmon (Salmo salar L.) PepT2 transporters.The Journal of physiology · 2022Article
- The peptide transporter 1a of the zebrafishGenes & nutrition · 2019Article
- Di- and tripeptide transport in vertebrates: the contribution of teleost fish models.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017Review
- Amino acid transporter B(0)AT1 (slc6a19) and ancillary protein: impact on function.Pflugers Archiv : European journal of physiology · 2016Article
- Teleost fish models in membrane transport research: the PEPT1(SLC15A1) H+-oligopeptide transporter as a case study.The Journal of physiology · 2014Review
- Conferring electrogenicity to the electroneutral phosphate cotransporter NaPi-IIc (SLC34A3) reveals an internal cation release step.Pflugers Archiv : European journal of physiology · 2013Article
- An inverse relationship links temperature and substrate apparent affinity in the ion-coupled cotransporters rGAT1 and KAAT1.International journal of molecular sciences · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The effects of temperature on the functional properties of the intestinal oligopeptide transporter PepT1 from rabbit have been investigated using electrophysiological methods. The dipeptide Gly-Gln at pH 6.5 or 7.5 was used as substrate. Raising the temperature in the range 20-30 °C causes an increase in the maximal transport-associated current (I (max)) with a Q (10) close to 4. Higher temperatures accelerate the rate of decline of the presteady-state currents observed in the absence of organic substrate. The voltage dependencies of the intramembrane charge movement and of the time constant of decline are both shifted towards more negative potentials by higher temperatures. The shift is due to a stronger action of temperature on the outward rate of charge movement compared to the inward rate, indicating a lower activation energy for the latter process. Consistently, the activation energy for the complete cycle is similar to that of the inward rate of charge movement. Temperature also affects the binding rate of the substrate: the K (0.5) -V curve is shifted to more negative potentials by higher temperatures, resulting in a lower apparent affinity in the physiological range of potentials. The overall efficiency of transport, estimated as the I (max)/K (0.5) ratio is significantly increased at body temperature.
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