Unified modeling of the mammalian and fish proton-dependent oligopeptide transporter PepT1

Renna, Maria Daniela; Sangaletti, Rachele; Bossi, Elena; Cherubino, Francesca; Kottra, Gábor; Peres, Antonio

doi:10.4161/chan.5.1.13505

Cited by 15 publications

(39 citation statements)

References 32 publications

(87 reference statements)

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“…1 is close to saturation. The values of K 0.5 are U-shaped, as already reported [21,22]. Interestingly, a shift of this curve toward more negative potential is observed at the higher temperature.…”

Section: Affinity Changes With Temperaturesupporting

confidence: 65%

“…3a), the combination of these two effects produces recordings that resemble those that can be obtained in the seabass or zebrafish isoforms of PepT1 at lower temperatures ( Fig. 3b and [21,23]). …”

Section: Presteady-state Currentsmentioning

confidence: 73%

“…As mentioned above, this kind of effect was previously reported in other ion-coupled cotransporters [2] and reflects the acceleration in the rate constants of the intramembrane charge movement that underlies these currents. At pH 7.5, the acceleration of the decline rate induced by temperature adds up to that caused by the alkaline pH itself [3,21]. This combined effect makes it difficult to perform a reliable analysis of the presteady-state currents in these conditions, and for this reason, we have limited this part of our study to pH 6.5.…”

Section: Presteady-state Currentsmentioning

confidence: 94%

“…Presteady-state currents were isolated using the subtraction method as previously explained [3,21], i.e., by subtracting the records in the presence of a saturating amount of substrate (3 mM) from the corresponding ones in its absence. The amount of displaced charge (Q in ) was obtained by integration of the isolated transients, while the decline time constant (τ) was derived by single exponential fitting of the traces.…”

Section: Electrophysiology and Data Analysismentioning

confidence: 99%

“…Oocytes and RNAs were prepared as previously described in detail [21]. Briefly, to prepare the mRNA, the cDNA encoding the PepT1 transporters was cloned into the pSPORT-1 vector [18] and linearized with NotI for rbPepT1, and with HindIII for sbPepT1.…”

Section: Oocyte Expressionmentioning

confidence: 99%

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Temperature effects on the kinetic properties of the rabbit intestinal oligopeptide cotransporter PepT1

Bossi

Cherubino

Margheritis

et al. 2012

Pflugers Arch - Eur J Physiol

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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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Section: Affinity Changes With Temperaturesupporting

confidence: 65%

Section: Presteady-state Currentsmentioning

confidence: 73%

Section: Presteady-state Currentsmentioning

confidence: 94%

Section: Electrophysiology and Data Analysismentioning

confidence: 99%

Section: Oocyte Expressionmentioning

confidence: 99%

See 3 more Smart Citations

Temperature effects on the kinetic properties of the rabbit intestinal oligopeptide cotransporter PepT1

Bossi

Cherubino

Margheritis

et al. 2012

Pflugers Arch - Eur J Physiol

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Di- and tripeptide transport in vertebrates: the contribution of teleost fish models

et al. 2016

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Solute Carrier 15 (SLC15) family, alias H-coupled oligopeptide cotransporter family, is a group of membrane transporters known for their role in the cellular uptake of di- and tripeptides (di/tripeptides) and peptide-like molecules. Of its members, SLC15A1 (PEPT1) chiefly mediates intestinal absorption of luminal di/tripeptides from dietary protein digestion, while SLC15A2 (PEPT2) mainly allows renal tubular reabsorption of di/tripeptides from ultrafiltration, SLC15A3 (PHT2) and SLC15A4 (PHT1) possibly interact with di/tripeptides and histidine in certain immune cells, and SLC15A5 has unknown function. Our understanding of this family in vertebrates has steadily increased, also due to the surge of genomic-to-functional information from 'non-conventional' animal models, livestock, poultry, and aquaculture fish species. Here, we review the literature on the SLC15 transporters in teleost fish with emphasis on SLC15A1 (PEPT1), one of the solute carriers better studied amongst teleost fish because of its relevance in animal nutrition. We report on the operativity of the transporter, the molecular diversity, and multiplicity of structural-functional solutions of the teleost fish orthologs with respect to higher vertebrates, its relevance at the intersection of the alimentary and osmoregulative functions of the gut, its response under various physiological states and dietary solicitations, and its possible involvement in examples of total body plasticity, such as growth and compensatory growth. By a comparative approach, we also review the few studies in teleost fish on SLC15A2 (PEPT2), SLC15A4 (PHT1), and SLC15A3 (PHT2). By representing the contribution of teleost fish to the knowledge of the physiology of di/tripeptide transport and transporters, we aim to fill the gap between higher and lower vertebrates.

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Amino acid transporter B0AT1 (slc6a19) and ancillary protein: impact on function

Margheritis

Imperiali

Cinquetti

et al. 2016

Pflugers Arch - Eur J Physiol

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Amino acids play an important role in the metabolism of all organisms. Their epithelial re-absorption is due to specific transport proteins, such as B(0)AT1, a Na(+)-coupled neutral amino acid symporter belonging to the solute carrier 6 family. Here, a recently cloned fish orthologue, from the intestine of Salmo salar, was electrophysiologically characterized with the two-electrode voltage clamp technique, in Xenopus laevis oocytes heterologously expressing the transporter. Substrate specificity, apparent affinities and the ionic dependence of the transport mechanism were determined in the presence of specific collectrin. Results demonstrated that like the human, but differently from sea bass (Dicentrarchus labrax) orthologue, salmon B(0)AT1 needs to be associated with partner proteins to be correctly expressed at the oocyte plasma membrane. Cloning of sea bass collectrin and comparison of membrane expression and functionality of the B(0)AT1 orthologue transporters allowed a deeper investigation on the role of their interactions. The parameters acquired by electrophysiological and immunolocalization experiments in the mammalian and fish transporters contributed to highlight the dynamic of relations and impacts on transport function of the ancillary proteins. The comparative characterization of the physiological parameters of amino acid transporters with auxiliary proteins can help the comprehension of the regulatory mechanism of essential nutrient absorption.

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Unified modeling of the mammalian and fish proton-dependent oligopeptide transporter PepT1

Cited by 15 publications

References 32 publications

Temperature effects on the kinetic properties of the rabbit intestinal oligopeptide cotransporter PepT1

Temperature effects on the kinetic properties of the rabbit intestinal oligopeptide cotransporter PepT1

Di- and tripeptide transport in vertebrates: the contribution of teleost fish models

Amino acid transporter B0AT1 (slc6a19) and ancillary protein: impact on function

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