SLC15A2 Membrane Protein Introduction

Introduction of SLC15A2

SLC15A2 is also known as Solute carrier family 15 member 2, Kidney H⁺/peptide cotransporter, Oligopeptide transporter, kidney isoform, Peptide transporter 2, and PepT2. It belongs to the more widely distributed proton-dependent oligopeptide transporter, or POT family, which are evolutionarily well conserved from bacteria to human beings. Structurally, SLC15A2 contains 12 transmembrane (TM)-spanning α helices arranged into two TM bundles of six that fold to resemble a V-shaped protein that resides within the inner membrane of bacteria and plasma membrane of eukaryotes.

Function of SLC15A2 Membrane Protein

In mammals, the plasma membrane transporters SLC15A2 mediate the uptake and retention of dietary peptides. SLC15A2 belongs to the proton-coupled symporters, recognizing di- and tri-peptides on the outside of the cell and utilizing the energy stored in the inwardly directed proton electrochemical gradient to drive their uptake into the cell. SLC15A2 also recognizes and transport a number of important drug families, including β-lactam antibiotics and anti-cancer agents and are important targets in the ongoing attempts of the pharmaceutical industry to improve the pharmacokinetic properties of drug molecules. In vitro binding assays demonstrate that the extracellular domains of SLC15A2 interact with the intestinal protease trypsin, potentially answering an interesting observation made in the late 1960s of a specific and tight interaction of trypsin with human intestinal mucosa. The function of the extracellular domains of SLC15A2 is to recruit trypsin to the site of the peptide transport on the plasma membrane. The interaction between the extracellular domains of PepT2 and trypsin plays an important physiological role in absorbing small peptides arising from digestion of dietary proteins in the small intestine.

Fig.1 A Model for the Interaction between Trypsin and PepT2 (SLC15A2). (Beale, 2015)

Application of SLC15A2 Membrane Protein in Literature

1. Beale J.H., et al. Crystal Structures of the Extracellular Domain from PepT1 and PepT2 Provide Novel Insights into Mammalian Peptide Transport. Structure(London, England:1993). 2015, 23(10):1889-1899. PubMed ID: 26320580
   
   

   This article reports that the crystal structure of PepT1 (SLC15A1) and PepT2 (SLC15A2). The functional and biophysical studies of this article demonstrate that the extracellular domains of PepT1 (SLC15A1) and PepT2 (SLC15A2) interact with the intestinal protease trypsin, suggesting a role in clustering proteolytic activity to the site of peptide transport in eukaryotic cells.

2. Smith D.E., et al. Proton-coupled oligopeptide transporter family SLC15: Physiological, pharmacological and pathological implications. Molecular aspects of medicine. 2013, 34(2-3):323-336. PubMed ID: 23506874
   
   

   This article provides updated information on the structure-function of PepT1 (SLC15A1), PepT2 (SLC15A2), PhT1 (SLC15A4) and PhT2 (SLC15A3), and their expression and localization in key tissues.

3. Takano M., et al. Expression and function of PEPT2 during transdifferentiation of alveolar epithelial cells. Life Sci. 2013, 93(17):630-636. PubMed ID: 23988852
   
   

   This article clarifies the expression and function of peptide transporter 2 (PEPT2) in primary cultured alveolar type II epithelial cells and the expression decreases along with trans differentiation, the expression is almost completely lost in type I cells.

4. Chen X., et al. Influence of Peptide Transporter 2 (PEPT2) on the Distribution of Cefadroxil in Mouse Brain: A Microdialysis Study. Biochem. Pharmacol. 2017,131:89-97. PubMed ID: 28192085
   
   

   The results of this article suggested that PEPT2 plays an important role in modulating the physiological, pharmacological and toxicological activities of CNS-relevant endogenous substrates and drugs.

5. Alghamdi O.A., et al. A new use of β-Ala-Lys (AMCA) as a transport reporter for PEPT1 and PEPT2 in renal brush border membrane vesicles from the outer cortex and outer medulla. Biochim. Biophys. Acta. 2018, 1860(5):960-964. PubMed ID: 29291378
   
   

   This article demonstrates that β-Ala-Lys (AMCA) can be used as a biosensor to measure the transport activity of the renal-type PEPT1 and PEPT2 in BBMV-OC and BMMV-OM respectively.

SLC15A2 Preparation Options

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Reference

1. Beale J H., et al. (2015) Crystal Structures of the Extracellular Domain from PepT1 and PepT2 Provide Novel Insights into Mammalian Peptide Transport. Structure(London, England:1993. 23(10):1889-1899.

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