SLC15A1 is also known as solute carrier family 15 member 1, intestinal H⁺/peptide cotransporter, oligopeptide transporter, small intestine isoform, peptide transporter 1 (PepT1), plasma membrane transporters. It belongs to the peptide transporter (PTR) family and serves as integral membrane proteins for the cellular uptake of di- and tripeptides 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. Structurally, SLC15A1 contains 12 transmembranes (TM)-spanning helices.
|Basic Information of SLC15A1|
|Protein Name||Solute carrier family 15 member 1|
|Aliases||Intestinal H⁺/peptide cotransporter, Peptide transporter 1 (PepT1), Oligopeptide transporter, small intestine isoform, Olasma membrane transporters|
|Organism||Homo sapiens (Human)|
SLC15A1 is a member of the more widely distributed proton-dependent oligopeptide transporter, or POT, family, which are evolutionarily well conserved from bacteria to man. Mammalian peptide transport is a physiologically important route to both assimilate dietary nitrogen in the form of small di- and tri-peptides from ingested protein and retain peptides in the body by selective reabsorption in the kidneys. SLC15A1 mediates the uptake and retention of dietary peptides in mammals. SLC15A1 also recognizes and transports a number of important drug families, including β-lactam antibiotics and anti-cancer agents. SLC15A1 is an important target in the ongoing attempts of the pharmaceutical industry to improve the pharmacokinetic properties of drug molecules. SLC15A1 has the ability to transport peptidomimetics and other substrates with therapeutic activities or precursors of pharmacologically active agents, they are of considerable importance in pharmacology. SLC15A1 also plays an important physiological role in absorbing small peptides arising from digestion of dietary proteins in the small intestine, as well as in reabsorbing filtered peptides generated from luminal peptidases in the kidney.
Fig.1 Crystal structure of the extracellular domains of SLC15A1. (Beale, 2015)
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.
This article reviews the structural characteristics of the peptide transporters PepT1 (SLC15A1) and PepT2 (SLC15A2), the structural requirements for substrates, the distribution of the peptide transporters in the organism, and finally their regulation in the organism in healthy and pathological situations.
This article focuses on the pharmaceutical relevance of the intestinal peptide transporter PepT1(SLC15A1). The concept that PepT1 (SLC15A1) serves as a drug transporter has been further substantiated and significant progress has been made on drugs such as cefadroxil and valacyclovir.
This article reports the development and characterization of mice humanized for PEPT1 (SLC15A1) for the first time. This novel transgenic huPEPT1 mouse model should prove useful in examining the role, relevance, and regulation of PEPT1 in diet and disease, and in the drug discovery process.
This article summarizes the progress made in the regulation of PepT1 (SLC15A1) and provides insights into the PepT1’s potential in clinical aspects of nutritional and drug therapies.
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