Biology:Peptide transporter 1
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Short description: Mammalian protein found in Homo sapiens
 Generic protein structure example |
Peptide transporter 1 (PepT 1) also known as solute carrier family 15 member 1 (SLC15A1) is a protein that in humans is encoded by SLC15A1 gene.[1][2] PepT 1 is a solute carrier for oligopeptides. It functions in renal oligopeptide reabsorption and in the intestines in a proton dependent way, hence acting like a cotransporter.[3]
Function
SLC15A1is localized to the brush border membrane of the intestinal epithelium and mediates the uptake of di- and tripeptides from the lumen into the enterocytes. This protein plays an important role in the uptake and digestion of dietary proteins. This protein also facilitates the absorption of numerous peptidomimetic drugs.[1][3] Peptide transporter 1 functions in nutrient and drug transport have been studied using intestinal organoids.[4][5]
See also
References
- ↑ 1.0 1.1 "Entrez Gene: SLC15A1 Solute carrier family 15 (oligopeptide transporter), member 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6564.
- ↑ "Human intestinal H+/peptide cotransporter. Cloning, functional expression, and chromosomal localization". J. Biol. Chem. 270 (12): 6456–63. March 1995. doi:10.1074/jbc.270.12.6456. PMID 7896779.
- ↑ 3.0 3.1 "The oligopeptide transporter (Pept-1) in human intestine: biology and function". Gastroenterology 113 (1): 332–40. July 1997. doi:10.1016/S0016-5085(97)70112-4. PMID 9207295.
- ↑ "Intestinal organoids for assessing nutrient transport, sensing and incretin secretion". Scientific Reports 5 (1): 16831. November 2015. doi:10.1038/srep16831. PMID 26582215.
- ↑ "Organoids to Study Intestinal Nutrient Transport, Drug Uptake and Metabolism – Update to the Human Model and Expansion of Applications". Frontiers in Bioengineering and Biotechnology 8: 577656. 2020. doi:10.3389/fbioe.2020.577656. PMID 33015026.
Further reading
- "Regulation of expression of the intestinal oligopeptide transporter (Pept-1) in health and disease". Am. J. Physiol. Gastrointest. Liver Physiol. 285 (5): G779–88. 2003. doi:10.1152/ajpgi.00056.2003. PMID 14561585.
- "Differential recognition of beta -lactam antibiotics by intestinal and renal peptide transporters, PEPT 1 and PEPT 2". J. Biol. Chem. 270 (43): 25672–7. 1995. doi:10.1074/jbc.270.43.25672. PMID 7592745.
- "An active mechanism for completion of the final stage of protein degradation in the liver, lysosomal transport of dipeptides". J. Biol. Chem. 272 (18): 11786–90. 1997. doi:10.1074/jbc.272.18.11786. PMID 9115234.
- "Cloning and characterization of a pH-sensing regulatory factor that modulates transport activity of the human H+/peptide cotransporter, PEPT1". Biochem. Biophys. Res. Commun. 237 (3): 577–82. 1997. doi:10.1006/bbrc.1997.7129. PMID 9299407.
- "An oligopeptide transporter is expressed at high levels in the pancreatic carcinoma cell lines AsPc-1 and Capan-2". Cancer Res. 58 (3): 519–25. 1998. PMID 9458100.
- "Substrate upregulation of the human small intestinal peptide transporter, hPepT1". J. Physiol. 507 (3): 697–706. 1998. doi:10.1111/j.1469-7793.1998.697bs.x. PMID 9508831.
- "Thyroid hormone regulates the activity and expression of the peptide transporter PEPT1 in Caco-2 cells". Am. J. Physiol. Gastrointest. Liver Physiol. 282 (4): G617–23. 2002. doi:10.1152/ajpgi.00344.2001. PMID 11897620.
- "Importance of a small N-terminal region in mammalian peptide transporters for substrate affinity and function". J. Membr. Biol. 186 (2): 55–62. 2002. doi:10.1007/s00232-001-0135-9. PMID 11944083.
- "Expression of the peptide transporter hPepT1 in human colon: a potential route for colonic protein nitrogen and drug absorption". Histochem. Cell Biol. 119 (1): 37–43. 2003. doi:10.1007/s00418-002-0479-y. PMID 12548404.
- "Delta-aminolevulinic acid transport in cancer cells of the human extrahepatic biliary duct". J. Pharmacol. Exp. Ther. 305 (1): 219–24. 2003. doi:10.1124/jpet.102.046573. PMID 12649372.
- "Hormonal regulation of dipeptide transporter (PepT1) in Caco-2 cells with normal and anoxia/reoxygenation management". World J. Gastroenterol. 9 (4): 808–12. 2003. doi:10.3748/wjg.v9.i4.808. PMID 12679938.
- "Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathway". Biochem. Biophys. Res. Commun. 306 (1): 177–85. 2003. doi:10.1016/S0006-291X(03)00926-4. PMID 12788085.
- "Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis". J. Biol. Chem. 278 (51): 51833–40. 2004. doi:10.1074/jbc.M308356200. PMID 14532279.
- "Biophysical evidence for His57 as a proton-binding site in the mammalian intestinal transporter hPepT1". Pharm. Res. 20 (12): 1911–6. 2004. doi:10.1023/B:PHAM.0000008036.05892.e9. PMID 14725353.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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