ペプチドトランスポーター1

ペプチドトランスポーター1 （英: Peptide transporter 1、PepT1、PEPT1）は、溶質キャリアファミリー15メンバー1（solute carrier family 15 member 1、SLC15A1）としても知られ、ヒトではSLC15A1 遺伝子によってコードされるタンパク質。PepT 1は、 オリゴペプチドの輸送担体で、腎でオリゴペプチドの再吸収、腸でプロトン依存的に機能するため、共輸送体のように作用する 。 SLC15A1は小腸上皮の刷子縁膜（brush border membrane)に局在し、内腔（lumen）から腸細胞（enterocyte)へのジペプチドおよびトリペプチドの取り込みを媒介する。 このタンパク質は、食物中のタンパク質の摂取と消化に重要な役割を果たしている。 このタンパク質はまた、多数のペプチド模倣薬の吸収を促進する。 溶質キャリアファミリー（Solute carrier family） ^ a b “Entrez Gene: SLC15A1 Solute carrier family 15 (oligopeptide transporter), member 1”. 2020年1月9日閲覧。 ^ “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.  ^ a b “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.  “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. PMC 2230834. PMID 9508831. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2230834/.  “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. PMC 4611455. PMID 12679938. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4611455/.  “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.