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[1][2]。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 [3]。
機能
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[1][3]。
関連項目
- 溶質キャリアファミリー（Solute carrier family）
脚注
- ^ 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).
参考文献
- “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).
- “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).
- “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.