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<!--{{Infobox gene}}-->'''ペプチドトランスポーター1''' （{{lang-en-short|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]]<ref name="entrez">{{Cite web|title=Entrez Gene: SLC15A1 Solute carrier family 15 (oligopeptide transporter), member 1|url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6564|accessdate=2020-01-09}}</ref><ref name="pmid7896779">{{Cite journal|date=March 1995|title=Human intestinal H+/peptide cotransporter. Cloning, functional expression, and chromosomal localization|journal=J. Biol. Chem.|volume=270|issue=12|pages=6456–63| |
<!--{{Infobox gene}}-->'''ペプチドトランスポーター1''' （{{lang-en-short|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]]<ref name="entrez">{{Cite web|title=Entrez Gene: SLC15A1 Solute carrier family 15 (oligopeptide transporter), member 1|url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6564|accessdate=2020-01-09}}</ref><ref name="pmid7896779">{{Cite journal|date=March 1995|title=Human intestinal H+/peptide cotransporter. Cloning, functional expression, and chromosomal localization|journal=J. Biol. Chem.|volume=270|issue=12|pages=6456–63|doi=10.1074/jbc.270.12.6456|pmid=7896779}}</ref>。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 <ref name="pmid9207295">{{Cite journal|date=July 1997|title=The oligopeptide transporter (Pept-1) in human intestine: biology and function|journal=Gastroenterology|volume=113|issue=1|pages=332–40|doi=10.1016/S0016-5085(97)70112-4|pmid=9207295}}</ref>。 |
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== 機能 == |
== 機能 == |
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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<ref name="entrez" /><ref name="pmid9207295">{{Cite journal|date=July 1997|title=The oligopeptide transporter (Pept-1) in human intestine: biology and function|journal=Gastroenterology|volume=113|issue=1|pages=332–40| |
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<ref name="entrez" /><ref name="pmid9207295">{{Cite journal|date=July 1997|title=The oligopeptide transporter (Pept-1) in human intestine: biology and function|journal=Gastroenterology|volume=113|issue=1|pages=332–40|doi=10.1016/S0016-5085(97)70112-4|pmid=9207295}}</ref>。 |
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== 関連項目 == |
== 関連項目 == |
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== 参考文献 == |
== 参考文献 == |
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{{Refbegin|2}} |
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* {{Cite journal|year=2003|title=Regulation of expression of the intestinal oligopeptide transporter (Pept-1) in health and disease|journal=Am. J. Physiol. Gastrointest. Liver Physiol.|volume=285|issue=5|pages=G779–88| |
* {{Cite journal|year=2003|title=Regulation of expression of the intestinal oligopeptide transporter (Pept-1) in health and disease|journal=Am. J. Physiol. Gastrointest. Liver Physiol.|volume=285|issue=5|pages=G779–88|doi=10.1152/ajpgi.00056.2003|pmid=14561585}} |
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* {{Cite journal|year=1995|title=Differential recognition of beta -lactam antibiotics by intestinal and renal peptide transporters, PEPT 1 and PEPT 2|journal=J. Biol. Chem.|volume=270|issue=43|pages=25672–7| |
* {{Cite journal|year=1995|title=Differential recognition of beta -lactam antibiotics by intestinal and renal peptide transporters, PEPT 1 and PEPT 2|journal=J. Biol. Chem.|volume=270|issue=43|pages=25672–7|doi=10.1074/jbc.270.43.25672|pmid=7592745}} |
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* {{Cite journal|year=1997|title=An active mechanism for completion of the final stage of protein degradation in the liver, lysosomal transport of dipeptides|journal=J. Biol. Chem.|volume=272|issue=18|pages=11786–90| |
* {{Cite journal|year=1997|title=An active mechanism for completion of the final stage of protein degradation in the liver, lysosomal transport of dipeptides|journal=J. Biol. Chem.|volume=272|issue=18|pages=11786–90|doi=10.1074/jbc.272.18.11786|pmid=9115234}} |
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* {{Cite journal|year=1997|title=Cloning and characterization of a pH-sensing regulatory factor that modulates transport activity of the human H+/peptide cotransporter, PEPT1|journal=Biochem. Biophys. Res. Commun.|volume=237|issue=3|pages=577–82| |
* {{Cite journal|year=1997|title=Cloning and characterization of a pH-sensing regulatory factor that modulates transport activity of the human H+/peptide cotransporter, PEPT1|journal=Biochem. Biophys. Res. Commun.|volume=237|issue=3|pages=577–82|doi=10.1006/bbrc.1997.7129|pmid=9299407}} |
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* {{Cite journal|year=1998|title=An oligopeptide transporter is expressed at high levels in the pancreatic carcinoma cell lines AsPc-1 and Capan-2|journal=Cancer Res.|volume=58|issue=3|pages=519–25| |
* {{Cite journal|year=1998|title=An oligopeptide transporter is expressed at high levels in the pancreatic carcinoma cell lines AsPc-1 and Capan-2|journal=Cancer Res.|volume=58|issue=3|pages=519–25|doi=|pmid=9458100}} |
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* {{Cite journal|year=1998|title=Substrate upregulation of the human small intestinal peptide transporter, hPepT1|journal=J. Physiol.|volume=507|issue=3|pages=697–706| |
* {{Cite journal|year=1998|title=Substrate upregulation of the human small intestinal peptide transporter, hPepT1|journal=J. Physiol.|volume=507|issue=3|pages=697–706|doi=10.1111/j.1469-7793.1998.697bs.x|pmid=9508831|pmc=2230834}} |
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* {{Cite journal|year=2002|title=Thyroid hormone regulates the activity and expression of the peptide transporter PEPT1 in Caco-2 cells|journal=Am. J. Physiol. Gastrointest. Liver Physiol.|volume=282|issue=4|pages=G617–23| |
* {{Cite journal|year=2002|title=Thyroid hormone regulates the activity and expression of the peptide transporter PEPT1 in Caco-2 cells|journal=Am. J. Physiol. Gastrointest. Liver Physiol.|volume=282|issue=4|pages=G617–23|doi=10.1152/ajpgi.00344.2001|pmid=11897620}} |
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* {{Cite journal|year=2002|title=Importance of a small N-terminal region in mammalian peptide transporters for substrate affinity and function|journal=J. Membr. Biol.|volume=186|issue=2|pages=55–62| |
* {{Cite journal|year=2002|title=Importance of a small N-terminal region in mammalian peptide transporters for substrate affinity and function|journal=J. Membr. Biol.|volume=186|issue=2|pages=55–62|doi=10.1007/s00232-001-0135-9|pmid=11944083}} |
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* {{Cite journal|year=2003|title=Expression of the peptide transporter hPepT1 in human colon: a potential route for colonic protein nitrogen and drug absorption|journal=Histochem. Cell Biol.|volume=119|issue=1|pages=37–43| |
* {{Cite journal|year=2003|title=Expression of the peptide transporter hPepT1 in human colon: a potential route for colonic protein nitrogen and drug absorption|journal=Histochem. Cell Biol.|volume=119|issue=1|pages=37–43|doi=10.1007/s00418-002-0479-y|pmid=12548404}} |
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* {{Cite journal|year=2003|title=Delta-aminolevulinic acid transport in cancer cells of the human extrahepatic biliary duct|journal=J. Pharmacol. Exp. Ther.|volume=305|issue=1|pages=219–24| |
* {{Cite journal|year=2003|title=Delta-aminolevulinic acid transport in cancer cells of the human extrahepatic biliary duct|journal=J. Pharmacol. Exp. Ther.|volume=305|issue=1|pages=219–24|doi=10.1124/jpet.102.046573|pmid=12649372}} |
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* {{Cite journal|year=2003|title=Hormonal regulation of dipeptide transporter (PepT1) in Caco-2 cells with normal and anoxia/reoxygenation management|journal=World J. Gastroenterol.|volume=9|issue=4|pages=808–12| |
* {{Cite journal|year=2003|title=Hormonal regulation of dipeptide transporter (PepT1) in Caco-2 cells with normal and anoxia/reoxygenation management|journal=World J. Gastroenterol.|volume=9|issue=4|pages=808–12|doi=10.3748/wjg.v9.i4.808|pmid=12679938|pmc=4611455}} |
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* {{Cite journal|year=2003|title=Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathway|journal=Biochem. Biophys. Res. Commun.|volume=306|issue=1|pages=177–85| |
* {{Cite journal|year=2003|title=Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathway|journal=Biochem. Biophys. Res. Commun.|volume=306|issue=1|pages=177–85|doi=10.1016/S0006-291X(03)00926-4|pmid=12788085}} |
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* {{Cite journal|year=2004|title=Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis|journal=J. Biol. Chem.|volume=278|issue=51|pages=51833–40| |
* {{Cite journal|year=2004|title=Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis|journal=J. Biol. Chem.|volume=278|issue=51|pages=51833–40|doi=10.1074/jbc.M308356200|pmid=14532279}} |
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* {{Cite journal|year=2004|title=Biophysical evidence for His57 as a proton-binding site in the mammalian intestinal transporter hPepT1|journal=Pharm. Res.|volume=20|issue=12|pages=1911–6| |
* {{Cite journal|year=2004|title=Biophysical evidence for His57 as a proton-binding site in the mammalian intestinal transporter hPepT1|journal=Pharm. Res.|volume=20|issue=12|pages=1911–6|doi=10.1023/B:PHAM.0000008036.05892.e9|pmid=14725353}} |
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{{Refend}} |
{{Refend}} |
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2020年1月25日 (土) 19:07時点における版
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.