메뉴 건너뛰기




Volumn 93, Issue 8, 2013, Pages 888-899

PepT1 expressed in immune cells has an important role in promoting the immune response during experimentally induced colitis

Author keywords

Inflammation; PepT1 KO; siRNA

Indexed keywords

CXCL1 CHEMOKINE; DEXTRAN SULFATE; GAMMA INTERFERON; INTERLEUKIN 6; LEUCINE RICH REPEAT KINASE 2; MESSENGER RNA; MONOCYTE CHEMOTACTIC PROTEIN 1; MURAMYL DIPEPTIDE; MYELOPEROXIDASE; PEPTIDE TRANSPORTER 1;

EID: 84881037638     PISSN: 00236837     EISSN: 15300307     Source Type: Journal    
DOI: 10.1038/labinvest.2013.77     Document Type: Article
Times cited : (30)

References (56)
  • 1
    • 0015160590 scopus 로고
    • Intestinal transport of dipeptides in man: Relative importance of hydrolysis and intact absorption
    • Adibi SA. Intestinal transport of dipeptides in man: relative importance of hydrolysis and intact absorption. J Clin Invest 1971;50: 2266-2275.
    • (1971) J Clin Invest , vol.50 , pp. 2266-2275
    • Adibi, S.A.1
  • 3
    • 0142244159 scopus 로고    scopus 로고
    • Regulation of expression of the intestinal oligopeptide transporter (Pept-1) in health and disease
    • Adibi SA. Regulation of expression of the intestinal oligopeptide transporter (Pept-1) in health and disease. Am J Physiol Gastrointest Liver Physiol 2003;285: G779-G788.
    • (2003) Am J Physiol Gastrointest Liver Physiol , vol.285
    • Adibi, S.A.1
  • 4
    • 0028333611 scopus 로고
    • Expression cloning of a mammalian proton-coupled oligopeptide transporter
    • Fei YJ, Kanai Y, Nussberger S, et al. Expression cloning of a mammalian proton-coupled oligopeptide transporter. Nature 1994;368: 563-566.
    • (1994) Nature , vol.368 , pp. 563-566
    • Fei, Y.J.1    Kanai, Y.2    Nussberger, S.3
  • 5
    • 0028920129 scopus 로고
    • Human intestinal H+/peptide cotransporter. Cloning, functional expression, and chromosomal localization
    • Liang R, Fei YJ, Prasad PD, et al. Human intestinal H+/peptide cotransporter. Cloning, functional expression, and chromosomal localization. J Biol Chem 1995;270: 6456-6463.
    • (1995) J Biol Chem , vol.270 , pp. 6456-6463
    • Liang, R.1    Fei, Y.J.2    Prasad, P.D.3
  • 6
    • 0040699988 scopus 로고    scopus 로고
    • Intestinal transport of betalactam antibiotics: Analysis of the affinity at the H+/peptide symporter (PEPT1), the uptake into Caco-2 cell monolayers and the transepithelial flux
    • Bretschneider B, Brandsch M, Neubert R. Intestinal transport of betalactam antibiotics: analysis of the affinity at the H+/peptide symporter (PEPT1), the uptake into Caco-2 cell monolayers and the transepithelial flux. Pharm Res 1999;16: 55-61.
    • (1999) Pharm Res , vol.16 , pp. 55-61
    • Bretschneider, B.1    Brandsch, M.2    Neubert, R.3
  • 7
    • 0036018543 scopus 로고    scopus 로고
    • Transport of peptidomimetic drugs by the intestinal Di/tri-peptide transporter, PepT1
    • Brodin B, Nielsen CU, Steffansen B, et al. Transport of peptidomimetic drugs by the intestinal Di/tri-peptide transporter, PepT1. Pharmacol Toxicol 2002;90: 285-296.
    • (2002) Pharmacol Toxicol , vol.90 , pp. 285-296
    • Brodin, B.1    Nielsen, C.U.2    Steffansen, B.3
  • 8
    • 0032158915 scopus 로고    scopus 로고
    • Transport of L-valine-acyclovir via the oligopeptide transporter in the human intestinal cell line, Caco-2
    • de Vrueh RL, Smith PL, Lee CP. Transport of L-valine-acyclovir via the oligopeptide transporter in the human intestinal cell line, Caco-2. J Pharmacol Exp Ther 1998;286: 1166-1170.
    • (1998) J Pharmacol Exp Ther , vol.286 , pp. 1166-1170
    • De Vrueh, R.L.1    Smith, P.L.2    Lee, C.P.3
  • 9
    • 0024909165 scopus 로고
    • Intestinal absorption mechanism of dipeptide angiotensin converting enzyme inhibitors of the lysylproline type: Lisinopril and SQ 29, 852
    • Friedman DI, Amidon GL. Intestinal absorption mechanism of dipeptide angiotensin converting enzyme inhibitors of the lysylproline type: lisinopril and SQ 29,852. J Pharm Sci 1989;78: 995-998.
    • (1989) J Pharm Sci , vol.78 , pp. 995-998
    • Friedman, D.I.1    Amidon, G.L.2
  • 10
    • 0025106137 scopus 로고
    • Interaction of renin inhibitors with the intestinal uptake system for oligopeptides and beta-lactam antibiotics
    • Kramer W, Girbig F, Gutjahr U, et al. Interaction of renin inhibitors with the intestinal uptake system for oligopeptides and beta-lactam antibiotics. Biochim Biophys Acta 1990;1027: 25-30.
    • (1990) Biochim Biophys Acta , vol.1027 , pp. 25-30
    • Kramer, W.1    Girbig, F.2    Gutjahr, U.3
  • 11
    • 0036744803 scopus 로고    scopus 로고
    • Transport characteristics of L-carnosine and the anticancer derivative 4-toluenesulfonylureidocarnosine in a human epithelial cell line
    • Nielsen CU, Supuran CT, Scozzafava A, et al. Transport characteristics of L-carnosine and the anticancer derivative 4-toluenesulfonylureidocarnosine in a human epithelial cell line. Pharm Res 2002;19: 1337-1344.
    • (2002) Pharm Res , vol.19 , pp. 1337-1344
    • Nielsen, C.U.1    Supuran, C.T.2    Scozzafava, A.3
  • 12
    • 2342644210 scopus 로고    scopus 로고
    • Molecular and integrative physiology of intestinal peptide transport
    • Daniel H. Molecular and integrative physiology of intestinal peptide transport. Annu Rev Physiol 2004;66: 361-384.
    • (2004) Annu Rev Physiol , vol.66 , pp. 361-384
    • Daniel, H.1
  • 13
    • 0032435805 scopus 로고    scopus 로고
    • HPepT1-mediated epithelial transport of bacteria-derived chemotactic peptides enhances neutrophil-epithelial interactions
    • Merlin D, Steel A, Gewirtz AT, et al. hPepT1-mediated epithelial transport of bacteria-derived chemotactic peptides enhances neutrophil- epithelial interactions. J Clin Invest 1998;102: 2011-2018.
    • (1998) J Clin Invest , vol.102 , pp. 2011-2018
    • Merlin, D.1    Steel, A.2    Gewirtz, A.T.3
  • 14
    • 0142151072 scopus 로고    scopus 로고
    • Interferon-gamma increases hPepT1-mediated uptake of di-tripeptides including the bacterial tripeptide fMLP in polarized intestinal epithelia
    • Buyse M, Charrier L, Sitaraman S, et al. Interferon-gamma increases hPepT1-mediated uptake of di-tripeptides including the bacterial tripeptide fMLP in polarized intestinal epithelia. Am J Pathol 2003;163: 1969-1977.
    • (2003) Am J Pathol , vol.163 , pp. 1969-1977
    • Buyse, M.1    Charrier, L.2    Sitaraman, S.3
  • 15
    • 7644234401 scopus 로고    scopus 로고
    • HPepT1 transports muramyl dipeptide, activating NF-kappaB and stimulating IL-8 secretion in human colonic Caco2/bbe cells
    • Vavricka SR, Musch MW, Chang JE, et al. hPepT1 transports muramyl dipeptide, activating NF-kappaB and stimulating IL-8 secretion in human colonic Caco2/bbe cells. Gastroenterology 2004;127: 1401-1409.
    • (2004) Gastroenterology , vol.127 , pp. 1401-1409
    • Vavricka, S.R.1    Musch, M.W.2    Chang, J.E.3
  • 16
    • 77957000911 scopus 로고    scopus 로고
    • PepT1 mediates transport of the proinflammatory bacterial tripeptide L-Ala-{gamma}- D-Glu-meso-DAP in intestinal epithelial cells
    • Dalmasso G, Nguyen HT, Charrier-Hisamuddin L, et al. PepT1 mediates transport of the proinflammatory bacterial tripeptide L-Ala-{gamma}- D-Glu-meso-DAP in intestinal epithelial cells. Am J Physiol Gastrointest Liver Physiol 2010;299: G687-G696.
    • (2010) Am J Physiol Gastrointest Liver Physiol , vol.299
    • Dalmasso, G.1    Nguyen, H.T.2    Charrier-Hisamuddin, L.3
  • 17
    • 0035011324 scopus 로고    scopus 로고
    • Colonic epithelial hPepT1 expression occurs in inflammatory bowel disease: Transport of bacterial peptides influences expression of MHC class 1 molecules
    • Merlin D, Si-Tahar M, Sitaraman SV, et al. Colonic epithelial hPepT1 expression occurs in inflammatory bowel disease: transport of bacterial peptides influences expression of MHC class 1 molecules. Gastroenterology 2001;120: 1666-1679.
    • (2001) Gastroenterology , vol.120 , pp. 1666-1679
    • Merlin, D.1    Si-Tahar, M.2    Sitaraman, S.V.3
  • 18
    • 70349428307 scopus 로고    scopus 로고
    • Pathogenic bacteria induce colonic PepT1 expression: An implication in host defense response
    • e1-2
    • Nguyen HT, Dalmasso G, Powell KR, et al. Pathogenic bacteria induce colonic PepT1 expression: an implication in host defense response. Gastroenterology 2009;137: 1435-47, e1-2.
    • (2009) Gastroenterology , vol.137 , pp. 1435-1447
    • Nguyen, H.T.1    Dalmasso, G.2    Powell, K.R.3
  • 19
    • 33847700163 scopus 로고    scopus 로고
    • Leptin transcriptionally enhances peptide transporter (hPepT1) expression and activity via the cAMPresponse element-binding protein and Cdx2 transcription factors
    • Nduati V, Yan Y, Dalmasso G, et al. Leptin transcriptionally enhances peptide transporter (hPepT1) expression and activity via the cAMPresponse element-binding protein and Cdx2 transcription factors. J Biol Chem 2007;282: 1359-1373.
    • (2007) J Biol Chem , vol.282 , pp. 1359-1373
    • Nduati, V.1    Yan, Y.2    Dalmasso, G.3
  • 20
    • 33646858115 scopus 로고    scopus 로고
    • The oligopeptide transporter hPepT1: Gateway to the innate immune response
    • Charrier L, Merlin D. The oligopeptide transporter hPepT1: gateway to the innate immune response. Lab Invest 2006;86: 538-546.
    • (2006) Lab Invest , vol.86 , pp. 538-546
    • Charrier, L.1    Merlin, D.2
  • 21
    • 0035451799 scopus 로고    scopus 로고
    • Intestinal macrophages lack CD14 and CD89 and consequently are downregulated for LPS- and IgA-mediated activities
    • Smith PD, Smythies LE, Mosteller-Barnum M, et al. Intestinal macrophages lack CD14 and CD89 and consequently are downregulated for LPS- and IgA-mediated activities. J Immunol 2001;167: 2651-2656.
    • (2001) J Immunol , vol.167 , pp. 2651-2656
    • Smith, P.D.1    Smythies, L.E.2    Mosteller-Barnum, M.3
  • 22
    • 13744256812 scopus 로고    scopus 로고
    • Human intestinal macrophages display profound inflammatory anergy despite avid phagocytic and bacteriocidal activity
    • Smythies LE, Sellers M, Clements RH, et al. Human intestinal macrophages display profound inflammatory anergy despite avid phagocytic and bacteriocidal activity. J Clin Invest 2005;115: 66-75.
    • (2005) J Clin Invest , vol.115 , pp. 66-75
    • Smythies, L.E.1    Sellers, M.2    Clements, R.H.3
  • 23
    • 0036889016 scopus 로고    scopus 로고
    • PepT1-mediated fMLP transport induces intestinal inflammation in vivo
    • Buyse M, Tsocas A, Walker F, et al. PepT1-mediated fMLP transport induces intestinal inflammation in vivo. Am J Physiol Cell Physiol 2002;283: C1795-C1800.
    • (2002) Am J Physiol Cell Physiol , vol.283
    • Buyse, M.1    Tsocas, A.2    Walker, F.3
  • 24
    • 0033517126 scopus 로고    scopus 로고
    • The majority of H2-M3 is retained intracellularly in a peptide-receptive state and traffics to the cell surface in the presence of N-formylated peptides
    • Chiu NM, Chun T, Fay M, et al. The majority of H2-M3 is retained intracellularly in a peptide-receptive state and traffics to the cell surface in the presence of N-formylated peptides. J Exp Med 1999; 190: 423-434.
    • (1999) J Exp Med , vol.190 , pp. 423-434
    • Chiu, N.M.1    Chun, T.2    Fay, M.3
  • 25
    • 0036839229 scopus 로고    scopus 로고
    • Formyl-peptide receptors revisited
    • Le Y, Murphy PM, Wang JM. Formyl-peptide receptors revisited. Trends Immunol 2002;23: 541-548.
    • (2002) Trends Immunol , vol.23 , pp. 541-548
    • Le, Y.1    Murphy, P.M.2    Wang, J.M.3
  • 26
    • 1542380052 scopus 로고    scopus 로고
    • Innate immunity and mucosal bacterial interactions in the intestine
    • Eckmann L. Innate immunity and mucosal bacterial interactions in the intestine. Curr Opin Gastroenterol 2004;20: 82-88.
    • (2004) Curr Opin Gastroenterol , vol.20 , pp. 82-88
    • Eckmann, L.1
  • 27
    • 33646887917 scopus 로고    scopus 로고
    • Sensor molecules in intestinal innate immunity against bacterial infections
    • Eckmann L. Sensor molecules in intestinal innate immunity against bacterial infections. Curr Opin Gastroenterol 2006;22: 95-101.
    • (2006) Curr Opin Gastroenterol , vol.22 , pp. 95-101
    • Eckmann, L.1
  • 28
    • 5144228220 scopus 로고    scopus 로고
    • The role of Toll-like receptors and Nod proteins in bacterial infection
    • Philpott DJ, Girardin SE. The role of Toll-like receptors and Nod proteins in bacterial infection. Mol Immunol 2004;41: 1099-1108.
    • (2004) Mol Immunol , vol.41 , pp. 1099-1108
    • Philpott, D.J.1    Girardin, S.E.2
  • 29
    • 19944431742 scopus 로고    scopus 로고
    • Inherited disorders of human Tolllike receptor signaling: Immunological implications
    • Ku CL, Yang K, Bustamante J, et al. Inherited disorders of human Tolllike receptor signaling: immunological implications. Immunol Rev 2005;203: 10-20.
    • (2005) Immunol Rev , vol.203 , pp. 10-20
    • Ku, C.L.1    Yang, K.2    Bustamante, J.3
  • 30
    • 0041827164 scopus 로고    scopus 로고
    • Nods, Nalps and Naip: Intracellular regulators of bacterial-induced inflammation
    • Chamaillard M, Girardin SE, Viala J, et al. Nods, Nalps and Naip: intracellular regulators of bacterial-induced inflammation. Cell Microbiol 2003;5: 581-592.
    • (2003) Cell Microbiol , vol.5 , pp. 581-592
    • Chamaillard, M.1    Girardin, S.E.2    Viala, J.3
  • 31
    • 22244465576 scopus 로고    scopus 로고
    • Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition
    • Barnich N, Aguirre JE, Reinecker HC, et al. Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition. J Cell Biol 2005;170: 21-26.
    • (2005) J Cell Biol , vol.170 , pp. 21-26
    • Barnich, N.1    Aguirre, J.E.2    Reinecker, H.C.3
  • 32
    • 17644366913 scopus 로고    scopus 로고
    • NOD-LRR proteins: Role in host-microbial interactions and inflammatory disease
    • Inohara Chamaillard, McDonald C, Nunez G. NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Ann RevBiochem 2005;74: 355-383.
    • (2005) Ann RevBiochem , vol.74 , pp. 355-383
    • Chamaillard, I.1    McDonald, C.2    Nunez, G.3
  • 33
    • 0038624558 scopus 로고    scopus 로고
    • NODs: Intracellular proteins involved in inflammation and apoptosis
    • Inohara N, Nunez G. NODs: intracellular proteins involved in inflammation and apoptosis. Nat RevImmunol 2003;3: 371-382.
    • (2003) Nat RevImmunol , vol.3 , pp. 371-382
    • Inohara, N.1    Nunez, G.2
  • 34
    • 0042433511 scopus 로고    scopus 로고
    • Toll-like receptors and NOD/CARD proteins: Pattern recognition receptors are key elements in the regulation of immune response
    • Murillo LS, Morre SA, Pena AS. Toll-like receptors and NOD/CARD proteins: pattern recognition receptors are key elements in the regulation of immune response. Drugs Today 2003;39: 415-438.
    • (2003) Drugs Today , vol.39 , pp. 415-438
    • Murillo, L.S.1    Morre, S.A.2    Pena, A.S.3
  • 35
    • 33244472793 scopus 로고    scopus 로고
    • Signalling pathways and molecular interactions of NOD1 and NOD2
    • Strober W, Murray PJ, Kitani A, et al. Signalling pathways and molecular interactions of NOD1 and NOD2. Nat Rev Immunol 2006; 6: 9-20.
    • (2006) Nat Rev Immunol , vol.6 , pp. 9-20
    • Strober, W.1    Murray, P.J.2    Kitani, A.3
  • 36
    • 2342583513 scopus 로고    scopus 로고
    • Regulatory regions and critical residues of NOD2 involved in muramyl dipeptide recognition
    • Tanabe T, Chamaillard M, Ogura Y, et al. Regulatory regions and critical residues of NOD2 involved in muramyl dipeptide recognition. EMBO J 2004;23: 1587-1597.
    • (2004) EMBO J , vol.23 , pp. 1587-1597
    • Tanabe, T.1    Chamaillard, M.2    Ogura, Y.3
  • 37
    • 3242794263 scopus 로고    scopus 로고
    • Nods and 'intracellular' innate immunity
    • Viala J, Sansonetti P, Philpott DJ. Nods and 'intracellular' innate immunity. C R Biol 2004;327: 551-555.
    • (2004) C R Biol , vol.327 , pp. 551-555
    • Viala, J.1    Sansonetti, P.2    Philpott, D.J.3
  • 38
    • 80053616405 scopus 로고    scopus 로고
    • The PepT1-NOD2 signaling pathway aggravates induced colitis in mice
    • Dalmasso G, Nguyen HT, Ingersoll SA, et al. The PepT1-NOD2 signaling pathway aggravates induced colitis in mice. Gastroenterology 2011; 141: 1334-1345.
    • (2011) Gastroenterology , vol.141 , pp. 1334-1345
    • Dalmasso, G.1    Nguyen, H.T.2    Ingersoll, S.A.3
  • 39
    • 80052230551 scopus 로고    scopus 로고
    • L-Ala-gamma-D-Glu-meso-diaminopimelic acid (DAP) interacts directly with leucine-rich region domain of nucleotide-binding oligomerization domain 1, increasing phosphorylation activity of receptor-interacting serine/threonine- protein kinase 2 and its interaction with nucleotide-binding oligomerization domain 1
    • Laroui H, Yan Y, Narui Y, et al. L-Ala-gamma-D-Glu-meso-diaminopimelic acid (DAP) interacts directly with leucine-rich region domain of nucleotide-binding oligomerization domain 1, increasing phosphorylation activity of receptor-interacting serine/threonine-protein kinase 2 and its interaction with nucleotide-binding oligomerization domain 1. J Biol Chem 2011;286: 31003-31013.
    • (2011) J Biol Chem , vol.286 , pp. 31003-31013
    • Laroui, H.1    Yan, Y.2    Narui, Y.3
  • 40
    • 0027224059 scopus 로고
    • Clinicopathologic study of dextran sulfate sodium experimental murine colitis
    • Cooper HS, Murthy SN, Shah RS, et al. Clinicopathologic study of dextran sulfate sodium experimental murine colitis. Lab Invest 1993;69: 238-249.
    • (1993) Lab Invest , vol.69 , pp. 238-249
    • Cooper, H.S.1    Murthy, S.N.2    Shah, R.S.3
  • 41
    • 84861858185 scopus 로고    scopus 로고
    • Intestinal epithelial CD98 synthesis specifically modulates expression of colonic microRNAs during colitis
    • Charania MA, Ayyadurai S, Ingersoll SA, et al. Intestinal epithelial CD98 synthesis specifically modulates expression of colonic microRNAs during colitis. Am J Physiol Gastrointest Liver Physiol 2012;302: G1282-G1291.
    • (2012) Am J Physiol Gastrointest Liver Physiol , vol.302
    • Charania, M.A.1    Ayyadurai, S.2    Ingersoll, S.A.3
  • 42
    • 84874743026 scopus 로고    scopus 로고
    • Intestinal epithelial CD98 directly modulates the innate host response to enteric bacterial pathogens
    • Charania MA, Laroui H, Liu H, et al. Intestinal epithelial CD98 directly modulates the innate host response to enteric bacterial pathogens. Infect Immun 2013;81: 923-934.
    • (2013) Infect Immun , vol.81 , pp. 923-934
    • Charania, M.A.1    Laroui, H.2    Liu, H.3
  • 43
    • 38449084962 scopus 로고    scopus 로고
    • Isolation and subsequent analysis of murine lamina propria mononuclear cells from colonic tissue
    • Weigmann B, Tubbe I, Seidel D, et al. Isolation and subsequent analysis of murine lamina propria mononuclear cells from colonic tissue. Nat Protoc 2007;2: 2307-2311.
    • (2007) Nat Protoc , vol.2 , pp. 2307-2311
    • Weigmann, B.1    Tubbe, I.2    Seidel, D.3
  • 44
    • 0019487913 scopus 로고
    • Chemotaxis by mouse macrophage cell lines
    • Aksamit RR, Falk W, Leonard EJ. Chemotaxis by mouse macrophage cell lines. J Immunol 1981;126: 2194-2199.
    • (1981) J Immunol , vol.126 , pp. 2194-2199
    • Aksamit, R.R.1    Falk, W.2    Leonard, E.J.3
  • 45
    • 34848889673 scopus 로고    scopus 로고
    • Communicable ulcerative colitis induced by T-bet deficiency in the innate immune system
    • Garrett WS, Lord GM, Punit S, et al. Communicable ulcerative colitis induced by T-bet deficiency in the innate immune system. Cell 2007;131: 33-45.
    • (2007) Cell , vol.131 , pp. 33-45
    • Garrett, W.S.1    Lord, G.M.2    Punit, S.3
  • 46
    • 0037112050 scopus 로고    scopus 로고
    • Critical roles of activationinduced cytidine deaminase in the homeostasis of gut flora
    • Fagarasan S, Muramatsu M, Suzuki K, et al. Critical roles of activationinduced cytidine deaminase in the homeostasis of gut flora. Science 2002;298: 1424-1427.
    • (2002) Science , vol.298 , pp. 1424-1427
    • Fagarasan, S.1    Muramatsu, M.2    Suzuki, K.3
  • 47
    • 3242664636 scopus 로고    scopus 로고
    • Recognition of commensal microflora by toll-like receptors is required for intestinal homeostasis
    • Rakoff-Nahoum S, Paglino J, Eslami-Varzaneh F, et al. Recognition of commensal microflora by toll-like receptors is required for intestinal homeostasis. Cell 2004;118: 229-241.
    • (2004) Cell , vol.118 , pp. 229-241
    • Rakoff-Nahoum, S.1    Paglino, J.2    Eslami-Varzaneh, F.3
  • 48
    • 33646122461 scopus 로고    scopus 로고
    • HPepT1 mediates bacterial tripeptide fMLP uptake in human monocytes
    • Charrier L, Driss A, Yan Y, et al. hPepT1 mediates bacterial tripeptide fMLP uptake in human monocytes. Lab Invest 2006;86: 490-503.
    • (2006) Lab Invest , vol.86 , pp. 490-503
    • Charrier, L.1    Driss, A.2    Yan, Y.3
  • 49
    • 70349092762 scopus 로고    scopus 로고
    • Changes in mRNA expression levels of solute carrier transporters in inflammatory bowel disease patients
    • Wojtal KA, Eloranta JJ, Hruz P, et al. Changes in mRNA expression levels of solute carrier transporters in inflammatory bowel disease patients. Drug Metab Dispos 2009;37: 1871-1877.
    • (2009) Drug Metab Dispos , vol.37 , pp. 1871-1877
    • Wojtal, K.A.1    Eloranta, J.J.2    Hruz, P.3
  • 50
    • 70450189276 scopus 로고    scopus 로고
    • PepT1 oligopeptide transporter (SLC15A1) gene polymorphism in inflammatory bowel disease
    • Zucchelli M, Torkvist L, Bresso F, et al. PepT1 oligopeptide transporter (SLC15A1) gene polymorphism in inflammatory bowel disease. Inflamm Bowel Dis 2009;15: 1562-1569.
    • (2009) Inflamm Bowel Dis , vol.15 , pp. 1562-1569
    • Zucchelli, M.1    Torkvist, L.2    Bresso, F.3
  • 51
    • 84874045942 scopus 로고    scopus 로고
    • Significance of peptide transporter 1 in the intestinal permeability of valacyclovir in wild-type and PepT1 knockout mice
    • Yang B, Smith D. Significance of peptide transporter 1 in the intestinal permeability of valacyclovir in wild-type and PepT1 knockout mice. Drug Metab Dispos 2013;41: 608-614.
    • (2013) Drug Metab Dispos , vol.41 , pp. 608-614
    • Yang, B.1    Smith, D.2
  • 52
    • 78649546509 scopus 로고    scopus 로고
    • Lactobacillus plantarum consumption increases PepT1-mediated amino acid absorption by enhancing protein kinase C activity in spontaneously colitic mice
    • Chen HQ, Shen TY, Zhou YK, et al. Lactobacillus plantarum consumption increases PepT1-mediated amino acid absorption by enhancing protein kinase C activity in spontaneously colitic mice. J Nutr 2010;140: 2201-2206.
    • (2010) J Nutr , vol.140 , pp. 2201-2206
    • Chen, H.Q.1    Shen, T.Y.2    Zhou, Y.K.3
  • 53
    • 78649743335 scopus 로고    scopus 로고
    • Lactobacillus plantarum ameliorates colonic epithelial barrier dysfunction by modulating the apical junctional complex and PepT1 in IL-10 knockout mice
    • Chen HQ, Yang J, Zhang M, et al. Lactobacillus plantarum ameliorates colonic epithelial barrier dysfunction by modulating the apical junctional complex and PepT1 in IL-10 knockout mice. Am J Physiol Gastrointest Liver Physiol 2010;299: G1287-G1297.
    • (2010) Am J Physiol Gastrointest Liver Physiol , vol.299
    • Chen, H.Q.1    Yang, J.2    Zhang, M.3
  • 54
    • 64649096522 scopus 로고    scopus 로고
    • Targeted disruption of peptide transporter Pept1 gene in mice significantly reduces dipeptide absorption in intestine
    • Hu Y, Smith DE, Ma K, et al. Targeted disruption of peptide transporter Pept1 gene in mice significantly reduces dipeptide absorption in intestine. Mol Pharm 2008;5: 1122-1130.
    • (2008) Mol Pharm , vol.5 , pp. 1122-1130
    • Hu, Y.1    Smith, D.E.2    Ma, K.3
  • 55
    • 0036291818 scopus 로고    scopus 로고
    • Transport and utilization of arginine and arginine-containing peptides by rat alveolar macrophages
    • Yang XD, Ma JY, Barger MW, et al. Transport and utilization of arginine and arginine-containing peptides by rat alveolar macrophages. Pharm Res 2002;19: 825-831.
    • (2002) Pharm Res , vol.19 , pp. 825-831
    • Yang, X.D.1    Ma, J.Y.2    Barger, M.W.3
  • 56
    • 79953084107 scopus 로고    scopus 로고
    • The Nlrp3 inflammasome: Contributions to intestinal homeostasis
    • Zaki MH, Lamkanfi M, Kanneganti TD. The Nlrp3 inflammasome: contributions to intestinal homeostasis. Trends Immunol 2011;32: 171-179.
    • (2011) Trends Immunol , vol.32 , pp. 171-179
    • Zaki, M.H.1    Lamkanfi, M.2    Kanneganti, T.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.