메뉴 건너뛰기




Volumn 84, Issue 12, 2006, Pages 1313-1319

hPepT1 selectively transports muramyl dipeptide but not Nod1-activating muramyl peptides

Author keywords

Crohn's disease; hPepT1; Inflammation; Muramyl peptides; Nod1; Nod2; Peptidoglycan

Indexed keywords

6 O STEAROYL MURAMYL DIPEPTIDE; CASPASE RECRUITMENT DOMAIN PROTEIN 15; CASPASE RECRUITMENT DOMAIN PROTEIN 4; LACTOYL LEUCYLALANYLASPARTYLGLUTAMYL MESO DIAMINOPIMELIC ACID GLYCINE; LEUCYLALANYLASPARTYLGLUTAMYL MESO DIAMINOPIMELIC ACID; MURAMYL DIPEPTIDE; MURAMYL PEPTIDE; N ACETYL GLUCOSAMINE BETA 1,4 N ACETYL ANHYDRO MURAMYL LEUCYLALANYLASPARTYLGLUTAMYL MESO DIAMINOPIMELIC ACID ASPARTYLALANINE; N ACETYL GLUCOSAMINE BETA 1,4 N ACETYL MURAMYL DIPEPTIDE; N ACETYL MURAMYL LEUCYLALANYLASPARTYLGLUTAMYL MESO DIAMINOPIMELIC ACID; N ACETYL MURAMYL LYSYLALANYLASPARTYLGLUTAMYLLEUCYLLYSINE; PEPTIDE TRANSPORTER 1; UNCLASSIFIED DRUG;

EID: 34248152308     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/Y06-076     Document Type: Article
Times cited : (78)

References (35)
  • 1
    • 0033532091 scopus 로고    scopus 로고
    • Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-κB
    • doi:10.1074/jbc.274.19. 12955
    • Benin, J., Nir, W.J., Fischer, C.M., Tayber, O.V., Errada, P.R., Grant, J.R., et al. 1999. Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-κB. J. Biol. Chem. 274: 12955-12958. doi:10.1074/jbc.274.19. 12955.
    • (1999) J. Biol. Chem , vol.274 , pp. 12955-12958
    • Benin, J.1    Nir, W.J.2    Fischer, C.M.3    Tayber, O.V.4    Errada, P.R.5    Grant, J.R.6
  • 2
    • 13444266131 scopus 로고    scopus 로고
    • The role of peptidoglycan in pathogenesis
    • doi:10.1016/j.mib.2004.12.008
    • Boneca, I.G. 2005. The role of peptidoglycan in pathogenesis. Curr. Opin. Microbiol. 8: 46-53. doi:10.1016/j.mib.2004.12.008.
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 46-53
    • Boneca, I.G.1
  • 3
    • 0038824980 scopus 로고    scopus 로고
    • An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
    • doi:10.1038/ni945
    • Chamaillard, M., Hashimoto, M., Horie, Y., Masumoto, J., Qiu, S., Saab, L., et al. 2003. An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nat. Immunol. 4: 702-707. doi:10.1038/ni945.
    • (2003) Nat. Immunol , vol.4 , pp. 702-707
    • Chamaillard, M.1    Hashimoto, M.2    Horie, Y.3    Masumoto, J.4    Qiu, S.5    Saab, L.6
  • 5
    • 0348048803 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins (PGRPs)
    • doi:10.1016/j.molimm.2003.10. 011
    • Dziarski, R. 2004. Peptidoglycan recognition proteins (PGRPs). Mol. Immunol. 40: 877-886. doi:10.1016/j.molimm.2003.10. 011.
    • (2004) Mol. Immunol , vol.40 , pp. 877-886
    • Dziarski, R.1
  • 6
    • 23344449406 scopus 로고    scopus 로고
    • Staphylococcus aureus peptidoglycan is a toll-like receptor 2 activator: A reevaluation
    • doi:10.1128/IAI.73.8.5212-5216.2005
    • Dziarski, R., and Gupta, D. 2005. Staphylococcus aureus peptidoglycan is a toll-like receptor 2 activator: a reevaluation. Infect. Immun. 73: 5212-5216. doi:10.1128/IAI.73.8.5212-5216.2005.
    • (2005) Infect. Immun , vol.73 , pp. 5212-5216
    • Dziarski, R.1    Gupta, D.2
  • 7
    • 0032502682 scopus 로고    scopus 로고
    • Binding of bacterial peptidoglycan to CD14
    • doi:10.1074/jbc.273.15.8680
    • Dziarski, R., Tapping, R.I., and Tobias, P.S. 1998. Binding of bacterial peptidoglycan to CD14. J. Biol. Chem. 273: 8680-8690. doi:10.1074/jbc.273.15.8680.
    • (1998) J. Biol. Chem , vol.273 , pp. 8680-8690
    • Dziarski, R.1    Tapping, R.I.2    Tobias, P.S.3
  • 8
    • 3442893287 scopus 로고    scopus 로고
    • Mini-review: The role of peptidoglycan recognition in innate immunity
    • doi:10.1002/eji.200425095
    • Girardin, S.E., and Philpott, D.J. 2004. Mini-review: the role of peptidoglycan recognition in innate immunity. Eur. J. Immunol. 34: 1777-1782. doi:10.1002/eji.200425095.
    • (2004) Eur. J. Immunol , vol.34 , pp. 1777-1782
    • Girardin, S.E.1    Philpott, D.J.2
  • 9
    • 17944380130 scopus 로고    scopus 로고
    • Girardin, S.E., Tournebize, R., Mavris, M., Page, A.L., Li, X., Stark, G.R., et al. 2001. CARD4/Nod1 mediates NF-κB and JNK activation by invasive Shigella flexneri. EMBO Rep. 2: 736-742. doi:10.1093/embo-reports/kvel55.
    • Girardin, S.E., Tournebize, R., Mavris, M., Page, A.L., Li, X., Stark, G.R., et al. 2001. CARD4/Nod1 mediates NF-κB and JNK activation by invasive Shigella flexneri. EMBO Rep. 2: 736-742. doi:10.1093/embo-reports/kvel55.
  • 10
    • 0038615855 scopus 로고    scopus 로고
    • Nodi detects a unique muropeptide from Gram-negative bacterial peptidoglycan
    • doi:10.1126/science.1084677
    • Girardin, S.E., Boneca, I.G., Carneiro, L.A., Antignac, A., Jehanno, M., Viala, J., et al. 2003a. Nodi detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science (Washington, D.C), 300: 1584-1587. doi:10.1126/science.1084677.
    • (2003) Science (Washington, D.C) , vol.300 , pp. 1584-1587
    • Girardin, S.E.1    Boneca, I.G.2    Carneiro, L.A.3    Antignac, A.4    Jehanno, M.5    Viala, J.6
  • 12
    • 0345303939 scopus 로고    scopus 로고
    • Lessons from Nod2 studies: Towards a link between Crohn's disease and bacterial sensing
    • doi:10.1016/j.it.2003.10.007
    • Girardin, S.E., Hugot, J.P., and Sansonetti, P.J. 2003c. Lessons from Nod2 studies: towards a link between Crohn's disease and bacterial sensing. Trends Immunol. 24: 652-658. doi:10.1016/j.it.2003.10.007.
    • (2003) Trends Immunol , vol.24 , pp. 652-658
    • Girardin, S.E.1    Hugot, J.P.2    Sansonetti, P.J.3
  • 15
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
    • doi:10.1038/35079107
    • Hugot, J.-P., Chamaillard, M., Zouali, H., Lesage, S., Cezard, J.-P., Belaiche, J., et al. 2001. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature (London), 411: 599-603. doi:10.1038/35079107.
    • (2001) Nature (London) , vol.411 , pp. 599-603
    • Hugot, J.-P.1    Chamaillard, M.2    Zouali, H.3    Lesage, S.4    Cezard, J.-P.5    Belaiche, J.6
  • 16
    • 33645691172 scopus 로고    scopus 로고
    • Synthesis of peptidoglycan fragments and evaluation of their biological activity
    • doi:10.1039/b511866b
    • Inamura, S., Fujimoto, Y., Kawasaki, A., Shiokawa, Z., Woelk, E., Heine, H., et al. 2006. Synthesis of peptidoglycan fragments and evaluation of their biological activity. Org. Biomol. Chem. 4: 232-242. doi:10.1039/b511866b.
    • (2006) Org. Biomol. Chem , vol.4 , pp. 232-242
    • Inamura, S.1    Fujimoto, Y.2    Kawasaki, A.3    Shiokawa, Z.4    Woelk, E.5    Heine, H.6
  • 17
    • 0033591330 scopus 로고    scopus 로고
    • Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-κB
    • doi:10.1074/jbc.274.21.14560
    • Inohara, N., Koseki, T., del Peso, L., Hu, Y., Yee, C., Chen, S., et al. 1999. Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-κB. J. Biol. Chem. 274: 14560-14567. doi:10.1074/jbc.274.21.14560.
    • (1999) J. Biol. Chem , vol.274 , pp. 14560-14567
    • Inohara, N.1    Koseki, T.2    del Peso, L.3    Hu, Y.4    Yee, C.5    Chen, S.6
  • 18
    • 0037458665 scopus 로고    scopus 로고
    • Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease
    • doi:10.1074/jbc.C200673200
    • Inohara, N., Ogura, Y., Fontalba, A., Gutierrez, O., Pons, F., Crespo, J., et al. 2003. Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease. J. Biol. Chem. 278: 5509-5512. doi:10.1074/jbc.C200673200.
    • (2003) J. Biol. Chem , vol.278 , pp. 5509-5512
    • Inohara, N.1    Ogura, Y.2    Fontalba, A.3    Gutierrez, O.4    Pons, F.5    Crespo, J.6
  • 19
    • 0034754481 scopus 로고    scopus 로고
    • Hepatic uptake of cholecystokinin octapeptide by organic anion-transporting polypeptides OATP4 and OATP8 of rat and human liver
    • doi:10.1053/gast.2001. 28704
    • Ismair, M.G., Stieger, B., Cattori, V., Hagenbuch, B., Fried, M., Meier, P.J., and Kullak-Ublick, G.A. 2001. Hepatic uptake of cholecystokinin octapeptide by organic anion-transporting polypeptides OATP4 and OATP8 of rat and human liver. Gastroenterology, 121: 1185-1190. doi:10.1053/gast.2001. 28704.
    • (2001) Gastroenterology , vol.121 , pp. 1185-1190
    • Ismair, M.G.1    Stieger, B.2    Cattori, V.3    Hagenbuch, B.4    Fried, M.5    Meier, P.J.6    Kullak-Ublick, G.A.7
  • 20
    • 0035125407 scopus 로고    scopus 로고
    • Organic anion-transporting polypeptide B (OATP-B) and its functional comparison with three other OATPs of human liver
    • doi:10.1053/gast.2001.21176
    • Kullak-Ublick, G.A., Ismair, M.G., Stieger, B., Landmann, L., Huber, R., Pizzagalli, F., et al. 2001. Organic anion-transporting polypeptide B (OATP-B) and its functional comparison with three other OATPs of human liver. Gastroenterology, 120: 525-533. doi:10.1053/gast.2001.21176.
    • (2001) Gastroenterology , vol.120 , pp. 525-533
    • Kullak-Ublick, G.A.1    Ismair, M.G.2    Stieger, B.3    Landmann, L.4    Huber, R.5    Pizzagalli, F.6
  • 21
    • 27744522261 scopus 로고    scopus 로고
    • Selective recognition of synthetic lysine and meso-diaminopimelic acid-type peptidoglycan fragments by human peptidoglycan recognition proteins I{α} and S
    • doi:10.1074/jbc. M506385200
    • Kumar, S., Roychowdhury, A., Ember, B., Wang, Q., Guan, R., Mariuzza, R.A., and Boons, G.J. 2005. Selective recognition of synthetic lysine and meso-diaminopimelic acid-type peptidoglycan fragments by human peptidoglycan recognition proteins I{α} and S. J. Biol. Chem. 280: 37005-37012. doi:10.1074/jbc. M506385200.
    • (2005) J. Biol. Chem , vol.280 , pp. 37005-37012
    • Kumar, S.1    Roychowdhury, A.2    Ember, B.3    Wang, Q.4    Guan, R.5    Mariuzza, R.A.6    Boons, G.J.7
  • 23
    • 28544434876 scopus 로고    scopus 로고
    • Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin
    • doi:10.1038/sj.embor.7400552
    • Magalhaes, J.G., Philpott, D.J., Nahori, M.A., Jehanno, M., Fritz, J., Bourhis, L.L., et al. 2005. Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin. EMBO Rep. 6: 1201-1207. doi:10.1038/sj.embor.7400552.
    • (2005) EMBO Rep , vol.6 , pp. 1201-1207
    • Magalhaes, J.G.1    Philpott, D.J.2    Nahori, M.A.3    Jehanno, M.4    Fritz, J.5    Bourhis, L.L.6
  • 24
    • 19044388766 scopus 로고    scopus 로고
    • Structure and metabolism of peptidoglycan and molecular requirements allowing its detection by the Drosophila innate immune system
    • doi:10.1179/096805105X35233
    • Mengin-Lecreulx, D., and Lemaitre, B. 2005. Structure and metabolism of peptidoglycan and molecular requirements allowing its detection by the Drosophila innate immune system. J. Endotoxin Res. 11: 105-111. doi:10.1179/096805105X35233.
    • (2005) J. Endotoxin Res , vol.11 , pp. 105-111
    • Mengin-Lecreulx, D.1    Lemaitre, B.2
  • 25
    • 0032435805 scopus 로고    scopus 로고
    • hPepT1-mediated epithelial transport of bacteria-derived chemotactic peptides enhances neutrophil-epithelial interactions
    • Merlin, D., Steel, A., Gewirtz, A.T., Si-Tahar, M., Hediger, M.A., and Madara, J.L. 1998. hPepT1-mediated epithelial transport of bacteria-derived chemotactic peptides enhances neutrophil-epithelial interactions. J. Clin. Invest. 102: 2011-2018.
    • (1998) J. Clin. Invest , vol.102 , pp. 2011-2018
    • Merlin, D.1    Steel, A.2    Gewirtz, A.T.3    Si-Tahar, M.4    Hediger, M.A.5    Madara, J.L.6
  • 26
    • 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
    • doi:10.1053/gast.2001.24845
    • Merlin, D., Si-Tahar, M., Sitaraman, S.V., Eastburn, K., Williams, I., Liu, X., Hediger, M.A., and Madara, J.L. 2001. Colonic epithelial hPepT1 expression occurs in inflammatory bowel disease: transport of bacterial peptides influences expression of MHC class 1 molecules. Gastroenterology, 120: 1666-1679. doi:10.1053/gast.2001.24845.
    • (2001) Gastroenterology , vol.120 , pp. 1666-1679
    • Merlin, D.1    Si-Tahar, M.2    Sitaraman, S.V.3    Eastburn, K.4    Williams, I.5    Liu, X.6    Hediger, M.A.7    Madara, J.L.8
  • 28
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
    • doi:10.1038/35079114
    • Ogura, Y., Bonen, D.K., Inohara, N., Nicolae, D.L., Chen, F.F., Ramos, R., et al. 2001a. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature (London), 411: 603-606. doi:10.1038/35079114.
    • (2001) Nature (London) , vol.411 , pp. 603-606
    • Ogura, Y.1    Bonen, D.K.2    Inohara, N.3    Nicolae, D.L.4    Chen, F.F.5    Ramos, R.6
  • 29
    • 0035895992 scopus 로고    scopus 로고
    • Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-κB
    • doi:10.1074/jbc.M008072200
    • Ogura, Y., Inohara, N., Benito, A., Chen, F.F., Yamaoka, S., and Nunez, G. 2001b. Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-κB. J. Biol. Chem. 276: 4812-4818. doi:10.1074/jbc.M008072200.
    • (2001) J. Biol. Chem , vol.276 , pp. 4812-4818
    • Ogura, Y.1    Inohara, N.2    Benito, A.3    Chen, F.F.4    Yamaoka, S.5    Nunez, G.6
  • 30
    • 10344251507 scopus 로고    scopus 로고
    • Peptidoglycan molecular requirements allowing detection by the Drosophila immune deficiency pathway
    • Stenbak, C.R., Ryu, J.H., Leulier, F., Pili-Floury, S., Parquet, C., Herve, M., et al. 2004. Peptidoglycan molecular requirements allowing detection by the Drosophila immune deficiency pathway. J. Immunol. 173: 7339-7348.
    • (2004) J. Immunol , vol.173 , pp. 7339-7348
    • Stenbak, C.R.1    Ryu, J.H.2    Leulier, F.3    Pili-Floury, S.4    Parquet, C.5    Herve, M.6
  • 31
    • 7944220803 scopus 로고    scopus 로고
    • Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition
    • doi:10.1038/sj.embor.7400248
    • Travassos, L.H., Girardin, S.E., Philpott, D.J., Blanot, D., Nahori, M.A., Werts, C., and Boneca, I.G. 2004. Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition. EMBO Rep. 5: 1000-1006. doi:10.1038/sj.embor.7400248.
    • (2004) EMBO Rep , vol.5 , pp. 1000-1006
    • Travassos, L.H.1    Girardin, S.E.2    Philpott, D.J.3    Blanot, D.4    Nahori, M.A.5    Werts, C.6    Boneca, I.G.7
  • 32
    • 4944223117 scopus 로고    scopus 로고
    • Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli
    • doi:10.1128/JB.186.20.6728-6737.2004
    • Ursinus, A., van den Ent, F., Brechtel, S., de Pedro, M., Holtje, J.V., Lowe, J., and Vollmer, W. 2004. Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli. J. Bacteriol. 186: 6728-6737. doi:10.1128/JB.186.20.6728-6737.2004.
    • (2004) J. Bacteriol , vol.186 , pp. 6728-6737
    • Ursinus, A.1    van den Ent, F.2    Brechtel, S.3    de Pedro, M.4    Holtje, J.V.5    Lowe, J.6    Vollmer, W.7
  • 33
    • 7644234401 scopus 로고    scopus 로고
    • hPepT1 transports muramyl dipeptide, activating NF-kappaB and stimulating IL-8 secretion in human colonic Caco2/bbe cells
    • doi:10.1053/j.gastro.2004.07.024
    • Vavricka, S.R., Musch, M.W., Chang, J.E., Nakagawa, Y., Phanvijhitsiri, K., Waypa, T.S., et al. 2004. hPepT1 transports muramyl dipeptide, activating NF-kappaB and stimulating IL-8 secretion in human colonic Caco2/bbe cells. Gastroenterology, 127: 1401-1409. doi:10.1053/j.gastro.2004.07.024.
    • (2004) Gastroenterology , vol.127 , pp. 1401-1409
    • Vavricka, S.R.1    Musch, M.W.2    Chang, J.E.3    Nakagawa, Y.4    Phanvijhitsiri, K.5    Waypa, T.S.6
  • 35
    • 33645958613 scopus 로고    scopus 로고
    • TIR, CARD and PYRIN: Three domains for an antimicrobial triad
    • doi:10.1038/sj.cdd.4401890
    • Werts, C., Girardin, S.E., and Philpott, D.J. 2006. TIR, CARD and PYRIN: three domains for an antimicrobial triad. Cell Death Differ. 13: 798-815. doi:10.1038/sj.cdd.4401890.
    • (2006) Cell Death Differ , vol.13 , pp. 798-815
    • Werts, C.1    Girardin, S.E.2    Philpott, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.