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Volumn 79, Issue 4, 2011, Pages 1623-1630

Primary human colonic myofibroblasts are resistant to Clostridium difficile toxin A-induced, but not toxin B-induced, cell death

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SMOOTH MUSCLE ACTIN; CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; RAC1 PROTEIN;

EID: 79953322027     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00686-10     Document Type: Article
Times cited : (9)

References (46)
  • 1
    • 0030719443 scopus 로고    scopus 로고
    • Keratinocyte growth factor in inflammatory bowel disease. Increased mRNA transcripts in ulcerative colitis compared with Crohn's disease in biopsies and isolated mucosal myofibroblasts
    • Bajaj-Elliott, M., E. Breese, R. Poulsom, P. D. Fairclough, and T. T. Mac-Donald. 1997. Keratinocyte growth factor in inflammatory bowel disease. Increased mRNA transcripts in ulcerative colitis compared with Crohn's disease in biopsies and isolated mucosal myofibroblasts. Am. J. Pathol. 151:1469-1476.
    • (1997) Am. J. Pathol. , vol.151 , pp. 1469-1476
    • Bajaj-Elliott, M.1    Breese, E.2    Poulsom, R.3    Fairclough, P.D.4    Mac-Donald, T.T.5
  • 3
    • 0032857965 scopus 로고    scopus 로고
    • Human colonic subepithelial myofibroblasts modulate transepithelial resistance and secretory response
    • Beltinger, J., et al. 1999. Human colonic subepithelial myofibroblasts modulate transepithelial resistance and secretory response. Am. J. Physiol. 277: C271-C279.
    • (1999) Am. J. Physiol. , vol.277
    • Beltinger, J.1
  • 4
    • 0030730632 scopus 로고    scopus 로고
    • Inactivation of the small GTPase Rho disrupts cellular attachment and induces adhesion-dependent and adhesion-independent apoptosis
    • Bobak, D., J. Moorman, A. Guanzon, L. Gilmer, and C. Hahn. 1997. Inactivation of the small GTPase Rho disrupts cellular attachment and induces adhesion-dependent and adhesion-independent apoptosis. Oncogene 15:2179-2189.
    • (1997) Oncogene , vol.15 , pp. 2179-2189
    • Bobak, D.1    Moorman, J.2    Guanzon, A.3    Gilmer, L.4    Hahn, C.5
  • 5
    • 0030909985 scopus 로고    scopus 로고
    • Early functional effects of Clostridium difficile toxin A on human colonocytes
    • Branka, J. E., et al. 1997. Early functional effects of Clostridium difficile toxin A on human colonocytes. Gastroenterology 112:1887-1894.
    • (1997) Gastroenterology , vol.112 , pp. 1887-1894
    • Branka, J.E.1
  • 6
    • 0037111088 scopus 로고    scopus 로고
    • Mechanism of Clostridium difficile toxin A-induced apoptosis in T84 cells
    • Brito, G. A., et al. 2002. Mechanism of Clostridium difficile toxin A-induced apoptosis in T84 cells. J. Infect. Dis. 186:1438-1447.
    • (2002) J. Infect. Dis. , vol.186 , pp. 1438-1447
    • Brito, G.A.1
  • 7
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K., and K. Wennerberg. 2004. Rho and Rac take center stage. Cell 116:167-179.
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 8
    • 0028987414 scopus 로고
    • Involvement of Ras-related Rho proteins in the mechanisms of action of Clostridium difficile toxin A and toxin B
    • Dillon, S. T., et al. 1995. Involvement of Ras-related Rho proteins in the mechanisms of action of Clostridium difficile toxin A and toxin B. Infect. Immun. 63:1421-1426.
    • (1995) Infect. Immun. , vol.63 , pp. 1421-1426
    • Dillon, S.T.1
  • 9
    • 66649106333 scopus 로고    scopus 로고
    • Transforming growth factor beta signalling and matrix metalloproteinases in the mucosa overlying Crohn's disease strictures
    • Di Sabatino, A., et al. 2009. Transforming growth factor beta signalling and matrix metalloproteinases in the mucosa overlying Crohn's disease strictures. Gut 58:777-789.
    • (2009) Gut , vol.58 , pp. 777-789
    • Di Sabatino, A.1
  • 10
    • 0025367873 scopus 로고
    • Interaction of Clostridium difficile toxin A with cultured cells: cytoskeletal changes and nuclear polarization
    • Fiorentini, C., et al. 1990. Interaction of Clostridium difficile toxin A with cultured cells: cytoskeletal changes and nuclear polarization. Infect. Immun. 58:2329-2336.
    • (1990) Infect. Immun. , vol.58 , pp. 2329-2336
    • Fiorentini, C.1
  • 11
    • 33646942752 scopus 로고    scopus 로고
    • Cellular stability of Rho-GTPases glucosylated by Clostridium difficile toxin B
    • Genth, H., et al. 2006. Cellular stability of Rho-GTPases glucosylated by Clostridium difficile toxin B. FEBS Lett. 580:3565-3569.
    • (2006) FEBS Lett , vol.580 , pp. 3565-3569
    • Genth, H.1
  • 12
    • 0036088374 scopus 로고    scopus 로고
    • IL-17 stimulates inflammatory responses via NFkappaB and MAP kinase pathways in human colonic myofibroblasts
    • Hata, K., et al. 2002. IL-17 stimulates inflammatory responses via NFkappaB and MAP kinase pathways in human colonic myofibroblasts. Am. J. Physiol. Gastrointest. Liver Physiol. 282:G1035-G1044.
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.282
    • Hata, K.1
  • 13
    • 0036207579 scopus 로고    scopus 로고
    • Clostridium difficile toxin A triggers human colonocyte IL-8 release via mitochondrial oxygen radical generation
    • He, D., et al. 2002. Clostridium difficile toxin A triggers human colonocyte IL-8 release via mitochondrial oxygen radical generation. Gastroenterology 122:1048-1057.
    • (2002) Gastroenterology , vol.122 , pp. 1048-1057
    • He, D.1
  • 14
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman, S. J., and A. J. Ridley. 2008. Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat. Rev. Mol. Cell. Biol. 9:690-701.
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 15
    • 0024204607 scopus 로고
    • Clostridium difficile toxin A perturbs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers
    • Hecht, G., C. Pothoulakis, J. T. LaMont, and J. L. Madara. 1988. Clostridium difficile toxin A perturbs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers. J. Clin. Invest. 82: 1516-1524.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1516-1524
    • Hecht, G.1    Pothoulakis, C.2    LaMont, J.T.3    Madara, J.L.4
  • 16
    • 0036784378 scopus 로고    scopus 로고
    • Rho protein inactivation induced apoptosis of cultured human endothelial cells
    • Hippenstiel, S., et al. 2002. Rho protein inactivation induced apoptosis of cultured human endothelial cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 283:L830-L838.
    • (2002) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.283
    • Hippenstiel, S.1
  • 17
    • 33846807241 scopus 로고    scopus 로고
    • Difference in the cytotoxic effects of toxin B from Clostridium difficile strain VPI 10463 and toxin B from variant Clostridium difficile strain 1470
    • Huelsenbeck, J., et al. 2007. Difference in the cytotoxic effects of toxin B from Clostridium difficile strain VPI 10463 and toxin B from variant Clostridium difficile strain 1470. Infect. Immun. 75:801-809.
    • (2007) Infect. Immun. , vol.75 , pp. 801-809
    • Huelsenbeck, J.1
  • 18
    • 78650077745 scopus 로고    scopus 로고
    • Expression profiling of Wnt family of genes in normal and inflammatory bowel disease primary human intestinal myofibroblasts and normal human colonic crypt epithelial cells
    • Hughes, K. R., F. Sablitzky, and Y. R. Mahida. 2011. Expression profiling of Wnt family of genes in normal and inflammatory bowel disease primary human intestinal myofibroblasts and normal human colonic crypt epithelial cells. Inflamm. Bowel Dis. 17:213-220.
    • (2011) Inflamm. Bowel Dis. , vol.17 , pp. 213-220
    • Hughes, K.R.1    Sablitzky, F.2    Mahida, Y.R.3
  • 19
    • 33947260554 scopus 로고    scopus 로고
    • Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function
    • Jank, T., T. Giesemann, and K. Aktories. 2007. Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function. Glycobiology 17:15R-22R.
    • (2007) Glycobiology , vol.17
    • Jank, T.1    Giesemann, T.2    Aktories, K.3
  • 20
    • 2542486247 scopus 로고    scopus 로고
    • Differential effects of varying concentrations of Clostridium difficile toxin A on epithelial barrier function and expression of cytokines
    • Johal, S. S., K. Solomon, S. Dodson, S. P. Borriello, and Y. R. Mahida. 2004. Differential effects of varying concentrations of Clostridium difficile toxin A on epithelial barrier function and expression of cytokines. J. Infect. Dis. 189:2110-2119.
    • (2004) J. Infect. Dis. , vol.189 , pp. 2110-2119
    • Johal, S.S.1    Solomon, K.2    Dodson, S.3    Borriello, S.P.4    Mahida, Y.R.5
  • 21
    • 0024440715 scopus 로고
    • Purification and characterisation of Clostridium difficile toxin A by bovine thyroglobulin affinity chromatography and dissociation in denaturing conditions with or without reduction
    • Kamiya, S., P. J. Reed, and S. P. Borriello. 1989. Purification and characterisation of Clostridium difficile toxin A by bovine thyroglobulin affinity chromatography and dissociation in denaturing conditions with or without reduction. J. Med. Microbiol. 30:69-77.
    • (1989) J. Med. Microbiol. , vol.30 , pp. 69-77
    • Kamiya, S.1    Reed, P.J.2    Borriello, S.P.3
  • 22
    • 0242490282 scopus 로고    scopus 로고
    • Reduced migration of fibroblasts in inflammatory bowel disease: role of inflammatory mediators and focal adhesion kinase
    • Leeb, S. N., et al. 2003. Reduced migration of fibroblasts in inflammatory bowel disease: role of inflammatory mediators and focal adhesion kinase. Gastroenterology 125:1341-1354.
    • (2003) Gastroenterology , vol.125 , pp. 1341-1354
    • Leeb, S.N.1
  • 23
    • 0022460391 scopus 로고
    • Characterization of toxins A and B of Clostridium difficile with monoclonal antibodies
    • Lyerly, D. M., C. J. Phelps, J. Toth, and T. D. Wilkins. 1986. Characterization of toxins A and B of Clostridium difficile with monoclonal antibodies. Infect. Immun. 54:70-76.
    • (1986) Infect. Immun. , vol.54 , pp. 70-76
    • Lyerly, D.M.1    Phelps, C.J.2    Toth, J.3    Wilkins, T.D.4
  • 24
    • 0031408125 scopus 로고    scopus 로고
    • Adult human colonic subepithelial myofibroblasts express extracellular matrix proteins and cyclooxygenase-1 and -2
    • Mahida, Y. R., et al. 1997. Adult human colonic subepithelial myofibroblasts express extracellular matrix proteins and cyclooxygenase-1 and -2. Am. J. Physiol. 273:G1341-G1348.
    • (1997) Am. J. Physiol. , vol.273
    • Mahida, Y.R.1
  • 25
    • 0032425435 scopus 로고    scopus 로고
    • Effect of Clostridium difficile toxin A on human colonic lamina propria cells: early loss of macrophages followed by T-cell apoptosis
    • Mahida, Y. R., et al. 1998. Effect of Clostridium difficile toxin A on human colonic lamina propria cells: early loss of macrophages followed by T-cell apoptosis. Infect. Immun. 66:5462-5469.
    • (1998) Infect. Immun. , vol.66 , pp. 5462-5469
    • Mahida, Y.R.1
  • 26
    • 0029868433 scopus 로고    scopus 로고
    • Effect of Clostridium difficile toxin A on human intestinal epithelial cells: induction of interleukin 8 production and apoptosis after cell detachment
    • Mahida, Y. R., S. Makh, S. Hyde, T. Gray, and S. P. Borriello. 1996. Effect of Clostridium difficile toxin A on human intestinal epithelial cells: induction of interleukin 8 production and apoptosis after cell detachment. Gut 38:337-347.
    • (1996) Gut , vol.38 , pp. 337-347
    • Mahida, Y.R.1    Makh, S.2    Hyde, S.3    Gray, T.4    Borriello, S.P.5
  • 27
    • 0036073299 scopus 로고    scopus 로고
    • Differential expression of TGF-beta isoforms by normal and inflammatory bowel disease intestinal myofibroblasts
    • McKaig, B. C., K. Hughes, P. J. Tighe, and Y. R. Mahida. 2002. Differential expression of TGF-beta isoforms by normal and inflammatory bowel disease intestinal myofibroblasts. Am. J. Physiol. Cell Physiol. 282:C172-C182.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • McKaig, B.C.1    Hughes, K.2    Tighe, P.J.3    Mahida, Y.R.4
  • 28
    • 0033049460 scopus 로고    scopus 로고
    • Normal human colonic subepithelial myofibroblasts enhance epithelial migration (restitution) via TGF-beta3
    • McKaig, B. C., S. S. Makh, C. J. Hawkey, D. K. Podolsky, and Y. R. Mahida. 1999. Normal human colonic subepithelial myofibroblasts enhance epithelial migration (restitution) via TGF-beta3. Am. J. Physiol. 276:G1087-G1093.
    • (1999) Am. J. Physiol. , vol.276
    • McKaig, B.C.1    Makh, S.S.2    Hawkey, C.J.3    Podolsky, D.K.4    Mahida, Y.R.5
  • 29
    • 0345237913 scopus 로고    scopus 로고
    • Expression and regulation of tissue inhibitor of metalloproteinase-1 and matrix metalloproteinases by intestinal myofibroblasts in inflammatory bowel disease
    • McKaig, B. C., D. McWilliams, S. A. Watson, and Y. R. Mahida. 2003. Expression and regulation of tissue inhibitor of metalloproteinase-1 and matrix metalloproteinases by intestinal myofibroblasts in inflammatory bowel disease. Am. J. Pathol. 162:1355-1360.
    • (2003) Am. J. Pathol. , vol.162 , pp. 1355-1360
    • McKaig, B.C.1    McWilliams, D.2    Watson, S.A.3    Mahida, Y.R.4
  • 30
    • 0023923499 scopus 로고
    • Purification and characterization of toxin B from Clostridium difficile
    • Meador, J., III, and R. K. Tweten. 1988. Purification and characterization of toxin B from Clostridium difficile. Infect. Immun. 56:1708-1714.
    • (1988) Infect. Immun. , vol.56 , pp. 1708-1714
    • Meador III, J.1    Tweten, R.K.2
  • 31
    • 0024426122 scopus 로고
    • Villus contraction aids repair of intestinal epithelium after injury
    • Moore, R., S. Carlson, and J. L. Madara. 1989. Villus contraction aids repair of intestinal epithelium after injury. Am. J. Physiol. 257:G274-G283.
    • (1989) Am. J. Physiol. , vol.257
    • Moore, R.1    Carlson, S.2    Madara, J.L.3
  • 32
    • 0029991647 scopus 로고    scopus 로고
    • Inactivation of the small GTP binding protein Rho induces multinucleate cell formation and apoptosis in murine T lymphoma EL4
    • Moorman, J. P., D. A. Bobak, and C. S. Hahn. 1996. Inactivation of the small GTP binding protein Rho induces multinucleate cell formation and apoptosis in murine T lymphoma EL4. J. Immunol. 156:4146-4153.
    • (1996) J. Immunol. , vol.156 , pp. 4146-4153
    • Moorman, J.P.1    Bobak, D.A.2    Hahn, C.S.3
  • 33
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann, T. 1983. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65:55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 34
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti, I., G. Migliorati, M. C. Pagliacci, F. Grignani, and C. Riccardi. 1991. A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J. Immunol. Methods 139: 271-279.
    • (1991) J. Immunol. Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 35
    • 0022618287 scopus 로고
    • Purification and properties of Clostridium difficile cytotoxin B
    • Pothoulakis, C., et al. 1986. Purification and properties of Clostridium difficile cytotoxin B. J. Biol. Chem. 261:1316-1321.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1316-1321
    • Pothoulakis, C.1
  • 36
    • 0032782848 scopus 로고    scopus 로고
    • Myofibroblasts. I. Paracrine cells important in health and disease
    • Powell, D. W., et al. 1999. Myofibroblasts. I. Paracrine cells important in health and disease. Am. J. Physiol. 277:C1-C9.
    • (1999) Am. J. Physiol. , vol.277
    • Powell, D.W.1
  • 37
    • 0032833987 scopus 로고    scopus 로고
    • Myofibroblasts. II. Intestinal subepithelial myofibroblasts
    • Powell, D. W., et al. 1999. Myofibroblasts. II. Intestinal subepithelial myofibroblasts. Am. J. Physiol. 277:C183-C201.
    • (1999) Am. J. Physiol. , vol.277
    • Powell, D.W.1
  • 39
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 40
    • 0026654125 scopus 로고
    • The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., H. F. Paterson, C. L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 41
    • 0028935286 scopus 로고
    • Clostridium difficile toxin B is more potent than toxin A in damaging human colonic epithelium in vitro
    • Riegler, M., et al. 1995. Clostridium difficile toxin B is more potent than toxin A in damaging human colonic epithelium in vitro. J. Clin. Invest. 95:2004-2011.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2004-2011
    • Riegler, M.1
  • 42
    • 15544364759 scopus 로고    scopus 로고
    • Monocytes are highly sensitive to Clostridium difficile toxin A-induced apoptotic and nonapoptotic cell death
    • Solomon, K., J. Webb, N. Ali, R. A. Robins, and Y. R. Mahida. 2005. Monocytes are highly sensitive to Clostridium difficile toxin A-induced apoptotic and nonapoptotic cell death. Infect. Immun. 73:1625-1634.
    • (2005) Infect. Immun. , vol.73 , pp. 1625-1634
    • Solomon, K.1    Webb, J.2    Ali, N.3    Robins, R.A.4    Mahida, Y.R.5
  • 43
    • 0034651952 scopus 로고    scopus 로고
    • Polymeric IgA is superior to monomeric IgA and IgG carrying the same variable domain in preventing Clostridium difficile toxin A damaging of T84 monolayers
    • Stubbe, H., J. Berdoz, J. P. Kraehenbuhl, and B. Corthesy. 2000. Polymeric IgA is superior to monomeric IgA and IgG carrying the same variable domain in preventing Clostridium difficile toxin A damaging of T84 monolayers. J. Immunol. 164:1952-1960.
    • (2000) J. Immunol. , vol.164 , pp. 1952-1960
    • Stubbe, H.1    Berdoz, J.2    Kraehenbuhl, J.P.3    Corthesy, B.4
  • 44
    • 0020003645 scopus 로고
    • Purification and characterization of toxins A and B of Clostridium difficile
    • Sullivan, N. M., S. Pellett, and T. D. Wilkins. 1982. Purification and characterization of toxins A and B of Clostridium difficile. Infect. Immun. 35: 1032-1040.
    • (1982) Infect. Immun. , vol.35 , pp. 1032-1040
    • Sullivan, N.M.1    Pellett, S.2    Wilkins, T.D.3
  • 45
    • 49649103133 scopus 로고    scopus 로고
    • Essential role of toxin A in C. difficile 027 and reference strain supernatant-mediated disruption of Caco-2 intestinal epithelial barrier function
    • Sutton, P. A., et al. 2008. Essential role of toxin A in C. difficile 027 and reference strain supernatant-mediated disruption of Caco-2 intestinal epithelial barrier function. Clin. Exp. Immunol. 153:439-447.
    • (2008) Clin. Exp. Immunol. , vol.153 , pp. 439-447
    • Sutton, P.A.1
  • 46
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: mechanism of action and role in disease
    • Voth, D. E., and J. D. Ballard. 2005. Clostridium difficile toxins: mechanism of action and role in disease. Clin. Microbiol. Rev. 18:247-263.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2


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