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Volumn 105, Issue , 2015, Pages 27-33

Prevention of renal damage caused by Shiga toxin type 2: Action of Miglustat on human endothelial and epithelial cells

Author keywords

Hemolytic uremic syndrome; Human glomerular endothelial cells; Immortalized human proximal tubule epithelial cells; Miglustat; Shiga toxin type 2

Indexed keywords

CERAMIDE GLUCOSYLTRANSFERASE; MIGLUSTAT; RECEPTOR; SHIGA TOXIN RECEPTOR; UNCLASSIFIED DRUG; VEROTOXIN 2; 1 DEOXYNOJIRIMYCIN; SHIGA TOXIN;

EID: 84940996699     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2015.08.021     Document Type: Article
Times cited : (16)

References (36)
  • 2
    • 84940971833 scopus 로고    scopus 로고
    • Recent advances in the diagnosis and treatment of niemann-pick disease type C in children: A guide to early diagnosis for the general pediatrician
    • H. Alobaidy Recent advances in the diagnosis and treatment of niemann-pick disease type C in children: a guide to early diagnosis for the general pediatrician Int. J. Pediatr. 2015 2015 816593
    • (2015) Int. J. Pediatr. , vol.2015 , pp. 816593
    • Alobaidy, H.1
  • 4
    • 0033005150 scopus 로고    scopus 로고
    • Differential effects of glycolipid biosynthesis inhibitors on ceramide-induced cell death in neuroblastoma cells
    • E. Bieberich, B. Freischutz, M. Suzuki, and R.K. Yu Differential effects of glycolipid biosynthesis inhibitors on ceramide-induced cell death in neuroblastoma cells J. Neurochem. 72 1999 1040 1049
    • (1999) J. Neurochem. , vol.72 , pp. 1040-1049
    • Bieberich, E.1    Freischutz, B.2    Suzuki, M.3    Yu, R.K.4
  • 5
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • E.G. Bligh, and W.J. Dyer A rapid method of total lipid extraction and purification Can. J. Biochem. Physiol. 37 1959 911 917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 6
    • 32244445841 scopus 로고    scopus 로고
    • Cytotoxic effect of Shiga toxin-2 holotoxin and its B subunit on human renal tubular epithelial cells
    • V.P. Creydt, C. Silberstein, E. Zotta, and C. Ibarra Cytotoxic effect of Shiga toxin-2 holotoxin and its B subunit on human renal tubular epithelial cells Microbes Infect. 8 2006 410 419
    • (2006) Microbes Infect. , vol.8 , pp. 410-419
    • Creydt, V.P.1    Silberstein, C.2    Zotta, E.3    Ibarra, C.4
  • 9
    • 0022508584 scopus 로고
    • Pathogenesis of shigella diarrhea. XI. Isolation of a shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide
    • M. Jacewicz, H. Clausen, E. Nudelman, A. Donohue-Rolfe, and G.T. Keusch Pathogenesis of shigella diarrhea. XI. Isolation of a shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide J. Exp. Med. 163 1986 1391 1404
    • (1986) J. Exp. Med. , vol.163 , pp. 1391-1404
    • Jacewicz, M.1    Clausen, H.2    Nudelman, E.3    Donohue-Rolfe, A.4    Keusch, G.T.5
  • 10
    • 0021946215 scopus 로고
    • The association between idiopathic hemolytic uremic syndrome and infection by verotoxin-producing Escherichia coli
    • M.A. Karmali, M. Petric, C. Lim, P.C. Fleming, G.S. Arbus, and H. Lior The association between idiopathic hemolytic uremic syndrome and infection by verotoxin-producing Escherichia coli J. Infect. Dis. 151 1985 775 782
    • (1985) J. Infect. Dis. , vol.151 , pp. 775-782
    • Karmali, M.A.1    Petric, M.2    Lim, C.3    Fleming, P.C.4    Arbus, G.S.5    Lior, H.6
  • 11
    • 0036890775 scopus 로고    scopus 로고
    • Haemolytic uraemic syndrome and thrombotic thrombocytopenic purpura
    • D. Karpman Haemolytic uraemic syndrome and thrombotic thrombocytopenic purpura Curr. Paediatr. 12 2002 569 574
    • (2002) Curr. Paediatr. , vol.12 , pp. 569-574
    • Karpman, D.1
  • 13
    • 0037135608 scopus 로고    scopus 로고
    • Combinatorial ganglioside biosynthesis
    • T. Kolter, R.L. Proia, and K. Sandhoff Combinatorial ganglioside biosynthesis J. Biol. Chem. 277 2002 25859 25862
    • (2002) J. Biol. Chem. , vol.277 , pp. 25859-25862
    • Kolter, T.1    Proia, R.L.2    Sandhoff, K.3
  • 14
    • 84861380070 scopus 로고    scopus 로고
    • A comparison of Shiga-toxin 2 bacteriophage from classical enterohemorrhagic Escherichia coli serotypes and the German E. Coli O104:H4 outbreak strain
    • C.R. Laing, Y. Zhang, M.W. Gilmour, V. Allen, R. Johnson, J.E. Thomas, and V.P. Gannon A comparison of shiga-toxin 2 bacteriophage from classical enterohemorrhagic Escherichia coli serotypes and the German E. coli O104:H4 outbreak strain Plos One 7 2012 e37362
    • (2012) Plos One , vol.7 , pp. e37362
    • Laing, C.R.1    Zhang, Y.2    Gilmour, M.W.3    Allen, V.4    Johnson, R.5    Thomas, J.E.6    Gannon, V.P.7
  • 15
    • 0033591332 scopus 로고    scopus 로고
    • Improved inhibitors of glucosylceramide synthase
    • L. Lee, A. Abe, and J.A. Shayman Improved inhibitors of glucosylceramide synthase J. Biol. Chem. 274 1999 14662 14669
    • (1999) J. Biol. Chem. , vol.274 , pp. 14662-14669
    • Lee, L.1    Abe, A.2    Shayman, J.A.3
  • 16
    • 0029916780 scopus 로고    scopus 로고
    • Role of verotoxin receptors in pathogenesis
    • C.A. Lingwood Role of verotoxin receptors in pathogenesis Trends Microbiol. 4 1996 147 153
    • (1996) Trends Microbiol. , vol.4 , pp. 147-153
    • Lingwood, C.A.1
  • 18
    • 4844228035 scopus 로고    scopus 로고
    • A method for the isolation of glomerular and tubulointerstitial endothelial cells and a comparison of characteristics with the human umbilical vein endothelial cell model
    • S. McGinn, P. Poronnik, E.D. Gallery, and C.A. Pollock A method for the isolation of glomerular and tubulointerstitial endothelial cells and a comparison of characteristics with the human umbilical vein endothelial cell model Nephrology (Carlton) 9 2004 229 237
    • (2004) Nephrology (Carlton) , vol.9 , pp. 229-237
    • McGinn, S.1    Poronnik, P.2    Gallery, E.D.3    Pollock, C.A.4
  • 19
    • 24644519117 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate suppresses galactose-alpha1,4-galactose-1beta,4-glucose ceramide expression in TNF-alpha stimulated human intestinal epithelial cells through inhibition of MAPKs and NF-kappaB
    • D.O. Moon, S.R. Choi, C.M. Lee, G.Y. Kim, H.J. Lee, and Y.M. Park Epigallocatechin-3-gallate suppresses galactose-alpha1,4-galactose-1beta,4-glucose ceramide expression in TNF-alpha stimulated human intestinal epithelial cells through inhibition of MAPKs and NF-kappaB J. Korean Med. Sci. 20 2005 548 554
    • (2005) J. Korean Med. Sci. , vol.20 , pp. 548-554
    • Moon, D.O.1    Choi, S.R.2    Lee, C.M.3    Kim, G.Y.4    Lee, H.J.5    Park, Y.M.6
  • 20
    • 33745685704 scopus 로고    scopus 로고
    • Curcumin decreases binding of Shiga-like toxin-1B on human intestinal epithelial cell line HT29 stimulated with TNF-alpha and IL-1beta: Suppression of p38, JNK and NF-kappaB p65 as potential targets
    • D.O. Moon, C.Y. Jin, J.D. Lee, Y.H. Choi, S.C. Ahn, C.M. Lee, S.C. Jeong, Y.M. Park, and G.Y. Kim Curcumin decreases binding of Shiga-like toxin-1B on human intestinal epithelial cell line HT29 stimulated with TNF-alpha and IL-1beta: suppression of p38, JNK and NF-kappaB p65 as potential targets Biol. Pharm. Bull. 29 2006 1470 1475
    • (2006) Biol. Pharm. Bull. , vol.29 , pp. 1470-1475
    • Moon, D.O.1    Jin, C.Y.2    Lee, J.D.3    Choi, Y.H.4    Ahn, S.C.5    Lee, C.M.6    Jeong, S.C.7    Park, Y.M.8    Kim, G.Y.9
  • 21
    • 79952087639 scopus 로고    scopus 로고
    • Escherichia coli Shiga toxin mechanisms of action in renal disease
    • T.G. Obrig Escherichia coli shiga toxin mechanisms of action in renal disease Toxins (Basel) 2 2010 2769 2794
    • (2010) Toxins (Basel) , vol.2 , pp. 2769-2794
    • Obrig, T.G.1
  • 23
    • 0026605452 scopus 로고
    • Binding of verocytotoxin 1 to its receptor is influenced by differences in receptor fatty acid content
    • A. Pellizzari, H. Pang, and C.A. Lingwood Binding of verocytotoxin 1 to its receptor is influenced by differences in receptor fatty acid content Biochemistry 31 1992 1363 1370
    • (1992) Biochemistry , vol.31 , pp. 1363-1370
    • Pellizzari, A.1    Pang, H.2    Lingwood, C.A.3
  • 25
    • 0028176432 scopus 로고
    • N-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis
    • F.M. Platt, G.R. Neises, R.A. Dwek, and T.D. Butters N-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis J. Biol. Chem. 269 1994 8362 8365
    • (1994) J. Biol. Chem. , vol.269 , pp. 8362-8365
    • Platt, F.M.1    Neises, G.R.2    Dwek, R.A.3    Butters, T.D.4
  • 26
    • 0030814767 scopus 로고    scopus 로고
    • Extensive glycosphingolipid depletion in the liver and lymphoid organs of mice treated with N-butyldeoxynojirimycin
    • F.M. Platt, G. Reinkensmeier, R.A. Dwek, and T.D. Butters Extensive glycosphingolipid depletion in the liver and lymphoid organs of mice treated with N-butyldeoxynojirimycin J. Biol. Chem. 272 1997 19365 19372
    • (1997) J. Biol. Chem. , vol.272 , pp. 19365-19372
    • Platt, F.M.1    Reinkensmeier, G.2    Dwek, R.A.3    Butters, T.D.4
  • 28
    • 0031463774 scopus 로고    scopus 로고
    • Epidemic hemolytic-uremic syndrome in children
    • H.A. Repetto Epidemic hemolytic-uremic syndrome in children Kidney Int. 52 1997 1708 1719
    • (1997) Kidney Int. , vol.52 , pp. 1708-1719
    • Repetto, H.A.1
  • 29
    • 33845775695 scopus 로고    scopus 로고
    • The epidemiology of hemolytic uremic syndrome in Argentina. Diagnosis of the etiologic agent, reservoirs and routes of transmission
    • M. Rivas, E. Miliwebsky, I. Chinen, N. Deza, and G.A. Leotta The epidemiology of hemolytic uremic syndrome in Argentina. Diagnosis of the etiologic agent, reservoirs and routes of transmission Medicina (B Aires) 66 Suppl. l3 2006 27 32
    • (2006) Medicina (B Aires) , vol.66 , pp. 27-32
    • Rivas, M.1    Miliwebsky, E.2    Chinen, I.3    Deza, N.4    Leotta, G.A.5
  • 31
    • 0028352977 scopus 로고
    • Retrograde transport from the Golgi complex to the ER of both Shiga toxin and the nontoxic Shiga B-fragment is regulated by butyric acid and cAMP
    • K. Sandvig, M. Ryd, O. Garred, E. Schweda, P.K. Holm, and B. van Deurs Retrograde transport from the Golgi complex to the ER of both Shiga toxin and the nontoxic Shiga B-fragment is regulated by butyric acid and cAMP J. Cell. Biol. 126 1994 53 64
    • (1994) J. Cell. Biol. , vol.126 , pp. 53-64
    • Sandvig, K.1    Ryd, M.2    Garred, O.3    Schweda, E.4    Holm, P.K.5    Van Deurs, B.6
  • 32
    • 70350663882 scopus 로고    scopus 로고
    • A glucosylceramide synthase inhibitor prevents the cytotoxic effects of Shiga toxin-2 on human renal tubular epithelial cells
    • C.D. Silbertsein C, W.L. Chiang, H.A. Repetto, and C. Ibarra A glucosylceramide synthase inhibitor prevents the cytotoxic effects of shiga toxin-2 on human renal tubular epithelial cells J. Epithel. Biol. Pharmacol. 1 2008 71 75
    • (2008) J. Epithel. Biol. Pharmacol. , vol.1 , pp. 71-75
    • Silbertsein, C.C.D.1    Chiang, W.L.2    Repetto, H.A.3    Ibarra, C.4
  • 33
    • 15244348050 scopus 로고    scopus 로고
    • Shiga-toxin-producing Escherichia coli and haemolytic uraemic syndrome
    • P.I. Tarr, C.A. Gordon, and W.L. Chandler Shiga-toxin-producing Escherichia coli and haemolytic uraemic syndrome Lancet 365 2005 1073 1086
    • (2005) Lancet , vol.365 , pp. 1073-1086
    • Tarr, P.I.1    Gordon, C.A.2    Chandler, W.L.3
  • 34
    • 83655201339 scopus 로고    scopus 로고
    • Activation of cell stress response pathways by Shiga toxins
    • V.L. Tesh Activation of cell stress response pathways by Shiga toxins Cell Microbiol. 14 2012 1 9
    • (2012) Cell Microbiol. , vol.14 , pp. 1-9
    • Tesh, V.L.1
  • 35
    • 33947314170 scopus 로고    scopus 로고
    • The pharmacokinetics and tissue distribution of the glucosylceramide synthase inhibitor miglustat in the rat
    • A. Treiber, O. Morand, and M. Clozel The pharmacokinetics and tissue distribution of the glucosylceramide synthase inhibitor miglustat in the rat Xenobiotica 37 2007 298 314
    • (2007) Xenobiotica , vol.37 , pp. 298-314
    • Treiber, A.1    Morand, O.2    Clozel, M.3
  • 36
    • 34248228704 scopus 로고    scopus 로고
    • Inhibiting glycosphingolipid synthesis improves glycemic control and insulin sensitivity in animal models of type 2 diabetes
    • H. Zhao, M. Przybylska, I.H. Wu, J. Zhang, C. Siegel, S. Komarnitsky, N.S. Yew, and S.H. Cheng Inhibiting glycosphingolipid synthesis improves glycemic control and insulin sensitivity in animal models of type 2 diabetes Diabetes 56 2007 1210 1218
    • (2007) Diabetes , vol.56 , pp. 1210-1218
    • Zhao, H.1    Przybylska, M.2    Wu, I.H.3    Zhang, J.4    Siegel, C.5    Komarnitsky, S.6    Yew, N.S.7    Cheng, S.H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.