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Volumn 6, Issue 1, 2010, Pages 87-95

Toxicoproteomic analysis of phalloidin-induced cholestasis in mouse liver

Author keywords

Cholestasis; Hepatotoxicity; HSP90 ; Phalloidin; Proteomics

Indexed keywords


EID: 77956778648     PISSN: 1738642X     EISSN: 20928467     Source Type: Journal    
DOI: 10.1007/s13273-010-0012-7     Document Type: Article
Times cited : (3)

References (35)
  • 1
    • 0031024468 scopus 로고    scopus 로고
    • The biochemical studies on phalloidin- induced cholestasis in rats
    • Ishizaki, K.et al.The biochemical studies on phalloidin- induced cholestasis in rats.Toxicol Lett 90:29-34 (1997).
    • (1997) Toxicol Lett , vol.90 , pp. 29-34
    • Ishizaki, K.1
  • 2
    • 0016698833 scopus 로고
    • Interaction of actin with phalloidin: Polymerization and stabilization of F-actin
    • Dancker, P., Low, I., Hasselbach, W. & Wieland, T.Interaction of actin with phalloidin: polymerization and stabilization of F-actin.Biochim Biophys Acta 400:407-414 (1975).
    • (1975) Biochim Biophys Acta , vol.400 , pp. 407-414
    • Dancker, P.1    Low, I.2    Hasselbach, W.3    Wieland, T.4
  • 3
    • 0018944339 scopus 로고
    • Influence of colchicine and phalloidin on bile secretion and hepatic ultrastructure in the rat.Possible interaction between microtubules and microfilaments
    • Dubin, M., Maurice, M., Feldmann, G. & Erlinger, S.Influence of colchicine and phalloidin on bile secretion and hepatic ultrastructure in the rat.Possible interaction between microtubules and microfilaments. Gastroenterology 79:646-654 (1980).
    • (1980) Gastroenterology , vol.79 , pp. 646-654
    • Dubin, M.1    Maurice, M.2    Feldmann, G.3    Erlinger, S.4
  • 4
    • 0018879931 scopus 로고
    • Phalloidin- induced cholestasis: A microfilament-mediated change in junctional complex permeability
    • Elias, E., Hruban, Z., Wade, J.B. & Boyer, J.L.Phalloidin- induced cholestasis: a microfilament-mediated change in junctional complex permeability.Proc Natl Acad Sci USA 77:2229-2233 (1980).
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2229-2233
    • Elias, E.1    Hruban, Z.2    Wade, J.B.3    Boyer, J.L.4
  • 5
    • 0020323915 scopus 로고
    • Phalloidin-induced morphological and functional changes of rat liver
    • Vonk, R.J., Yousef, I.M., Corriveau, J.P. & Tuchweber, B.Phalloidin-induced morphological and functional changes of rat liver.Liver 2:133-140 (1982).
    • (1982) Liver , vol.2 , pp. 133-140
    • Vonk, R.J.1    Yousef, I.M.2    Corriveau, J.P.3    Tuchweber, B.4
  • 6
    • 0020622063 scopus 로고
    • Phalloidin alters bile canalicular contractility in primary monolayer cultures of rat liver
    • Watanabe, S., Miyairi, M., Oshio, C., Smith, C.R. & Phillips, M.J.Phalloidin alters bile canalicular contractility in primary monolayer cultures of rat liver.Gastroenterology 85:245-253 (1983).
    • (1983) Gastroenterology , vol.85 , pp. 245-253
    • Watanabe, S.1    Miyairi, M.2    Oshio, C.3    Smith, C.R.4    Phillips, M.J.5
  • 7
    • 0023882264 scopus 로고
    • The transport of bile acids in liver cells
    • Frimmer, M. & Ziegler, K.The transport of bile acids in liver cells.Biochim Biophys Acta 947:75-99 (1988).
    • (1988) Biochim Biophys Acta , vol.947 , pp. 75-99
    • Frimmer, M.1    Ziegler, K.2
  • 8
    • 0026581884 scopus 로고
    • Effects of mushroom toxins on glycogenolysis; comparison of toxicity of phalloidin, alphaamanitin and DL-propargylglycine in isolated rat hepatocytes
    • Kawaji, A.et al.Effects of mushroom toxins on glycogenolysis; comparison of toxicity of phalloidin, alphaamanitin and DL-propargylglycine in isolated rat hepatocytes.J Pharmacobiodyn 15:107-112 (1992).
    • (1992) J Pharmacobiodyn , vol.15 , pp. 107-112
    • Kawaji, A.1
  • 9
    • 0034109482 scopus 로고    scopus 로고
    • Role of glutathione and oxidative stress in phalloidin-induced cholestasis
    • Bouchard, G., Yousef, I.M., Barriault, C. & Tuchweber, B.Role of glutathione and oxidative stress in phalloidin-induced cholestasis.J Hepatol 32:550-560 (2000).
    • (2000) J Hepatol , vol.32 , pp. 550-560
    • Bouchard, G.1    Yousef, I.M.2    Barriault, C.3    Tuchweber, B.4
  • 10
    • 34250340796 scopus 로고    scopus 로고
    • Effects of phalloidin on hepatic gene expression in mice
    • Lim, J.S.et al.Effects of phalloidin on hepatic gene expression in mice.Int J Toxicol 26:213-220 (2007).
    • (2007) Int J Toxicol , vol.26 , pp. 213-220
    • Lim, J.S.1
  • 11
    • 8544277251 scopus 로고    scopus 로고
    • Toxicoproteomics: Proteomics applied to toxicology and pathology
    • Wetmore, B.A. & Merrick, B.A.Toxicoproteomics: proteomics applied to toxicology and pathology.Toxicol Pathol 32:619-642 (2004).
    • (2004) Toxicol Pathol , vol.32 , pp. 619-642
    • Wetmore, B.A.1    Merrick, B.A.2
  • 12
    • 33644864832 scopus 로고    scopus 로고
    • Investigation of proteomic biomarkers in in vivo hepatotoxicity study of rat liver: Toxicity differentiation in hepatotoxicants
    • Yamamoto, T., Kikkawa, R., Yamada, H. & Horii, I.Investigation of proteomic biomarkers in in vivo hepatotoxicity study of rat liver: toxicity differentiation in hepatotoxicants.J Toxicol Sci 31:49-60 (2006).
    • (2006) J Toxicol Sci , vol.31 , pp. 49-60
    • Yamamoto, T.1    Kikkawa, R.2    Yamada, H.3    Horii, I.4
  • 13
    • 0036169110 scopus 로고    scopus 로고
    • Plakins: A family of versatile cytolinker proteins
    • Leung, C.L., Green, K.J. & Liem, R.K.Plakins: a family of versatile cytolinker proteins.Trends Cell Biol 12:37-45 (2002).
    • (2002) Trends Cell Biol , vol.12 , pp. 37-45
    • Leung, C.L.1    Green, K.J.2    Liem, R.K.3
  • 14
    • 0033552634 scopus 로고    scopus 로고
    • Microtubule actin cross-linking factor (MACF): A hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons
    • Leung, C.L., Sun, D., Zheng, M., Knowles, D.R. & Liem, R.K.Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons.J Cell Biol 147:1275-1286 (1999).
    • (1999) J Cell Biol , vol.147 , pp. 1275-1286
    • Leung, C.L.1    Sun, D.2    Zheng, M.3    Knowles, D.R.4    Liem, R.K.5
  • 15
    • 0344845405 scopus 로고    scopus 로고
    • ACF7: An essential integrator of microtubule dynamics
    • Kodama, A., Karakesisoglou, I., Wong, E., Vaezi, A. & Fuchs, E.ACF7: an essential integrator of microtubule dynamics.Cell 115:343-354 (2003).
    • (2003) Cell , vol.115 , pp. 343-354
    • Kodama, A.1    Karakesisoglou, I.2    Wong, E.3    Vaezi, A.4    Fuchs, E.5
  • 16
    • 0036151839 scopus 로고    scopus 로고
    • Keratins: Guardians of the liver
    • Omary, M.B., Ku, N.O. & Toivola, D.M.Keratins: guardians of the liver.Hepatology 35:251-257 (2002).
    • (2002) Hepatology , vol.35 , pp. 251-257
    • Omary, M.B.1    Ku, N.O.2    Toivola, D.M.3
  • 17
    • 0037282536 scopus 로고    scopus 로고
    • Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation
    • Herrmann, H., Hesse, M., Reichenzeller, M., Aebi, U. & Magin, T.M.Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation.Int Rev Cytol 223:83-175 (2003).
    • (2003) Int Rev Cytol , vol.223 , pp. 83-175
    • Herrmann, H.1    Hesse, M.2    Reichenzeller, M.3    Aebi, U.4    Magin, T.M.5
  • 18
    • 0037609535 scopus 로고    scopus 로고
    • Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies
    • Ku, N.O.et al.Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies.Proc Natl Acad Sci USA 100:6063-6068 (2003).
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6063-6068
    • Ku, N.O.1
  • 19
    • 4043154985 scopus 로고    scopus 로고
    • Keratin 8 and 18 hyperphosphorylation is a marker of progression of human liver disease
    • Toivola, D.M.et al.Keratin 8 and 18 hyperphosphorylation is a marker of progression of human liver disease.Hepatology 40:459-466 (2004).
    • (2004) Hepatology , vol.40 , pp. 459-466
    • Toivola, D.M.1
  • 20
    • 7944221186 scopus 로고    scopus 로고
    • The keratin cytoskeleton in liver diseases
    • Zatloukal, K.et al.The keratin cytoskeleton in liver diseases.J Pathol 204:367-376 (2004).
    • (2004) J Pathol , vol.204 , pp. 367-376
    • Zatloukal, K.1
  • 21
    • 0025342697 scopus 로고
    • Biochemical mechanisms and pathobiology of alpha 2uglobulin nephropathy
    • Borghoff, S.J., Short, B.G. & Swenberg, J.A.Biochemical mechanisms and pathobiology of alpha 2uglobulin nephropathy.Annu Rev Pharmacol Toxicol 30:349-367 (1990).
    • (1990) Annu Rev Pharmacol Toxicol , vol.30 , pp. 349-367
    • Borghoff, S.J.1    Short, B.G.2    Swenberg, J.A.3
  • 22
    • 0026338659 scopus 로고
    • Alpha 2u-globulin nephropathy without nephrocarcinogenesis in male Wistar rats administered 1-(aminomethyl) cyclohexaneacetic acid
    • Dominick, M.A.et al.Alpha 2u-globulin nephropathy without nephrocarcinogenesis in male Wistar rats administered 1-(aminomethyl) cyclohexaneacetic acid.Toxicol Appl Pharmacol 111:375-387 (1991).
    • (1991) Toxicol Appl Pharmacol , vol.111 , pp. 375-387
    • Dominick, M.A.1
  • 23
    • 0030953476 scopus 로고    scopus 로고
    • 1,3,5-Trinitrobenzene-induced alpha-2u-globulin nephropathy
    • Kim, S., Qualls, C.W.Jr., Reddy, G. & Stair, E.L.1,3,5- Trinitrobenzene-induced alpha-2u-globulin nephropathy.Toxicol Pathol 25:195-201 (1997).
    • (1997) Toxicol Pathol , vol.25 , pp. 195-201
    • Kim, S.1    Qualls Jr., C.W.2    Reddy, G.3    Stair, E.L.4
  • 24
    • 34249656236 scopus 로고    scopus 로고
    • Prevalidation of potential protein biomarkers in toxicology using iTRAQ reagent technology
    • Gluckmann, M.et al.Prevalidation of potential protein biomarkers in toxicology using iTRAQ reagent technology.Proteomics 7:1564-1574 (2007).
    • (2007) Proteomics , vol.7 , pp. 1564-1574
    • Gluckmann, M.1
  • 25
    • 0020954585 scopus 로고
    • Effect of several xenobiotics on the activities of enzymes affecting ascorbic acid synthesis in rats
    • Tokyo
    • Horio, F., Kimura, M. & Yoshida, A.Effect of several xenobiotics on the activities of enzymes affecting ascorbic acid synthesis in rats.J Nutr Sci Vitaminol (Tokyo) 29:233-247 (1983).
    • (1983) J Nutr Sci Vitaminol , vol.29 , pp. 233-247
    • Horio, F.1    Kimura, M.2    Yoshida, A.3
  • 26
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E.A., Gambill, B.D. & Nelson, R.J.Heat shock proteins: molecular chaperones of protein biogenesis.Microbiol Rev 57:402-414 (1993).
    • (1993) Microbiol Rev , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 27
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen, B. & Braakman, I., Protein folding and quality control in the endoplasmic reticulum.Curr Opin Cell Biol 16:343-349 (2004).
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 28
    • 60349113650 scopus 로고    scopus 로고
    • Induction of hsp70, hsp60, hsp83 and hsp26 and oxidative stress markers in benzene, toluene and xylene exposed Drosophila melanogaster: Role of ROS generation
    • Singh, M.P., Reddy, M.M., Mathur, N., Saxena, D.K. & Chowdhuri, D.K.Induction of hsp70, hsp60, hsp83 and hsp26 and oxidative stress markers in benzene, toluene and xylene exposed Drosophila melanogaster: role of ROS generation.Toxicol Appl Pharmacol 235:226-243 (2009).
    • (2009) Toxicol Appl Pharmacol , vol.235 , pp. 226-243
    • Singh, M.P.1    Reddy, M.M.2    Mathur, N.3    Saxena, D.K.4    Chowdhuri, D.K.5
  • 29
    • 0030059329 scopus 로고    scopus 로고
    • Biliary expression of heat shock protein: A non-specific feature of chronic cholestatic liver diseases
    • Martins, E.B., Chapman, R.W., Marron, K. & Fleming, K.A.Biliary expression of heat shock protein: a non-specific feature of chronic cholestatic liver diseases.J Clin Pathol 49:53-56 (1996).
    • (1996) J Clin Pathol , vol.49 , pp. 53-56
    • Martins, E.B.1    Chapman, R.W.2    Marron, K.3    Fleming, K.A.4
  • 30
    • 0033975561 scopus 로고    scopus 로고
    • Ursodeoxycholic acid reduces expression of heat shock proteins in primary biliary cirrhosis
    • Sakisaka, S.et al.Ursodeoxycholic acid reduces expression of heat shock proteins in primary biliary cirrhosis.Liver 20:78-87 (2000).
    • (2000) Liver , vol.20 , pp. 78-87
    • Sakisaka, S.1
  • 31
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang, P. & MacRae, T.H.Molecular chaperones and the cytoskeleton.J Cell Sci 110:1431-1440 (1997).
    • (1997) J Cell Sci , vol.110 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 32
    • 0034141706 scopus 로고    scopus 로고
    • Down-regulation of the endoplasmic reticulum chaperone GRP78/BiP by vomitoxin (Deoxynivalenol)
    • Yang, G.H., Li, S. & Pestka, J.J.Down-regulation of the endoplasmic reticulum chaperone GRP78/BiP by vomitoxin (Deoxynivalenol).Toxicol Appl Pharmacol 162:207-217 (2000).
    • (2000) Toxicol Appl Pharmacol , vol.162 , pp. 207-217
    • Yang, G.H.1    Li, S.2    Pestka, J.J.3
  • 33
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young, J.C., Moarefi, I. & Hartl, F.U.Hsp90: a specialized but essential protein-folding tool.J Cell Biol 154:267-273 (2001).
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 34
    • 55249092971 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitors protect and restore pulmonary endothelial barrier function
    • Antonov, A.et al.Heat shock protein 90 inhibitors protect and restore pulmonary endothelial barrier function.Am J Respir Cell Mol Biol 39:551-559 (2008).
    • (2008) Am J Respir Cell Mol Biol , vol.39 , pp. 551-559
    • Antonov, A.1
  • 35
    • 0142151383 scopus 로고    scopus 로고
    • Single-step perfusion chromatography with a throughput potential for enhanced peptide detection by matrix-assisted laser desorption/ionizationmass spectrometry
    • Choi, B.K., Cho, Y.M., Bae, S.H., Zoubaulis, C.C. & Paik, Y.K.Single-step perfusion chromatography with a throughput potential for enhanced peptide detection by matrix-assisted laser desorption/ionizationmass spectrometry.Proteomics 3:1955-1961 (2003)
    • (2003) Proteomics , vol.3 , pp. 1955-1961
    • Choi, B.K.1    Cho, Y.M.2    Bae, S.H.3    Zoubaulis, C.C.4    Paik, Y.K.5


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