메뉴 건너뛰기




Volumn 581, Issue 3, 2008, Pages 244-254

Microtubules-interfering agents restrict aryl hydrocarbon receptor-mediated CYP1A2 induction in primary cultures of human hepatocytes via c-jun-N-terminal kinase and glucocorticoid receptor

Author keywords

Aryl hydrocarbon receptor; Cytoskeleton; Glucocorticoid receptor; Human hepatocytes; MAPK kinases

Indexed keywords

AROMATIC HYDROCARBON RECEPTOR; COLCHICINE; CYCLOHEXIMIDE; CYTOCHROME P450 1A2; GLUCOCORTICOID RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; NOCODAZOLE; PACLITAXEL; STRESS ACTIVATED PROTEIN KINASE; VINBLASTINE; VINCRISTINE;

EID: 39149134269     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejphar.2007.11.059     Document Type: Article
Times cited : (35)

References (31)
  • 1
    • 0032589068 scopus 로고    scopus 로고
    • RT-PCR quantification of AHR, ARNT, GR, and CYP1A1 mRNA in craniofacial tissues of embryonic mice exposed to 2,3,7,8-tetrachlorodibenzo-p-dioxin and hydrocortisone
    • Abbott B.D., Schmid J.E., Brown J.G., Wood C.R., White R.D., Buckalew A.R., and Held G.A. RT-PCR quantification of AHR, ARNT, GR, and CYP1A1 mRNA in craniofacial tissues of embryonic mice exposed to 2,3,7,8-tetrachlorodibenzo-p-dioxin and hydrocortisone. Toxicol. Sci. 47 (1999) 76-85
    • (1999) Toxicol. Sci. , vol.47 , pp. 76-85
    • Abbott, B.D.1    Schmid, J.E.2    Brown, J.G.3    Wood, C.R.4    White, R.D.5    Buckalew, A.R.6    Held, G.A.7
  • 2
    • 1942452867 scopus 로고    scopus 로고
    • beta-naphthoflavone disrupts cortisol production and liver glucocorticoid responsiveness in rainbow trout
    • Aluru N., and Vijayan M.M. beta-naphthoflavone disrupts cortisol production and liver glucocorticoid responsiveness in rainbow trout. Aquat. Toxicol. 67 (2004) 273-285
    • (2004) Aquat. Toxicol. , vol.67 , pp. 273-285
    • Aluru, N.1    Vijayan, M.M.2
  • 3
    • 0029591827 scopus 로고
    • Cellular stresses differentially activate c-Jun N-terminal protein kinases and extracellular signal-regulated protein kinases in cultured ventricular myocytes
    • Bogoyevitch M.A., Ketterman A.J., and Sugden P.H. Cellular stresses differentially activate c-Jun N-terminal protein kinases and extracellular signal-regulated protein kinases in cultured ventricular myocytes. J. Biol. Chem. 270 (1995) 29710-29717
    • (1995) J. Biol. Chem. , vol.270 , pp. 29710-29717
    • Bogoyevitch, M.A.1    Ketterman, A.J.2    Sugden, P.H.3
  • 4
    • 15744398193 scopus 로고    scopus 로고
    • Arsenite inhibition of CYP1A1 induction by 2,3,7,8-tetrachlorodibenzo-p-dioxin is independent of cell cycle arrest
    • Bonzo J.A., Chen S., Galijatovic A., and Tukey R.H. Arsenite inhibition of CYP1A1 induction by 2,3,7,8-tetrachlorodibenzo-p-dioxin is independent of cell cycle arrest. Mol. Pharmacol. 67 (2005) 1247-1256
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1247-1256
    • Bonzo, J.A.1    Chen, S.2    Galijatovic, A.3    Tukey, R.H.4
  • 5
    • 27944465892 scopus 로고    scopus 로고
    • Microtubule disarray in primary cultures of human hepatocytes inhibits transcriptional activity of the glucocorticoid receptor via activation of c-jun N-terminal kinase
    • Dvorak Z., Maurel P., Ulrichova J., and Modriansky M. Microtubule disarray in primary cultures of human hepatocytes inhibits transcriptional activity of the glucocorticoid receptor via activation of c-jun N-terminal kinase. Biomed. Pap. Med. Fac. Palacky Univ. Olomouc Czech Repub. 148 (2004) 135-139
    • (2004) Biomed. Pap. Med. Fac. Palacky Univ. Olomouc Czech Repub. , vol.148 , pp. 135-139
    • Dvorak, Z.1    Maurel, P.2    Ulrichova, J.3    Modriansky, M.4
  • 6
    • 0037561538 scopus 로고    scopus 로고
    • Colchicine down-regulates cytochrome P450 2B6, 2C8, 2C9, and 3A4 in human hepatocytes by affecting their glucocorticoid receptor-mediated regulation
    • Dvorak Z., Modriansky M., Pichard-Garcia L., Balaguer P., Vilarem M.J., Ulrichova J., Maurel P., and Pascussi J.M. Colchicine down-regulates cytochrome P450 2B6, 2C8, 2C9, and 3A4 in human hepatocytes by affecting their glucocorticoid receptor-mediated regulation. Mol. Pharmacol. 64 (2003) 160-169
    • (2003) Mol. Pharmacol. , vol.64 , pp. 160-169
    • Dvorak, Z.1    Modriansky, M.2    Pichard-Garcia, L.3    Balaguer, P.4    Vilarem, M.J.5    Ulrichova, J.6    Maurel, P.7    Pascussi, J.M.8
  • 9
    • 0033523006 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton
    • Galigniana M.D., Housley P.R., DeFranco D.B., and Pratt W.B. Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton. J. Biol. Chem. 274 (1999) 16222-16227
    • (1999) J. Biol. Chem. , vol.274 , pp. 16222-16227
    • Galigniana, M.D.1    Housley, P.R.2    DeFranco, D.B.3    Pratt, W.B.4
  • 10
    • 0035805599 scopus 로고    scopus 로고
    • Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus
    • Galigniana M.D., Radanyi C., Renoir J.M., Housley P.R., and Pratt W.B. Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus. J. Biol. Chem. 276 (2001) 14884-14889
    • (2001) J. Biol. Chem. , vol.276 , pp. 14884-14889
    • Galigniana, M.D.1    Radanyi, C.2    Renoir, J.M.3    Housley, P.R.4    Pratt, W.B.5
  • 11
    • 0031757167 scopus 로고    scopus 로고
    • Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton
    • Galigniana M.D., Scruggs J.L., Herrington J., Welsh M.J., Carter-Su C., Housley P.R., and Pratt W.B. Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton. Mol. Endocrinol. 12 (1998) 1903-1913
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1903-1913
    • Galigniana, M.D.1    Scruggs, J.L.2    Herrington, J.3    Welsh, M.J.4    Carter-Su, C.5    Housley, P.R.6    Pratt, W.B.7
  • 14
    • 0142212164 scopus 로고    scopus 로고
    • The Jun N-terminal kinase inhibitor SP600125 is a ligand and antagonist of the aryl hydrocarbon receptor
    • Joiakim A., Mathieu P.A., Palermo C., Gasiewicz T.A., and Reiners Jr. J.J. The Jun N-terminal kinase inhibitor SP600125 is a ligand and antagonist of the aryl hydrocarbon receptor. Drug. Metab. Dispos. 31 (2003) 1279-1282
    • (2003) Drug. Metab. Dispos. , vol.31 , pp. 1279-1282
    • Joiakim, A.1    Mathieu, P.A.2    Palermo, C.3    Gasiewicz, T.A.4    Reiners Jr., J.J.5
  • 15
    • 0030998260 scopus 로고    scopus 로고
    • Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor
    • Krstic M.D., Rogatsky I., Yamamoto K.R., and Garabedian M.J. Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor. Mol. Cell. Biol. 17 (1997) 3947-3954
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3947-3954
    • Krstic, M.D.1    Rogatsky, I.2    Yamamoto, K.R.3    Garabedian, M.J.4
  • 16
    • 0032970253 scopus 로고    scopus 로고
    • Role of canonical glucocorticoid responsive elements in modulating expression of genes regulated by the arylhydrocarbon receptor
    • Linder M.W., Falkner K.C., Srinivasan G., Hines R.N., and Prough R.A. Role of canonical glucocorticoid responsive elements in modulating expression of genes regulated by the arylhydrocarbon receptor. Drug. Metab. Rev. 31 (1999) 247-271
    • (1999) Drug. Metab. Rev. , vol.31 , pp. 247-271
    • Linder, M.W.1    Falkner, K.C.2    Srinivasan, G.3    Hines, R.N.4    Prough, R.A.5
  • 17
    • 0022454455 scopus 로고
    • Synergistic induction of monooxygenase activity by glucocorticoids and polycyclic aromatic hydrocarbons in human fetal hepatocytes in primary monolayer culture
    • Mathis J.M., Prough R.A., and Simpson E.R. Synergistic induction of monooxygenase activity by glucocorticoids and polycyclic aromatic hydrocarbons in human fetal hepatocytes in primary monolayer culture. Arch. Biochem. Biophys. 244 (1986) 650-661
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 650-661
    • Mathis, J.M.1    Prough, R.A.2    Simpson, E.R.3
  • 18
    • 0030588645 scopus 로고    scopus 로고
    • The use of adult human hepatocytes in primary culture and other in vitro systems to investigate drug metabolism in man
    • Maurel P. The use of adult human hepatocytes in primary culture and other in vitro systems to investigate drug metabolism in man. Adv. Drug Deliv. Rev. 22 (1996) 105-132
    • (1996) Adv. Drug Deliv. Rev. , vol.22 , pp. 105-132
    • Maurel, P.1
  • 22
    • 0037145007 scopus 로고    scopus 로고
    • The mechanism of AH receptor protein down-regulation (degradation) and its impact on AH receptor-mediated gene regulation
    • Pollenz R.S. The mechanism of AH receptor protein down-regulation (degradation) and its impact on AH receptor-mediated gene regulation. Chem. Biol. Interact. 141 (2002) 41-61
    • (2002) Chem. Biol. Interact. , vol.141 , pp. 41-61
    • Pollenz, R.S.1
  • 23
    • 33750744456 scopus 로고    scopus 로고
    • Ligand-dependent and -independent degradation of the human aryl hydrocarbon receptor (hAHR) in cell culture models
    • Pollenz R.S., and Buggy C. Ligand-dependent and -independent degradation of the human aryl hydrocarbon receptor (hAHR) in cell culture models. Chem. Biol. Interact. 164 (2006) 49-59
    • (2006) Chem. Biol. Interact. , vol.164 , pp. 49-59
    • Pollenz, R.S.1    Buggy, C.2
  • 24
    • 33748929496 scopus 로고    scopus 로고
    • Role of endogenous XAP2 protein on the localization and nucleocytoplasmic shuttling of the endogenous mouse Ahb-1 receptor in the presence and absence of ligand
    • Pollenz R.S., Wilson S.E., and Dougherty E.J. Role of endogenous XAP2 protein on the localization and nucleocytoplasmic shuttling of the endogenous mouse Ahb-1 receptor in the presence and absence of ligand. Mol. Pharmacol. 70 (2006) 1369-1379
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1369-1379
    • Pollenz, R.S.1    Wilson, S.E.2    Dougherty, E.J.3
  • 25
    • 2442537231 scopus 로고    scopus 로고
    • Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
    • Pratt W.B., Galigniana M.D., Harrell J.M., and DeFranco D.B. Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement. Cell. Signal. 16 (2004) 857-872
    • (2004) Cell. Signal. , vol.16 , pp. 857-872
    • Pratt, W.B.1    Galigniana, M.D.2    Harrell, J.M.3    DeFranco, D.B.4
  • 26
    • 0032478254 scopus 로고    scopus 로고
    • Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase
    • Rogatsky I., Logan S.K., and Garabedian M.J. Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 2050-2055
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2050-2055
    • Rogatsky, I.1    Logan, S.K.2    Garabedian, M.J.3
  • 28
    • 0028291623 scopus 로고
    • Short and long term effects of cytoskeleton-disrupting drugs on cytochrome P450 Cyp1a-1 induction in murine hepatoma 1c1c7 cells: suppression by the microtubule inhibitor nocodazole
    • Scholler A., Hong N.J., Bischer P., and Reiners Jr. J.J. Short and long term effects of cytoskeleton-disrupting drugs on cytochrome P450 Cyp1a-1 induction in murine hepatoma 1c1c7 cells: suppression by the microtubule inhibitor nocodazole. Mol. Pharmacol. 45 (1994) 944-954
    • (1994) Mol. Pharmacol. , vol.45 , pp. 944-954
    • Scholler, A.1    Hong, N.J.2    Bischer, P.3    Reiners Jr., J.J.4
  • 29
    • 0036711207 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases (MAPKs) by aromatic hydrocarbons: role in the regulation of aryl hydrocarbon receptor (AHR) function
    • Tan Z., Chang X., Puga A., and Xia Y. Activation of mitogen-activated protein kinases (MAPKs) by aromatic hydrocarbons: role in the regulation of aryl hydrocarbon receptor (AHR) function. Biochem. Pharmacol. 64 (2002) 771-780
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 771-780
    • Tan, Z.1    Chang, X.2    Puga, A.3    Xia, Y.4
  • 30
    • 8444245911 scopus 로고    scopus 로고
    • A critical role for MAP kinases in the control of Ah receptor complex activity
    • Tan Z., Huang M., Puga A., and Xia Y. A critical role for MAP kinases in the control of Ah receptor complex activity. Toxicol. Sci. 82 (2004) 80-87
    • (2004) Toxicol. Sci. , vol.82 , pp. 80-87
    • Tan, Z.1    Huang, M.2    Puga, A.3    Xia, Y.4
  • 31
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell L., and Cook P. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol. Endocrinol. 10 (1996) 705-712
    • (1996) Mol. Endocrinol. , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.