Cytochrome P4501A induced differentially in endothelial cells cultured from different organs of Anguilia rostrata
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Endothelial cells are a structural barrier and an active regulator of many bodily processes. Cytochrome P4501A (CYPIA) activity is induced in the endothelium of teleosts and mammals exposed to lipophilic xenobiotics, such as polycyclic aromatic hydrocarbons, and can have significant consequences for endothelial functions. We exposed cultures of characterized endothelial cells from the heart, kidney, and rete mirabile of the eel, Anguilla rostrata, to aryl hydrocarbon receptor (AhR) agonists. In heart endothelial cells, the maximum response (based on O-deethylation of 7-ethoxyresorufin to resorufin [EROD] activity) to 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), 113 pmol/mg/min, was at 1 nM TCDD and the peak response to β-napthoflavone (βNF), 135 pmol/mg/min, was at 3 μM βNF. The maximum response to TCDD in the kidney endothelial cells is 12 pmol/mg/min at 0.3 nM TCDD. The rete mirabile capillary endothelial cells responded minimally or not at all to exposure to TCDD and βNF. Both the heart and kidney endothelial cells (but not the rete mirabile capillary cells) have a low level of EROD activity (12.7 and 5.2 pmol/mg/min, respectively) in untreated or dimethylsulfoxide-treated cells. The robust response of the heart endothelial cells to induction and the lack of response in the rete mirabile capillary endothelial cells indicate that these cells are a good resource to use to investigate the physiological consequences of AhR agonist exposure and CYP1A induction in different areas of the vasculature.
Key wordsteleost eel fish microvasculature endothelium pHAH cytochrome P450 EROD dioxin CYPIA
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- Dugas, T. R.; Morel, D. W.; Harrison, E. H. Novel cell culture medium for use in oxidation experiments provides insights into mechanisms of endothelial cell-mediated oxidation of LDL. In Vitro Cell. Dev. Biol. 36A:571–577; 2000.Google Scholar
- Ganassin, R. C.; Schirmer, K.; Bols, N. C. Cell and tissue culture. In: Ostrander, G. K., ed. The laboratory fish. San Diego, CA: Academic Press; 2000:631–651.Google Scholar
- Park, S. S.; Miller, H.; Klotz, A. V.; Kloepper-Sams, P. J.; Stegeman, J. J.; Gelboin, H. V. Monoclonal antibodies to liver microsomal cytochrome P-450E of the marine fish Stenotomus chrysops (scup): cross reactivity with 3-methylcholanthrene induced rat cytochrome P-450. Arch. Biochem. Biophys. 249(2):339–350; 1986.PubMedCrossRefGoogle Scholar
- Schlezinger, J. J.; Keller, J.; Verbrugge, L. A.; Stegeman, J. J. 3,3′,4,4′-tetrachlorobiphenyl oxidation in fish, bird and reptile species: relationship to cytochrome P4501A inactivation and reactive oxygen production. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 125(3):273–286; 2000.PubMedGoogle Scholar
- Smolowitz, R. M.; Hahn, M. E.; Stegeman, J. J. Immunohistochemical localization of cytochrome P4501A1 induced by 3,3′,4,4′-tetrachlorobiphenyl and by 2,3,7,8-tetrachlorodibenzofuran in liver and extrahepatic tissues of the teleost Stenotomus chrysops (scup). Drug Metab. Dispos. 19(1):113–123; 1991.PubMedGoogle Scholar
- Stegeman, J. J.; Hahn, M. E.; Weisbrod, R.; Woodin, B. R.; Joy, J. S.; Najibi, S.; Cohen, R. A. Induction of cytochrome P4501A1 by aryl hydrocarbon receptor agonists in porcine aorta endothelial cells in culture and cytochrome P4501A1 activity in intact cells. Mol. Pharmacol. 47(2):296–306; 1995.PubMedGoogle Scholar
- Stegeman, J. J.; Miller, M.; Singh, H.; Hinton, D. Cytochrome P450E induction and localization in liver and endothelial tissue of extrahepatic organs of scup. Fed. Proc. 46:379; 1987.Google Scholar
- Tom, D. J.; Lee, L. E.; Lew, J.; Bols, N. C. Induction of 7-ethoxyresorufin-o-deethylase activity by planar chlorinated hydrocarbons and polycyclic aromatic hydrocarbons in cell lines from the rainbow trout pituitary. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 128(2):185–198; 2001.PubMedCrossRefGoogle Scholar