Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-13159
Nakayama, A; Riesen, I; Köllner, B; Eppler, E; Segner, H (2008). Surface marker-defined head kidney granulocytes and B lymphocytes of rainbow trout express benzo[alpha]pyrene-inducible cytochrome P4501A protein. Toxicological Sciences, 103(1):86-96.
Polycyclic aromatic hydrocarbons (PAHs) such as benzo[a]pyrene (BaP) are immunotoxic to fish. Metabolism of PAHs in immune cells has been implicated in PAH immunotoxicity in mammals, but for fish the presence of metabolic enzymes in immune cells is less clear. The objective of this study was to examine localization and induction of the BaP-metabolizing biotransformation enzyme, cytochrome P4501A (CYP1A), in head kidney immune cells of rainbow trout (Oncorhynchus mykiss). In the first step, we measured induction of CYP1A-dependent 7-ethoxyresorufin-O-deethylase (EROD) activity and CYP1A protein in head kidney of rainbow trout treated with a single intraperitoneal (ip) injection of 25 mg BaP/kg body weight. From days 3 to 10 postinjection, the BaP treatment led to a significant elevation of EROD and CYP1A protein in head kidney and liver, with CYP1A expression levels in the head kidney being much lower than in the liver. Next, we examined the cellular localization of CYP1A protein in the head kidney cell types: vascular endothelial, endocrine and lymphoid cells. CYP1A immunoreactivity was detectable only in BaP-treated trout, where it was localized in endothelial and lymphoid cells. Finally, we aimed to clarify which of the hematopoietic cell types possess CYP1A protein. Using double immunostaining for CYP1A and surface markers of rainbow trout immune cells, we identified B lymphocytes and granulocytes expressing inducible CYP1A protein and being the likely sites of BaP metabolism in the head kidney.
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > Institute of Anatomy|
|DDC:||570 Life sciences; biology|
610 Medicine & health
|Date:||14 February 2008|
|Deposited On:||10 Feb 2009 09:02|
|Last Modified:||27 Nov 2013 20:14|
|Publisher:||Oxford University Press|
|Additional Information:||This is a pre-copy-editing, author-produced PDF of an article accepted for publication in Toxicological Sciences following peer review. The definitive publisher-authenticated version Toxicological Sciences, doi:10.1093/toxsci/kfn024 is available online at: http://toxsci.oxfordjournals.org/cgi/content/abstract/kfn024v1|
|Citations:||Web of Science®. Times cited: 12|
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