Detoxification enzyme activities (CYP1A1 and GST) in the skin of humpback whales as a function of organochlorine burdens and migration status


Autoria(s): Bengston Nash, S.; Daswon, A.; Burkhard , M.; Waugh, C.; Huston, W.
Data(s)

01/10/2014

Resumo

The activities of glutathione-s-transferase (GST) and cytochrome P-450 1A1 (CYP1A1) enzymes were measured in freshly extracted epidermis of live-biopsied, migrating, southern hemisphere humpback whales (Megaptera novaeangliae). The two quantified enzyme activities did not correlate strongly with each other. Similarly, neither correlated strongly with any of the organochlorine compound groups previously measured in the superficial blubber of the sample biopsy core, likely reflecting the anticipated low levels of typical aryl-hydrocarbon receptor ligands. GST activity did not differ significantly between genders or between northward (early migration) or southward (late migration) migrating cohorts. Indeed, the inter-individual variability in GST measurements was relatively low. This observation raises the possibility that measured activities were basal activities and that GST function was inherently impacted by the fasting state of the sampled animals, as seen in other species. These results do not support the implementation of CYP1A1 or GST as effective biomarkers of organochlorine contaminant burdens in southern hemisphere populations of humpback whales as advocated for other cetacean species. Further investigation of GST activity in feeding versus fasting cohorts may, however, provide some insight into the fasting metabolism of these behaviourally adapted populations.

Identificador

http://eprints.qut.edu.au/77691/

Publicador

Elsevier

Relação

DOI:10.1016/j.aquatox.2014.06.021

Bengston Nash, S., Daswon, A., Burkhard , M., Waugh, C., & Huston, W. (2014) Detoxification enzyme activities (CYP1A1 and GST) in the skin of humpback whales as a function of organochlorine burdens and migration status. Aquatic Toxicology, 155, pp. 207-212.

Direitos

Copyright 2014 Elsevier

This is the author’s version of a work that was accepted for publication in Aquatic Toxicology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in PUBLICATION, [VOL 155, (2014)] DOI: 10.1016/j.aquatox.2014.06.021

Fonte

School of Biomedical Sciences; Faculty of Health; Institute of Health and Biomedical Innovation

Palavras-Chave #060107 Enzymes
Tipo

Journal Article