In vivo exposure of Dreissena polymorpha mussels to the quinones menadione and lawsone: menadione is more toxic to mussels than lawsone.
The principal aim of this study was to assess whether the two quinones, menadione (2-methyl-1,4-naphthoquinone) and lawsone (2-hydroxy-1,4-naphthoquinone), elicit differential toxicity in mussels as has been reported for higher organisms. Therefore, the effects of short-term (48 h) and long-term (20 days) exposure of the two quinones at concentrations of 0.56 and 1 mg l(-1) to zebra mussels, Dreissena polymorpha, under laboratory conditions were studied. After the short-term exposure, the specific activities of the two-electron quinone oxidoreductase (DT-diaphorase) and the one-electron catalysing quinone reductases NADPH-cytochrome c reductase and NADH-cytochrome c reductase were determined in the gills and the rest of the soft tissues (soft mussel tissues minus the gills) of both treated and control mussels. At the higher concentrations of menadione and lawsone used, a significant reduction of the activity of NADPH-cytochrome c reductase in the gills and in the rest of the soft mussel tissues (by 33-34% and 31-43%, respectively) was observed. The activities of DT-diaphorase and NADH-cytochrome c reductase were not significantly affected. Interestingly, DT-diaphorase was observed in the gills, an organ requiring protection against antioxidants. Furthermore, a single-cell electrophoretic assay (comet assay) performed with gill cells to assess DNA damage by the quinones did not show any significant difference between the treated and the control organisms. This indicates that the formation of reactive species by the quinone metabolism in vivo in the mussels was possibly suppressed through the concerted action of DT-diaphorase and antioxidant enzymes. The results of in vitro experiments with gill extracts confirmed the protective role of DT-diaphorase. The rate of the two-electron quinone reduction was found to be five times that of the one-electron quinone reduction. The results of the long-term exposure unambiguously demonstrated that in mussels menadione, unlike in higher organisms, is more toxic than lawsone. The lack of detectability of xanthine oxidase in the mussel tissues could explain the comparatively lower toxicity of lawsone in the invertebtrate, lending support to a previous suggestion that xanthine oxidase might be responsible for the mechanism of toxicity of lawsone in higher organisms in vivo.
Osman
A M
AM
Institute for Inland Water Management and Waste Water Treatment, PO Box 17, 8200 AA Lelystad, The Netherlands. A.Osman@riza.rws.minvenw.nl
Rotteveel
S
S
den Besten
P J
PJ
van Noort
P C M
PC
D000818:Animals; D000933:Antifibrinolytic Agents / Q000633:toxicity*; D049872:Bivalvia / Q000737:chemistry; D020552:Comet Assay; D003238:Connective Tissue / Q000187:drug effects / Q000201:enzymology; D004249:DNA Damage; D004305:Dose-Response Relationship, Drug; D005880:Gills / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000378:metabolism; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D009285:Naphthoquinones / Q000633:toxicity*; D010088:Oxidoreductases; D014020:Tissue Extracts / Q000737:chemistry / Q000378:metabolism; D018675:Toxicity Tests / Q000379:methods*; D024483:Vitamin K 3 / Q000633:toxicity*
D000933:Antifibrinolytic Agents; D009285:Naphthoquinones; D014020:Tissue Extracts; D024483:Vitamin K 3; D010088:Oxidoreductases; D009251:NADPH-Ferrihemoprotein Reductase; D016660:NAD(P)H Dehydrogenase (Quinone); C005090:lawsone