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First published online October 30, 2009
Journal of Experimental Biology 212, 3612-3620 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.030817

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The role of signalling molecules on actin glutathionylation and protein carbonylation induced by cadmium in haemocytes of mussel Mytilus galloprovincialis (Lmk)

Stefanos Dailianis^1,*, Efterpi Patetsini² and Martha Kaloyianni²

¹ Section of Animal Biology, Department of Biology, Faculty of Sciences, University of Patras, 26 500, Greece
² Laboratory of Animal Physiology, Department of Zoology, School of Biology, Aristotle University of Thessaloniki 54124, Greece

^* Author for correspondence (sdailianis{at}upatras.gr)

Accepted 6 August 2009

This study investigated the role of Na⁺/H⁺ exchanger (NHE) and signalling molecules, such as cAMP, PKC, PI 3-kinase, and immune defence enzymes, NADPH oxidase and nitric oxide synthase, in the induction of protein glutathionylation and carbonylation in cadmium-treated haemocytes of mussel Mytilus galloprovincialis. Glutathionylation was detected by western blot analysis and showed actin as its main target. A significant increase of both actin glutathionylation and protein carbonylation, were observed in haemocytes exposed to micromolar concentration of cadmium chloride (5 µmol l^–1). Cadmium seems to cause actin polymerization that may lead to its increased glutathionylation, probably to protect it from cadmium-induced oxidative stress. It is therefore possible that polymerization of actin plays a signalling role in the induction of both glutathionylation and carbonylation processes. NHE seems to play a regulatory role in the induction of oxidative damage and actin glutathionylation, since its inhibition by 2 µmol l^–1 cariporide, significantly diminished cadmium effects in each case. Similarly, attenuation of cadmium effects were observed in cells pre-treated with either 11 µmol l^–1 GF-109203X, a potent inhibitor of PKC, 50 nmol l^–1 wortmannin, an inhibitor of PI 3-kinase, 0.01 mmol l^–1 forskolin, an adenylyl cyclase activator, 10 µmol l^–1 DPI, a NADPH oxidase inhibitor, or 10 µmol l^–1 L-NAME, a nitric oxide synthase inhibitor, suggesting a possible role of PKC, PI 3-kinase and cAMP, as well as NADPH oxidase and nitric oxide synthase in the enhancement of cadmium effects on both actin glutathionylation and protein carbonylation.

Key words: actin, cadmium, cAMP, carbonylation, glutathionylation, haemocytes, NHE, NADPH oxidase, nitric oxide synthase, PI 3-kinase, oxidative stress

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