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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).
J Exp Biol. 2009 Nov; 212(Pt 22):3612-20.JE

Abstract

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 micromol 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 micromol l(-1) cariporide, significantly diminished cadmium effects in each case. Similarly, attenuation of cadmium effects were observed in cells pre-treated with either 11 micromol 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 micromol l(-1) DPI, a NADPH oxidase inhibitor, or 10 micromol 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.

Authors+Show Affiliations

Department of Biology, University of Patras, Greece. sdailianis@upatras.grNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

19880721

Citation

Dailianis, Stefanos, et al. "The Role of Signalling Molecules On Actin Glutathionylation and Protein Carbonylation Induced By Cadmium in Haemocytes of Mussel Mytilus Galloprovincialis (Lmk)." The Journal of Experimental Biology, vol. 212, no. Pt 22, 2009, pp. 3612-20.
Dailianis S, Patetsini E, Kaloyianni M. The role of signalling molecules on actin glutathionylation and protein carbonylation induced by cadmium in haemocytes of mussel Mytilus galloprovincialis (Lmk). J Exp Biol. 2009;212(Pt 22):3612-20.
Dailianis, S., Patetsini, E., & Kaloyianni, M. (2009). The role of signalling molecules on actin glutathionylation and protein carbonylation induced by cadmium in haemocytes of mussel Mytilus galloprovincialis (Lmk). The Journal of Experimental Biology, 212(Pt 22), 3612-20. https://doi.org/10.1242/jeb.030817
Dailianis S, Patetsini E, Kaloyianni M. The Role of Signalling Molecules On Actin Glutathionylation and Protein Carbonylation Induced By Cadmium in Haemocytes of Mussel Mytilus Galloprovincialis (Lmk). J Exp Biol. 2009;212(Pt 22):3612-20. PubMed PMID: 19880721.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The role of signalling molecules on actin glutathionylation and protein carbonylation induced by cadmium in haemocytes of mussel Mytilus galloprovincialis (Lmk). AU - Dailianis,Stefanos, AU - Patetsini,Efterpi, AU - Kaloyianni,Martha, PY - 2009/11/3/entrez PY - 2009/11/3/pubmed PY - 2010/2/18/medline SP - 3612 EP - 20 JF - The Journal of experimental biology JO - J Exp Biol VL - 212 IS - Pt 22 N2 - 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 micromol 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 micromol l(-1) cariporide, significantly diminished cadmium effects in each case. Similarly, attenuation of cadmium effects were observed in cells pre-treated with either 11 micromol 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 micromol l(-1) DPI, a NADPH oxidase inhibitor, or 10 micromol 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. SN - 1477-9145 UR - https://www.unboundmedicine.com/medline/citation/19880721/The_role_of_signalling_molecules_on_actin_glutathionylation_and_protein_carbonylation_induced_by_cadmium_in_haemocytes_of_mussel_Mytilus_galloprovincialis__Lmk__ L2 - http://jeb.biologists.org/cgi/pmidlookup?view=long&pmid=19880721 DB - PRIME DP - Unbound Medicine ER -