Carbonylation and glutathionylation of proteins in the blue mussel Mytilus edulis detected by proteomic analysis and Western blotting: Actin as a target for oxidative stress

Tyther, Raymond; Sheehan, David

doi:10.1016/j.aquatox.2005.03.020

Cited by 115 publications

(66 citation statements)

References 40 publications

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“…Thus it is likely that the level of cytotoxic aldehydes will increase as temperature decreases. In turn, these aldehydes cause protein carbonylation, which affects protein conformation and function, leading to protein denaturation (McDonagh et al, 2005). Based on these changes, an important oxidative stress protein upregulated during cold acclimation in both species is an isoform of aldehyde dehydrogenase (ALDH2) located in the mitochondrion (Ellis, 2007).…”

Section: Cold Acclimationmentioning

confidence: 99%

Proteomic responses of blue mussel (Mytilus) congeners to temperature acclimation

Fields

Zuzow

Tomanek

2012

Journal of Experimental Biology

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SUMMARYThe ability to acclimate to variable environmental conditions affects the biogeographic range of species, their success at colonizing new habitats, and their likelihood of surviving rapid anthropogenic climate change. Here we compared responses to temperature acclimation (4weeks at 7, 13 and 19°C) in gill tissue of the warm-adapted intertidal blue mussel Mytilus galloprovincialis, an invasive species in the northeastern Pacific, and the cold-adapted M. trossulus, the native congener in the region, to better understand the physiological differences underlying the ongoing competition. Using two-dimensional gel electrophoresis and tandem mass spectrometry, we showed that warm acclimation caused changes in cytoskeletal composition and proteins of energy metabolism in both species, consistent with increasing rates of filtration and respiration due to increased ciliary activity. During cold acclimation, changes in cytoskeletal proteins were accompanied by increasing abundances of oxidative stress proteins and molecular chaperones, possibly because of the increased production of aldehydes as indicated by the upregulation of aldehyde dehydrogenase. The cold-adapted M. trossulus showed increased abundances of molecular chaperones at 19°C, but M. galloprovincialis did not, suggesting that the two species differ in their long-term upper thermal limits. In contrast, the warm-adapted M. galloprovincialis showed a stronger response to cold acclimation than M. trossulus, including changes in abundance in more proteins and differing protein expression profiles between 7 and 13°C, a pattern absent in M. trossulus. In general, increasing levels of oxidative stress proteins inversely correlate with modifications in Krebs cycle and electron transport chain proteins, indicating a trade-off between oxidative stress resistance and energy production. Overall, our results help explain why M. galloprovincialis has replaced M. trossulus in southern California over the last century, but also suggest that M. trossulus may maintain a competitive advantage at colder temperatures. Anthropogenic global warming may reinforce the advantage M. galloprovincialis has over M. trossulus in the warmer parts of the latterʼs historical range. Supplementary material available online at

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Section: Cold Acclimationmentioning

confidence: 99%

Proteomic responses of blue mussel (Mytilus) congeners to temperature acclimation

Fields

Zuzow

Tomanek

2012

Journal of Experimental Biology

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“…Although there are several reports concerning the effects of oxidative stress induced by heavy metals and its role in glutathionylation and carbonylation processes in tissues of mussels (Kirchin et al, 1992;Fagotti et al, 1996;Dalle-Donne et al, 2003a;Dalle-Donne et al, 2003b;Gomez-Mendikute and Cajaraville, 2003;McDonagh et al, 2005), the involvement of signal cascades in the induction of these processes in haemocytes of Mytilus after exposure to heavy metals still remains unclear. Cd has been reported to induce signal transduction cascades, such as protein kinase C (PKC), tyrosine kinase and casein kinase II (Adams et al, 2002), and recent studies in our laboratory have shown the induction of a PKC-mediated signal transduction pathway with a concomitant increase of ROS production and Na + /H + exchanger (NHE) stimulation in Cd-treated cells of mussels (Dailianis and Kaloyianni, 2004 expressed integral membrane protein involved in the coupled exchange of Na + with H + in a variety of eukaryotic cells, is considered of vital importance, since it has been suggested to play important roles in cytoskeletal reorganization, cell migration (Reshkin et al, 2000;McHardy et al, 2004;Paradiso et al, 2004;Konstantinidis et al, 2009), regulation of intracellular pH (pH i ) (Moolenaar et al, 1983;Bianchini and Pouyssegur, 1994), cell volume control (Cala, 1983a;Cala, 1983b) and other cell activities such as cell adhesion, proliferation and apoptosis (Tominaga and Barber, 1998;Khaled et al, 2001;Moor et al, 2001;Avkiran and Haworth, 2003;Orlowski and Grinstein, 2004;Koliakos et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

“…Actin is a key target of glutathionylation in mussels, providing an important means for the cytoskeleton to 'sense' altered redox status (Kirchin et al, 1992;Dalle-Donne et al, 2003a;McDonagh et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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

Dailianis

Patetsini

Kaloyianni

2009

Journal of Experimental Biology

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

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“…Using protein expression profiles, several authors have reported on the use of proteomic approaches for the establishment of ''protein signatures'' after exposure to a variety of environmental contaminants including PCBs, polyaromatic hydrocarbons (PAHs), heavy metals [50,51], and crude oil [52][53][54]. Additionally, proteomics has been used to compare profiles of mussels residing in polluted areas to those of reference sites [55,56]. Not only have the proteomes of these bivalve species been evaluated when exposed to individual contaminants, but to mixtures as well [57].…”

Section: Aquatic Invertebratesmentioning

confidence: 99%

“…Others have focused on machine learning techniques to process and extract informative expression signatures from MS data, instead of focusing on single protein identification [13]. Furthermore, changes in chemical status of proteins, such as modifications due to oxidative stress, have been used to help in protein identification [55,61,62,[71][72][73][74][75]. Overall, this demonstrates the limitations in protein identification when the species of interest does not have a sequenced genome.…”

Section: Aquatic Invertebratesmentioning

confidence: 99%

Review of recent proteomic applications in aquatic toxicology

Sanchez

Ralston-Hooper

Sepúlveda

2010

Enviro Toxic and Chemistry

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Abstract-Over the last decade, the environmental sciences have witnessed an incredible movement towards the utilization of highthroughput molecular tools that are capable of detecting simultaneous changes of hundreds, and even thousands, of molecules and molecular components after exposure of organisms to different environmental stressors. These techniques have received a great deal of attention because they not only offer the potential to unravel novel mechanisms of physiological and toxic action but are also amenable to the discovery of biomarkers of exposure and effects. In this article, we review the state of knowledge of one of these tools in ecotoxicological research: proteomics. We summarize the state of proteomics research in fish, and follow with studies conducted with aquatic invertebrates. A brief discussion on proteomic methods is also presented. We conclude with some ideas for future proteomic studies with fish and aquatic invertebrates. Environ. Toxicol. Chem. 2011;30:274-282. # 2010 SETAC

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Carbonylation and glutathionylation of proteins in the blue mussel Mytilus edulis detected by proteomic analysis and Western blotting: Actin as a target for oxidative stress

Cited by 115 publications

References 40 publications

Proteomic responses of blue mussel (Mytilus) congeners to temperature acclimation

Proteomic responses of blue mussel (Mytilus) congeners to temperature acclimation

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

Review of recent proteomic applications in aquatic toxicology

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