Naslov
Effects of Cu and thermal stress on mussel's haemolymph proteins oxidation

Autori
Boatti, L, Peric, L, Olivieri, S, Sforzini, S, Viarengo, A

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY 163 (1) / - : Elsevier, 2012, S8-S9

Skup
28th Congress - European Society for Comparative Physiology and Biochemistry - Cellular and molecular mechanisms for physiological adaptation to multiple stress

Mjesto i datum
Bilbao, Španjolska, 02.09.2012. - 05.09.2012

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
mussels; copper; oxidative stress

Sažetak
Mussels (Mytilus sp) are sentinel organisms routinely used for monitoring the health status of coastal ecosystems. As known, mussel’s haemolymph contains secreted proteins the roles of which are poorly understood. Previous studies have demonstrated that among the haemolymph proteins the most abundant is the Extra pallial protein (EP) whose role seems to be related to shell calcification. Other proteins, such as lysozymes, are secreted from haemolymph cells having an immune activity. In this study we present results concerning the evaluation of oxidative stress in the haemolmyph protein of the mussels exposed to a sublethal Cu concentration at different increasing temperatures. Mussels were exposed for 4 days to Cu (40μg/L) of Cu at 16 and 24 °C. Haemolmyph proteins were flocculated in the presence of acetone or chloroform and analysed by SDS-PAGE electrophoresis. The chloroform precipitation allow us to recover a phase in which was clearly evident a shift from low to high in the molecular weight of some proteins. This fact was clearly demonstrated in the extracted from Cu-exposed mussels and was more evident at higher temperatures. The evaluation of protein carbonyl demonstrates that both thermal stress and Cu contribute to the increase in protein oxidation and to the molecular weight shift. The proteins that aggregate to give higher molecular weight products in stressed mussels were identified as EP protein by ESI MS MS TOF de novo sequencing. Due to the evident oxidative damage of the haemolymph proteins, the presence in the haemolymph of LDH (lactate dehydrogenase), a protein characteristic of the cytosol in the cells of the different tissue, was investigated. The results demonstrated that in Cu and temperature-stressed organisms, the activity of the LDH in the haemolymph is highly increased, reflecting serious damage to the cell plasma membranes in the different mussel tissues.

Izvorni jezik
Engleski

Znanstvena područja
Geologija

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