Response to alkyltins of two Na+-dependent ATPase activities in Tapes philippinarum and Mytilus galloprovincialis.

Alessandra Pagliarani, Patrizia Bandiera, Vittoria Ventrella, Fabiana Trombetti, Maurizio Pirini, Anna Rosa Borgatti

Index: Toxicol. In Vitro 20(7) , 1145-53, (2006)

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Abstract

Organotin effects on the Na-dependent ATPases involved in ionic regulation of aquatic animals are poorly known, in spite of the largely documented contamination of seafood, especially bivalve molluscs. This study deals with the in vitro effect of TBT on the Na,K-ATPase and the ouabain-insensitive Na-ATPase in gill and mantle microsomes from the cultured bivalve molluscs Tapes philippinarum and Mytilus galloprovincialis. In the mussel also MBT, DBT and TeET were tested. While in both species the Na-ATPase showed an overall refractoriness to organotins, the Na,K-ATPase was progressively inhibited by increasing TBT concentrations (0-34 microM). In both species the Na,K-ATPase activity was more strongly inhibited in the gills than in the mantle. At the maximal TBT concentration tested (34.4 microM), while gill Na,K-ATPase activity was abolished, mantle enzyme activity was, respectively, reduced to 20% in T. philippinarum and to 50% in M. galloprovincialis. Mussel Na,K-ATPase was differently susceptive to the organotins tested and in both tissues showed an inhibition efficiency order TBT>DBT>>MBT=TeET (no effect), tentatively related to the different organotin polarity and to a possible interaction with membrane-bound enzyme complexes. The different response of the two ATPases to organotins is consistent with the known different susceptivity of the two enzyme activities to environmental contaminants, assay conditions and endogenous factors.