Adaptation of the cholinergic system of Crenomytilus grayanus (Bivalvia, Mytilidae) to the impact of natural and anthropogenic conditions

Kavun, V. Ya.; Chepkasova, A. I.; Podgurskaya, O. V.; Kovalev, N. F.

doi:10.1134/s1062359010061019

Cited by 4 publications

(1 citation statement)

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“…The results of the studies of activity and sensitivity towards organophosphorus inhibitors that is manifested by ChE from the gills, adductor muscles, foot, and digestive gland of Mytilus edulis, as well as the information on sub cellular distribution of this enzyme, have been published [20,21]. However, data on the properties of ChE in the hemolymph of bivalves are fragmentary [6,9,27]. Nev ertheless, the highest activity of this enzyme has been recorded from bivalve hemolymph [13].…”

Section: Introductionmentioning

confidence: 99%

Hemolymph cholinesterase activity in the Mussel Crenomytilus grayanus (Dunker, 1853) that was exposed to adverse natural and anthropogenic conditions

et al. 2016

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The influence of habitat conditions on the activity, the structure of the substrate specificity (the ratio of the substrate hydrolysis rates), and the kinetic parameters of substrate hydrolysis due to the effect of hemolymph cholinesterase of the mussel Crenomytilus grayanus was studied. Mussels were collected from areas that are influenced by seasonal and stationary upwelling, as well as from a polluted area. Upwelling and anthropogenic pressure were shown to alter the structure of hemolymph cholinesterase substrate specificity in mussels, up to complete loss of the ability to catalyze the hydrolysis of propionyl and butyrylthiocholine. It was established that during the seasonal upwelling the efficiency of the cholinergic process in mussels is provided by a wide range of effective concentrations of the substrates and by decreasing their affinity to the enzyme. Under the conditions of chronic anthropogenic pollution, the cholinesterase of the mussel hemolymph loses its ability to hydrolyze substrates other than acetylthiocholine.

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