Different expressions of organophosphate-resistant acetylcholinesterases in the bivalve mollusk Scapharca inaequivalvis living in three different habitats

The benthic mollusk Scapharca inaequivalvis was collected in spring 1999 from three areas of the northern Adriatic Sea. From the mollusk, molecular forms of acetylcholinesterase (AChE), consisting of two prevailing spontaneously soluble (SS) forms present in the blood, were obtained. These forms are...

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Bibliographic Details
Published in:Environmental toxicology and chemistry 2002-01, Vol.21 (1), p.102-108
Main Authors: Talesa, Vincenzo, Romani, Rita, Antognelli, Cinzia, Giovannini, Elvio, Rosi, Gabriella
Format: Article
Language:English
Subjects:
Acetylcholinesterase
Acetylcholinesterase - chemistry
Acetylcholinesterase - metabolism
Adriatic Sea
Animal, plant and microbial ecology
Animals
Applied ecology
Biological and medical sciences
Bivalvia
Centrifugation, Density Gradient
Cholinesterase Inhibitors - pharmacology
Chromatography, Affinity
Drug Resistance
Ecotoxicology, biological effects of pollution
Effects of pollution and side effects of pesticides on protozoa and invertebrates
Environmental Monitoring
Fundamental and applied biological sciences. Psychology
Isoflurophate - pharmacology
Marine
Mollusca - drug effects
Mollusca - enzymology
Mollusk monitoring
Northern
Organophosphate
Organophosphate resistance
Scapharca inaequivalvis
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Summary:The benthic mollusk Scapharca inaequivalvis was collected in spring 1999 from three areas of the northern Adriatic Sea. From the mollusk, molecular forms of acetylcholinesterase (AChE), consisting of two prevailing spontaneously soluble (SS) forms present in the blood, were obtained. These forms are a globular tetramer (SSG4), a dimer (SSG2) of catalytic subunits, and a minor amphiphilic globular dimer (low‐salt Triton [LST] G2) phosphatidylinositol tailed. All SS and LST forms, partially purified by affinity chromatography, are AChEs with a marked substrate specificity for acetylthiocholine and poor hydrolysis with butyrylthiocholine. They are poorly inhibited by carbamate eserine and show a different pattern of inhibition by organophosphate diisopropylfluorophosphate (DFP), with totally resistant SS forms from clams collected from the two stations nearest the Po River. Acetylcholinesterase SS and LST forms are expressed at highest, lowest, and middle levels in clams collected from the northern station, closer to the Po delta, and from the two more southern ones, respectively. The possibility that the expression pattern of AChE forms is due to effects of single or mixed classes of chemical pollutants is discussed.
ISSN:0730-7268
1552-8618
DOI:10.1002/etc.5620210115