Organophosphate-resistant forms of acetylcholinesterases in two scallops-the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus
We describe the acetylcholinesterase polymorphisms of two bivalve molluscs, Adamussium colbecki and Pecten jacobaeus. The research was aimed to point out differences in the expression of pesticide-resistant acetylcholinesterase forms in organisms living in different ecosystems such as the Ross Sea (...
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ftuniperugiairis:oai:research.unipg.it:11391/108280 2023-09-05T13:12:54+02:00 Organophosphate-resistant forms of acetylcholinesterases in two scallops-the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus ROMANI, Rita DE MEDIO, Gianna Evelina GIOVANNINI, Elvio ROSI, Gabriella CORSI ILARIA BONACCI STEFANO FOCARDI SILVANO DE SANTIS ALESSANDRA INCARNATO FRANCESCA Romani, Rita Corsi, Ilaria Bonacci, Stefano Focardi, Silvano DE MEDIO, Gianna Evelina DE SANTIS, Alessandra Incarnato, Francesca Giovannini, Elvio Rosi, Gabriella 2006 http://hdl.handle.net/11391/108280 eng eng volume:145 issue:2 firstpage:188 lastpage:196 journal:COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. C. TOXICOLOGY & PHARMACOLOGY http://hdl.handle.net/11391/108280 Acetylcholinesterase Adamussium colbecki Azamethiphos Diisopropylfluorophosphate Membrane lipids Molecular forms Organophosphate resistance Pecten jacobaeus Polymorphisms info:eu-repo/semantics/article 2006 ftuniperugiairis 2023-08-13T20:21:10Z We describe the acetylcholinesterase polymorphisms of two bivalve molluscs, Adamussium colbecki and Pecten jacobaeus. The research was aimed to point out differences in the expression of pesticide-resistant acetylcholinesterase forms in organisms living in different ecosystems such as the Ross Sea (Antarctica) and the Mediterranean Sea. In A. colbecki, distinct acetylcholinesterase molecular forms were purified and characterized from spontaneously soluble, low-salt-soluble and low-salt-Triton extracts from adductor muscle and gills. They consist of two non-amphiphilic acetylcholinesterases (G2, G4) and an amphiphilic-phosphatidylinositol-membrane-anchored form (G2); a further amphiphilic-low-salt-soluble G2 acetylcholinesterase was found only in adductor muscle. In the corresponding tissues of P. jacobaeus, we found a non-amphiphilic G4 and an amphiphilic G2 acetylcholinesterase; amphiphilic-low-salt-soluble acetylcholinesterases (G2) are completely lacking. Such results are related with differences in cell membrane lipid compositions. In both scallops, all non-amphiphilic AChEs are resistant to used pesticides. Differently, the adductor muscle amphiphilic forms are resistant to carbamate eserine and organophosphate diisopropylfluorophosphate, but sensitive to organophoshate azamethiphos. In the gills of P. jacobaeus, amphiphilic G2 forms are sensitive to all three pesticides, while the corresponding forms of A. colbecki are sensitive to eserine and diisopropylfluorophosphate, but resistant to azamethiphos. Results indicate that organophosphate and/or carbamate resistant AChE forms are present in species living in far different and far away environments. The possibility that these AChE forms could have ensued from a common origin and have been spread globally by migration is discussed. Article in Journal/Newspaper Antarc* Antarctic Antarctica Ross Sea IRIS UniversitĂ degli Studi di Perugia Antarctic The Antarctic Ross Sea Triton ENVELOPE(-55.615,-55.615,49.517,49.517) |
institution |
Open Polar |
collection |
IRIS UniversitĂ degli Studi di Perugia |
op_collection_id |
ftuniperugiairis |
language |
English |
topic |
Acetylcholinesterase Adamussium colbecki Azamethiphos Diisopropylfluorophosphate Membrane lipids Molecular forms Organophosphate resistance Pecten jacobaeus Polymorphisms |
spellingShingle |
Acetylcholinesterase Adamussium colbecki Azamethiphos Diisopropylfluorophosphate Membrane lipids Molecular forms Organophosphate resistance Pecten jacobaeus Polymorphisms ROMANI, Rita DE MEDIO, Gianna Evelina GIOVANNINI, Elvio ROSI, Gabriella CORSI ILARIA BONACCI STEFANO FOCARDI SILVANO DE SANTIS ALESSANDRA INCARNATO FRANCESCA Organophosphate-resistant forms of acetylcholinesterases in two scallops-the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus |
topic_facet |
Acetylcholinesterase Adamussium colbecki Azamethiphos Diisopropylfluorophosphate Membrane lipids Molecular forms Organophosphate resistance Pecten jacobaeus Polymorphisms |
description |
We describe the acetylcholinesterase polymorphisms of two bivalve molluscs, Adamussium colbecki and Pecten jacobaeus. The research was aimed to point out differences in the expression of pesticide-resistant acetylcholinesterase forms in organisms living in different ecosystems such as the Ross Sea (Antarctica) and the Mediterranean Sea. In A. colbecki, distinct acetylcholinesterase molecular forms were purified and characterized from spontaneously soluble, low-salt-soluble and low-salt-Triton extracts from adductor muscle and gills. They consist of two non-amphiphilic acetylcholinesterases (G2, G4) and an amphiphilic-phosphatidylinositol-membrane-anchored form (G2); a further amphiphilic-low-salt-soluble G2 acetylcholinesterase was found only in adductor muscle. In the corresponding tissues of P. jacobaeus, we found a non-amphiphilic G4 and an amphiphilic G2 acetylcholinesterase; amphiphilic-low-salt-soluble acetylcholinesterases (G2) are completely lacking. Such results are related with differences in cell membrane lipid compositions. In both scallops, all non-amphiphilic AChEs are resistant to used pesticides. Differently, the adductor muscle amphiphilic forms are resistant to carbamate eserine and organophosphate diisopropylfluorophosphate, but sensitive to organophoshate azamethiphos. In the gills of P. jacobaeus, amphiphilic G2 forms are sensitive to all three pesticides, while the corresponding forms of A. colbecki are sensitive to eserine and diisopropylfluorophosphate, but resistant to azamethiphos. Results indicate that organophosphate and/or carbamate resistant AChE forms are present in species living in far different and far away environments. The possibility that these AChE forms could have ensued from a common origin and have been spread globally by migration is discussed. |
author2 |
Romani, Rita Corsi, Ilaria Bonacci, Stefano Focardi, Silvano DE MEDIO, Gianna Evelina DE SANTIS, Alessandra Incarnato, Francesca Giovannini, Elvio Rosi, Gabriella |
format |
Article in Journal/Newspaper |
author |
ROMANI, Rita DE MEDIO, Gianna Evelina GIOVANNINI, Elvio ROSI, Gabriella CORSI ILARIA BONACCI STEFANO FOCARDI SILVANO DE SANTIS ALESSANDRA INCARNATO FRANCESCA |
author_facet |
ROMANI, Rita DE MEDIO, Gianna Evelina GIOVANNINI, Elvio ROSI, Gabriella CORSI ILARIA BONACCI STEFANO FOCARDI SILVANO DE SANTIS ALESSANDRA INCARNATO FRANCESCA |
author_sort |
ROMANI, Rita |
title |
Organophosphate-resistant forms of acetylcholinesterases in two scallops-the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus |
title_short |
Organophosphate-resistant forms of acetylcholinesterases in two scallops-the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus |
title_full |
Organophosphate-resistant forms of acetylcholinesterases in two scallops-the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus |
title_fullStr |
Organophosphate-resistant forms of acetylcholinesterases in two scallops-the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus |
title_full_unstemmed |
Organophosphate-resistant forms of acetylcholinesterases in two scallops-the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus |
title_sort |
organophosphate-resistant forms of acetylcholinesterases in two scallops-the antarctic adamussium colbecki and the mediterranean pecten jacobaeus |
publishDate |
2006 |
url |
http://hdl.handle.net/11391/108280 |
long_lat |
ENVELOPE(-55.615,-55.615,49.517,49.517) |
geographic |
Antarctic The Antarctic Ross Sea Triton |
geographic_facet |
Antarctic The Antarctic Ross Sea Triton |
genre |
Antarc* Antarctic Antarctica Ross Sea |
genre_facet |
Antarc* Antarctic Antarctica Ross Sea |
op_relation |
volume:145 issue:2 firstpage:188 lastpage:196 journal:COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. C. TOXICOLOGY & PHARMACOLOGY http://hdl.handle.net/11391/108280 |
_version_ |
1776202315734188032 |