In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: Analysis of enzyme, substrate and tissue dependence
Cholinesterases and carboxylesterases belong to the group of B-esterases, the serine superfamily of esterases that are inhibited by organophosphorus compounds. It is now generally accepted that before using the B-esterases as biomarkers of exposure to organophosphorus and carbamates in a given speci...
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| Publicado: |
2012
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0166445X_v112-113_n_p19_Kristoff http://hdl.handle.net/20.500.12110/paper_0166445X_v112-113_n_p19_Kristoff |
| Aporte de: |
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paper:paper_0166445X_v112-113_n_p19_Kristoff |
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dspace |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Azinphos-methyl Biomphalaria glabrata Carboxylesterases Cholinesterases Freshwater invertebrate Pesticides 1 naphthyl acetate 2 naphthyl acetate 4 nitrophenyl acetate acetic acid derivative acetylthiocholine azinphos methyl butyric acid 4 nitrophenyl ester butyric acid derivative butyrylthiocholine carboxylesterase choline derivative cholinesterase propionylthiocholine unclassified drug bioaccumulation biomarker carbamate (ester) enzyme activity inhibition insecticide organophosphate pollution exposure snail substrate animal experiment animal tissue article Biomphalaria glabrata concentration response controlled study environmental exposure enzyme activity enzyme analysis enzyme inhibition enzyme kinetics enzyme specificity enzyme substrate complex exocrine gland gonad in vivo study lung nonhuman physical sensitivity priority journal protein hydrolysis soft tissue tissue specificity Animals Azinphosmethyl Biomphalaria Carboxylesterase Cholinesterases Enzyme Activation Water Pollutants, Chemical Biomphalaria glabrata Gastropoda Invertebrata |
| spellingShingle |
Azinphos-methyl Biomphalaria glabrata Carboxylesterases Cholinesterases Freshwater invertebrate Pesticides 1 naphthyl acetate 2 naphthyl acetate 4 nitrophenyl acetate acetic acid derivative acetylthiocholine azinphos methyl butyric acid 4 nitrophenyl ester butyric acid derivative butyrylthiocholine carboxylesterase choline derivative cholinesterase propionylthiocholine unclassified drug bioaccumulation biomarker carbamate (ester) enzyme activity inhibition insecticide organophosphate pollution exposure snail substrate animal experiment animal tissue article Biomphalaria glabrata concentration response controlled study environmental exposure enzyme activity enzyme analysis enzyme inhibition enzyme kinetics enzyme specificity enzyme substrate complex exocrine gland gonad in vivo study lung nonhuman physical sensitivity priority journal protein hydrolysis soft tissue tissue specificity Animals Azinphosmethyl Biomphalaria Carboxylesterase Cholinesterases Enzyme Activation Water Pollutants, Chemical Biomphalaria glabrata Gastropoda Invertebrata Kristoff, Gisela Verrengia Guerrero, Noemí Rosario Cochón, Adriana Cristina In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: Analysis of enzyme, substrate and tissue dependence |
| topic_facet |
Azinphos-methyl Biomphalaria glabrata Carboxylesterases Cholinesterases Freshwater invertebrate Pesticides 1 naphthyl acetate 2 naphthyl acetate 4 nitrophenyl acetate acetic acid derivative acetylthiocholine azinphos methyl butyric acid 4 nitrophenyl ester butyric acid derivative butyrylthiocholine carboxylesterase choline derivative cholinesterase propionylthiocholine unclassified drug bioaccumulation biomarker carbamate (ester) enzyme activity inhibition insecticide organophosphate pollution exposure snail substrate animal experiment animal tissue article Biomphalaria glabrata concentration response controlled study environmental exposure enzyme activity enzyme analysis enzyme inhibition enzyme kinetics enzyme specificity enzyme substrate complex exocrine gland gonad in vivo study lung nonhuman physical sensitivity priority journal protein hydrolysis soft tissue tissue specificity Animals Azinphosmethyl Biomphalaria Carboxylesterase Cholinesterases Enzyme Activation Water Pollutants, Chemical Biomphalaria glabrata Gastropoda Invertebrata |
| description |
Cholinesterases and carboxylesterases belong to the group of B-esterases, the serine superfamily of esterases that are inhibited by organophosphorus compounds. It is now generally accepted that before using the B-esterases as biomarkers of exposure to organophosphorus and carbamates in a given species, the biochemical characteristics of these enzymes should be carefully studied. In this study, the enzyme/s and the tissue/s to be selected as sensitive biomarkers of organophosphorus exposition in the freshwater gastropod Biomphalaria glabrata were investigated. Firstly, the substrate dependence of cholinesterase and carboxylesterase activities in whole organism soft tissue and in different tissues of the snail (head-foot, pulmonary region, digestive gland, and gonads) was analyzed. Measurements of cholinesterase activity were performed using three substrates: acetylthiocholine (AcSCh), propionylthiocholine (PrSCh), and butyrylthiocholine (BuSCh). Carboxylesterase activity was determined using four different substrates: 1-naphthyl acetate (1-NA), 2-naphthyl acetate (2-NA), p-nitrophenyl acetate (p-NPA), and p-nitrophenyl butyrate (p-NPB). Regardless of the tissue analyzed, the highest specific activity was obtained when using AcSCh, followed by PrSCh. Cholinesterase activity measured with BuSCh was very low in all cases. On the other hand, the highest cholinesterase activity was measured in head-foot and in pulmonary region, representing in the case of AcSCh hydrolysis 196% and 180% of the activity measured in whole organism soft tissue, respectively. In contrast, AcSCh hydrolysis in digestive gland and gonads was 28% and 50% of that measured in whole organism soft tissue. Regarding carboxylesterase activity, although all tissues hydrolyzed the four substrates assayed, substrate preferences varied among tissues. In particular, digestive glands showed higher carboxylesterase activity than the other tissues (299%, 359% and 137% of whole organism soft tissue activity) when measured with 1-NA, 2-NA and p-NPA as substrates, respectively. In contrast, with p-NPB as substrate, the highest carboxylesterase activity was observed in pulmonary region. Exposure of the snails for 48h to azinphos-methyl concentrations in the range of 0.05-2.5mgL -1 resulted in different degrees of inhibition of cholinesterase and carboxylesterase activities, depending on the enzyme, pesticide concentration, the substrate, and the tissue analyzed. In general, carboxylesterase activity measured with p-NPA and p-NPB was much more sensitive to azinphos-methyl inhibition than cholinesterase activity. The results also showed that while B-esterase activities in whole organism soft tissue and pulmonary region recovered completely within 14 days, carboxylesterase activity in digestive glands remained highly inhibited. On the whole, the results of the present study emphasize how important it is to characterize and measure cholinesterase and carboxylesterase activities jointly to make a proper assessment of the impact of organophosphorus pesticides in non-target species. © 2012 Elsevier B.V.. |
| author |
Kristoff, Gisela Verrengia Guerrero, Noemí Rosario Cochón, Adriana Cristina |
| author_facet |
Kristoff, Gisela Verrengia Guerrero, Noemí Rosario Cochón, Adriana Cristina |
| author_sort |
Kristoff, Gisela |
| title |
In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: Analysis of enzyme, substrate and tissue dependence |
| title_short |
In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: Analysis of enzyme, substrate and tissue dependence |
| title_full |
In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: Analysis of enzyme, substrate and tissue dependence |
| title_fullStr |
In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: Analysis of enzyme, substrate and tissue dependence |
| title_full_unstemmed |
In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: Analysis of enzyme, substrate and tissue dependence |
| title_sort |
in vivo studies on inhibition and recovery of b-esterase activities in biomphalaria glabrata exposed to azinphos-methyl: analysis of enzyme, substrate and tissue dependence |
| publishDate |
2012 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0166445X_v112-113_n_p19_Kristoff http://hdl.handle.net/20.500.12110/paper_0166445X_v112-113_n_p19_Kristoff |
| work_keys_str_mv |
AT kristoffgisela invivostudiesoninhibitionandrecoveryofbesteraseactivitiesinbiomphalariaglabrataexposedtoazinphosmethylanalysisofenzymesubstrateandtissuedependence AT verrengiaguerreronoemirosario invivostudiesoninhibitionandrecoveryofbesteraseactivitiesinbiomphalariaglabrataexposedtoazinphosmethylanalysisofenzymesubstrateandtissuedependence AT cochonadrianacristina invivostudiesoninhibitionandrecoveryofbesteraseactivitiesinbiomphalariaglabrataexposedtoazinphosmethylanalysisofenzymesubstrateandtissuedependence |
| _version_ |
1768544773379981312 |
| spelling |
paper:paper_0166445X_v112-113_n_p19_Kristoff2023-06-08T15:15:45Z In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: Analysis of enzyme, substrate and tissue dependence Kristoff, Gisela Verrengia Guerrero, Noemí Rosario Cochón, Adriana Cristina Azinphos-methyl Biomphalaria glabrata Carboxylesterases Cholinesterases Freshwater invertebrate Pesticides 1 naphthyl acetate 2 naphthyl acetate 4 nitrophenyl acetate acetic acid derivative acetylthiocholine azinphos methyl butyric acid 4 nitrophenyl ester butyric acid derivative butyrylthiocholine carboxylesterase choline derivative cholinesterase propionylthiocholine unclassified drug bioaccumulation biomarker carbamate (ester) enzyme activity inhibition insecticide organophosphate pollution exposure snail substrate animal experiment animal tissue article Biomphalaria glabrata concentration response controlled study environmental exposure enzyme activity enzyme analysis enzyme inhibition enzyme kinetics enzyme specificity enzyme substrate complex exocrine gland gonad in vivo study lung nonhuman physical sensitivity priority journal protein hydrolysis soft tissue tissue specificity Animals Azinphosmethyl Biomphalaria Carboxylesterase Cholinesterases Enzyme Activation Water Pollutants, Chemical Biomphalaria glabrata Gastropoda Invertebrata Cholinesterases and carboxylesterases belong to the group of B-esterases, the serine superfamily of esterases that are inhibited by organophosphorus compounds. It is now generally accepted that before using the B-esterases as biomarkers of exposure to organophosphorus and carbamates in a given species, the biochemical characteristics of these enzymes should be carefully studied. In this study, the enzyme/s and the tissue/s to be selected as sensitive biomarkers of organophosphorus exposition in the freshwater gastropod Biomphalaria glabrata were investigated. Firstly, the substrate dependence of cholinesterase and carboxylesterase activities in whole organism soft tissue and in different tissues of the snail (head-foot, pulmonary region, digestive gland, and gonads) was analyzed. Measurements of cholinesterase activity were performed using three substrates: acetylthiocholine (AcSCh), propionylthiocholine (PrSCh), and butyrylthiocholine (BuSCh). Carboxylesterase activity was determined using four different substrates: 1-naphthyl acetate (1-NA), 2-naphthyl acetate (2-NA), p-nitrophenyl acetate (p-NPA), and p-nitrophenyl butyrate (p-NPB). Regardless of the tissue analyzed, the highest specific activity was obtained when using AcSCh, followed by PrSCh. Cholinesterase activity measured with BuSCh was very low in all cases. On the other hand, the highest cholinesterase activity was measured in head-foot and in pulmonary region, representing in the case of AcSCh hydrolysis 196% and 180% of the activity measured in whole organism soft tissue, respectively. In contrast, AcSCh hydrolysis in digestive gland and gonads was 28% and 50% of that measured in whole organism soft tissue. Regarding carboxylesterase activity, although all tissues hydrolyzed the four substrates assayed, substrate preferences varied among tissues. In particular, digestive glands showed higher carboxylesterase activity than the other tissues (299%, 359% and 137% of whole organism soft tissue activity) when measured with 1-NA, 2-NA and p-NPA as substrates, respectively. In contrast, with p-NPB as substrate, the highest carboxylesterase activity was observed in pulmonary region. Exposure of the snails for 48h to azinphos-methyl concentrations in the range of 0.05-2.5mgL -1 resulted in different degrees of inhibition of cholinesterase and carboxylesterase activities, depending on the enzyme, pesticide concentration, the substrate, and the tissue analyzed. In general, carboxylesterase activity measured with p-NPA and p-NPB was much more sensitive to azinphos-methyl inhibition than cholinesterase activity. The results also showed that while B-esterase activities in whole organism soft tissue and pulmonary region recovered completely within 14 days, carboxylesterase activity in digestive glands remained highly inhibited. On the whole, the results of the present study emphasize how important it is to characterize and measure cholinesterase and carboxylesterase activities jointly to make a proper assessment of the impact of organophosphorus pesticides in non-target species. © 2012 Elsevier B.V.. Fil:Kristoff, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Verrengia Guerrero, N.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cochón, A.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0166445X_v112-113_n_p19_Kristoff http://hdl.handle.net/20.500.12110/paper_0166445X_v112-113_n_p19_Kristoff |