메뉴 건너뛰기




Volumn 157, Issue 1, 2009, Pages 199-207

B-type esterases in the snail Xeropicta derbentina: An enzymological analysis to evaluate their use as biomarkers of pesticide exposure

Author keywords

Carboxylesterase; Cholinesterase; Pesticides; Pralidoxime; Terrestrial snail

Indexed keywords

BIOMARKERS; CLIMATOLOGY; CONCENTRATION (PROCESS); INSECTICIDES; ORGANIC COMPOUNDS; WASTEWATER TREATMENT;

EID: 56449097158     PISSN: 02697491     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.envpol.2008.07.003     Document Type: Article
Times cited : (78)

References (48)
  • 1
    • 0343193275 scopus 로고
    • Serum esterases I
    • Aldridge W.N. Serum esterases I. Biochem. J. 53 (1953) 110-117
    • (1953) Biochem. J. , vol.53 , pp. 110-117
    • Aldridge, W.N.1
  • 2
    • 0001537321 scopus 로고
    • Two selective inhibitors of cholinesterase
    • Austin L., and Berry W.K. Two selective inhibitors of cholinesterase. Biochem. J. 54 (1953) 695-700
    • (1953) Biochem. J. , vol.54 , pp. 695-700
    • Austin, L.1    Berry, W.K.2
  • 4
    • 0001281608 scopus 로고
    • Organophosphorus poisoning: some properties of avian esterase
    • Bunyan P.J., and Jennings D.M. Organophosphorus poisoning: some properties of avian esterase. J. Agric. Food Chem. 16 (1968) 326-331
    • (1968) J. Agric. Food Chem. , vol.16 , pp. 326-331
    • Bunyan, P.J.1    Jennings, D.M.2
  • 5
    • 0026338509 scopus 로고
    • Acute effects of the organophosphate paraoxon on schedule-controlled behaviour and esterase activity in rats: dose-response relationships
    • Carr R.L., and Chambers J.E. Acute effects of the organophosphate paraoxon on schedule-controlled behaviour and esterase activity in rats: dose-response relationships. Pharmacol. Biochem. Behav. 40 (1991) 929-936
    • (1991) Pharmacol. Biochem. Behav. , vol.40 , pp. 929-936
    • Carr, R.L.1    Chambers, J.E.2
  • 6
    • 33746096936 scopus 로고    scopus 로고
    • In vitro characterization of cholinesterases in the earthworm Eisenia andrei
    • Caselli F., Gastaldi L., Gambi N., and Fabbri E. In vitro characterization of cholinesterases in the earthworm Eisenia andrei. Comp. Biochem. Physiol. Part C 143 (2006) 416-421
    • (2006) Comp. Biochem. Physiol. Part C , vol.143 , pp. 416-421
    • Caselli, F.1    Gastaldi, L.2    Gambi, N.3    Fabbri, E.4
  • 7
    • 26844516745 scopus 로고    scopus 로고
    • Tissue-specific effects of chlorpyrifos on carboxylesterase and cholinesterase activity in adult rats: an in vitro and in vivo comparison
    • Chanda S.M., Mortensen S.R., Moser V.C., and Padilla S. Tissue-specific effects of chlorpyrifos on carboxylesterase and cholinesterase activity in adult rats: an in vitro and in vivo comparison. Fundam. Appl. Toxicol. 38 (1997) 148-157
    • (1997) Fundam. Appl. Toxicol. , vol.38 , pp. 148-157
    • Chanda, S.M.1    Mortensen, S.R.2    Moser, V.C.3    Padilla, S.4
  • 9
    • 0033797064 scopus 로고    scopus 로고
    • Dose-dependent growth inhibition and bioaccumulation of hexavalent chromium in the land snail Helix aspersa
    • Coeurdassier M., Saint-Denis M., Gomot-de Vaufleury A., and Badot P.M. Dose-dependent growth inhibition and bioaccumulation of hexavalent chromium in the land snail Helix aspersa. Environ. Toxicol. Chem. 19 (2000) 2571-2578
    • (2000) Environ. Toxicol. Chem. , vol.19 , pp. 2571-2578
    • Coeurdassier, M.1    Saint-Denis, M.2    Gomot-de Vaufleury, A.3    Badot, P.M.4
  • 10
    • 0034884176 scopus 로고    scopus 로고
    • The garden snail (Helix aspersa) as a bioindicator of organophosphorus exposure: effects of dimethoate on survival, growth, and acetylcholinesterase activity
    • Coeurdassier M., Saint-Denis M., Gomot-de Vaufleury A., Ribera D., and Badot P.M. The garden snail (Helix aspersa) as a bioindicator of organophosphorus exposure: effects of dimethoate on survival, growth, and acetylcholinesterase activity. Environ. Toxicol. Chem. 20 9 (2001) 1951-1957
    • (2001) Environ. Toxicol. Chem. , vol.20 , Issue.9 , pp. 1951-1957
    • Coeurdassier, M.1    Saint-Denis, M.2    Gomot-de Vaufleury, A.3    Ribera, D.4    Badot, P.M.5
  • 11
    • 0342948637 scopus 로고    scopus 로고
    • Concentration effects of selected insecticides on brain acetylcholinesterase in the common carp (Cyprinus carpio L.)
    • Dembéle K., Haubruge E., and Gaspar C. Concentration effects of selected insecticides on brain acetylcholinesterase in the common carp (Cyprinus carpio L.). Ecotoxicol. Environ. Saf. 45 (2000) 49-54
    • (2000) Ecotoxicol. Environ. Saf. , vol.45 , pp. 49-54
    • Dembéle, K.1    Haubruge, E.2    Gaspar, C.3
  • 13
    • 0030823268 scopus 로고    scopus 로고
    • The use of cholinesterase and carboxylesterase activities from Mytilus galloprovincialis in pollution monitoring
    • Escartín E., and Porte C. The use of cholinesterase and carboxylesterase activities from Mytilus galloprovincialis in pollution monitoring. Environ. Toxicol. Chem. 16 (1997) 2090-2095
    • (1997) Environ. Toxicol. Chem. , vol.16 , pp. 2090-2095
    • Escartín, E.1    Porte, C.2
  • 14
    • 0031012688 scopus 로고    scopus 로고
    • Ecotoxicology for risk assessment in arid zones: some key issues
    • Everts J.W. Ecotoxicology for risk assessment in arid zones: some key issues. Arch. Environ. Contam. Toxicol. 32 (1997) 1-10
    • (1997) Arch. Environ. Contam. Toxicol. , vol.32 , pp. 1-10
    • Everts, J.W.1
  • 15
    • 33846160502 scopus 로고    scopus 로고
    • Cholinesterase response in native birds exposed to fenitrothion during locust control operations in Eastern Australia
    • Fildes K., Astheimer L.B., Story P., Buttemer W.A., and Hooper M.J. Cholinesterase response in native birds exposed to fenitrothion during locust control operations in Eastern Australia. Environ. Toxicol. Chem. 25 (2006) 2964-2970
    • (2006) Environ. Toxicol. Chem. , vol.25 , pp. 2964-2970
    • Fildes, K.1    Astheimer, L.B.2    Story, P.3    Buttemer, W.A.4    Hooper, M.J.5
  • 16
    • 0036258955 scopus 로고    scopus 로고
    • Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe)
    • Forget J., Livet S., and Leboulanger F. Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe). Comp. Biochem. Physiol. Part C 132 (2002) 85-92
    • (2002) Comp. Biochem. Physiol. Part C , vol.132 , pp. 85-92
    • Forget, J.1    Livet, S.2    Leboulanger, F.3
  • 17
    • 0035166230 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibition in estuarine fish and invertebrates as an indicator of organophosphorus insecticide exposure and effects
    • Fulton M.H., and Key P.B. Acetylcholinesterase inhibition in estuarine fish and invertebrates as an indicator of organophosphorus insecticide exposure and effects. Environ. Toxicol. Chem. 20 (2001) 37-45
    • (2001) Environ. Toxicol. Chem. , vol.20 , pp. 37-45
    • Fulton, M.H.1    Key, P.B.2
  • 18
    • 0033971279 scopus 로고    scopus 로고
    • Growing snails used as sentinels to evaluate terrestrial environment contamination by trace elements
    • Gomot-de Vaufleury A., and Pihan F. Growing snails used as sentinels to evaluate terrestrial environment contamination by trace elements. Chemosphere 40 (2000) 275-284
    • (2000) Chemosphere , vol.40 , pp. 275-284
    • Gomot-de Vaufleury, A.1    Pihan, F.2
  • 19
    • 0001274729 scopus 로고
    • Human esterases
    • Gomori G. Human esterases. J. Lab. Clin. Med. 42 (1953) 445-453
    • (1953) J. Lab. Clin. Med. , vol.42 , pp. 445-453
    • Gomori, G.1
  • 20
    • 0028161061 scopus 로고
    • Food preferences and dietary overlap by terrestrial snails in logos area (Edessa, Macedonia, Northern Greece)
    • Hatziioannou M., Eleutheriadis N., and Lazaridou-Dimitriadou M. Food preferences and dietary overlap by terrestrial snails in logos area (Edessa, Macedonia, Northern Greece). J. Molluscan Stud. 60 (1994) 331-341
    • (1994) J. Molluscan Stud. , vol.60 , pp. 331-341
    • Hatziioannou, M.1    Eleutheriadis, N.2    Lazaridou-Dimitriadou, M.3
  • 22
    • 33646510543 scopus 로고    scopus 로고
    • Inhibition of cholinesterase activity by azinphos-methyl in two freshwater invertebrates: Biomphalaria glabrata and Lumbriculus variegatus
    • Kristoff G., Verrangia Guerrero N., Pechén de d'Angelo A.M., and Cochon A. Inhibition of cholinesterase activity by azinphos-methyl in two freshwater invertebrates: Biomphalaria glabrata and Lumbriculus variegatus. Toxicology 222 (2006) 185-194
    • (2006) Toxicology , vol.222 , pp. 185-194
    • Kristoff, G.1    Verrangia Guerrero, N.2    Pechén de d'Angelo, A.M.3    Cochon, A.4
  • 24
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell M.A.K., Hass S.M., Bieber L.L., and Tolbert N.E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87 (1978) 206-210
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Hass, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 26
    • 0013300287 scopus 로고    scopus 로고
    • Carboxylesterases: specificity and spontaneous reacivation of an endogenous scavenger for organophosphorus compound
    • Maxwell D.M., and Brecht K.M. Carboxylesterases: specificity and spontaneous reacivation of an endogenous scavenger for organophosphorus compound. J. Appl. Toxicol. 21 (2001) S103-S107
    • (2001) J. Appl. Toxicol. , vol.21
    • Maxwell, D.M.1    Brecht, K.M.2
  • 28
    • 0034533080 scopus 로고    scopus 로고
    • Methodological and biological aspects to be considered in acetylcholinesterase reactivation assays using 2-PAM
    • Monserrat J.M., and Bianchini A. Methodological and biological aspects to be considered in acetylcholinesterase reactivation assays using 2-PAM. Environ. Toxicol. Pharmacol. 9 (2000) 39-47
    • (2000) Environ. Toxicol. Pharmacol. , vol.9 , pp. 39-47
    • Monserrat, J.M.1    Bianchini, A.2
  • 29
    • 0032759192 scopus 로고    scopus 로고
    • Cholinesterase activity as potential biomarker in two bivalves
    • Mora P., Michel X., and Narbonne J.F. Cholinesterase activity as potential biomarker in two bivalves. Environ. Toxicol. Pharmacol. 7 (1999) 253-260
    • (1999) Environ. Toxicol. Pharmacol. , vol.7 , pp. 253-260
    • Mora, P.1    Michel, X.2    Narbonne, J.F.3
  • 30
    • 0031881999 scopus 로고    scopus 로고
    • Comparison of the in vitro sensitivity of rat acetylcholinesterase to chlorpyrifos-oxon: what do tissue IC50 values represent?
    • Mortensen S.R., Brimijoin S., Hooper M.J., and Padilla S. Comparison of the in vitro sensitivity of rat acetylcholinesterase to chlorpyrifos-oxon: what do tissue IC50 values represent?. Toxicol. Appl. Pharmacol. 148 (1998) 46-49
    • (1998) Toxicol. Appl. Pharmacol. , vol.148 , pp. 46-49
    • Mortensen, S.R.1    Brimijoin, S.2    Hooper, M.J.3    Padilla, S.4
  • 31
    • 0037340115 scopus 로고    scopus 로고
    • Toxic effects of chlorpyrifos on morphology and acetylcholinesterase activity in the earthworm, Eisenia foetida
    • Rao J.V., Pavan Y.S., and Madhavendra S.S. Toxic effects of chlorpyrifos on morphology and acetylcholinesterase activity in the earthworm, Eisenia foetida. Ecotoxicol. Environ. Saf. 54 (2003) 296-301
    • (2003) Ecotoxicol. Environ. Saf. , vol.54 , pp. 296-301
    • Rao, J.V.1    Pavan, Y.S.2    Madhavendra, S.S.3
  • 32
    • 34548476284 scopus 로고    scopus 로고
    • Chemical reactivation and aging kinetics of organophosphorus-inhibited cholinesterases from two earthworm species
    • Rodriguez-Castellanos L., and Sanchez-Hernandez J.C. Chemical reactivation and aging kinetics of organophosphorus-inhibited cholinesterases from two earthworm species. Environ. Toxicol. Chem. 26 9 (2007) 1992-2000
    • (2007) Environ. Toxicol. Chem. , vol.26 , Issue.9 , pp. 1992-2000
    • Rodriguez-Castellanos, L.1    Sanchez-Hernandez, J.C.2
  • 33
    • 4344652673 scopus 로고    scopus 로고
    • Inhibition of plasma butyrylcholinesterase activity in the lizard Gallotia galloti palmae by pesticides: a field study
    • Sanchez-Hernandez J.C., Carbonell R., Henríquez Pérez A., Montealegre M., and Gómez L. Inhibition of plasma butyrylcholinesterase activity in the lizard Gallotia galloti palmae by pesticides: a field study. Environ. Pollut. 132 (2004) 479-488
    • (2004) Environ. Pollut. , vol.132 , pp. 479-488
    • Sanchez-Hernandez, J.C.1    Carbonell, R.2    Henríquez Pérez, A.3    Montealegre, M.4    Gómez, L.5
  • 34
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: from molecules to functions
    • Satoh T., and Hosokawa M. The mammalian carboxylesterases: from molecules to functions. Annu. Rev. Pharmacol. Toxicol. 38 (1998) 257-288
    • (1998) Annu. Rev. Pharmacol. Toxicol. , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 35
    • 0346034776 scopus 로고    scopus 로고
    • A field method using microcosms to evaluate transfer of Cd, Cu, Ni, Pb and Zn from sewage sludge amended forest soils to Helix aspersa snails
    • Scheifler R., Ben Brahim M., Gomot-de Vaufleury A., Carnus J.M., and Badot P.M. A field method using microcosms to evaluate transfer of Cd, Cu, Ni, Pb and Zn from sewage sludge amended forest soils to Helix aspersa snails. Environ. Pollut. 122 (2003) 343-350
    • (2003) Environ. Pollut. , vol.122 , pp. 343-350
    • Scheifler, R.1    Ben Brahim, M.2    Gomot-de Vaufleury, A.3    Carnus, J.M.4    Badot, P.M.5
  • 36
    • 0037051175 scopus 로고    scopus 로고
    • Enzymes involved in the detoxification of organophosphorus, carbamatos and pyrethroid insecticides through hydrolysis
    • Sogorb M.A., and Vilanova E. Enzymes involved in the detoxification of organophosphorus, carbamatos and pyrethroid insecticides through hydrolysis. Toxicol. Lett. 128 (2002) 215-228
    • (2002) Toxicol. Lett. , vol.128 , pp. 215-228
    • Sogorb, M.A.1    Vilanova, E.2
  • 37
    • 0032957197 scopus 로고    scopus 로고
    • Altered cholinesterase and monooxygenase levels in Daphnia magna and Chironomus riparius exposed to environmental pollutants
    • Sturm A., and Hansen P.D. Altered cholinesterase and monooxygenase levels in Daphnia magna and Chironomus riparius exposed to environmental pollutants. Ecotoxicol. Environ. Saf. 42 (1999) 9-15
    • (1999) Ecotoxicol. Environ. Saf. , vol.42 , pp. 9-15
    • Sturm, A.1    Hansen, P.D.2
  • 38
    • 0028968426 scopus 로고
    • Cholinesterase in Helix pomatia (Gastropoda: Stylommatophora): presence of a soluble (hemolymph) and a membrane-bound form
    • Talesa V., Grauso M., Principato G.B., Giovannini E., and Rosi G. Cholinesterase in Helix pomatia (Gastropoda: Stylommatophora): presence of a soluble (hemolymph) and a membrane-bound form. Comp. Biochem. Physiol. 110 3 (1995) 649-656
    • (1995) Comp. Biochem. Physiol. , vol.110 , Issue.3 , pp. 649-656
    • Talesa, V.1    Grauso, M.2    Principato, G.B.3    Giovannini, E.4    Rosi, G.5
  • 39
    • 77951877237 scopus 로고    scopus 로고
    • Biomarkers, bioindicators, and the Trondheim Biomonitoring System
    • Lehr J.H., and Keeley J. (Eds), John Wiley and Sons, Inc., NJ
    • Triebskorn R. Biomarkers, bioindicators, and the Trondheim Biomonitoring System. In: Lehr J.H., and Keeley J. (Eds). Water Encyclopedia: Water Quality and Resource Development (2005), John Wiley and Sons, Inc., NJ
    • (2005) Water Encyclopedia: Water Quality and Resource Development
    • Triebskorn, R.1
  • 40
    • 0037626992 scopus 로고    scopus 로고
    • Characterization of cholinesterase activity in three bivalves inhabiting the North Adriatic Sea and their possible use as sentinel organisms for biosurveillance programmes
    • Valbonesi P., Sartor G., and Fabbri E. Characterization of cholinesterase activity in three bivalves inhabiting the North Adriatic Sea and their possible use as sentinel organisms for biosurveillance programmes. Sci. Total Environ. 312 (2003) 79-88
    • (2003) Sci. Total Environ. , vol.312 , pp. 79-88
    • Valbonesi, P.1    Sartor, G.2    Fabbri, E.3
  • 41
    • 0037290663 scopus 로고    scopus 로고
    • Fish bioaccumulation and biomarkers in environmental risk assessment: a review
    • Van der Oost R., Beyer J., and Vermeulen N.P.E. Fish bioaccumulation and biomarkers in environmental risk assessment: a review. Environ. Toxicol. Pharmacol. 13 (2003) 57-149
    • (2003) Environ. Toxicol. Pharmacol. , vol.13 , pp. 57-149
    • Van der Oost, R.1    Beyer, J.2    Vermeulen, N.P.E.3
  • 42
    • 23844496906 scopus 로고
    • On the occurrence of a species of Xeropicta in France
    • Van Regteren Altena C.O. On the occurrence of a species of Xeropicta in France. Basteria 24 (1960) 21-26
    • (1960) Basteria , vol.24 , pp. 21-26
    • Van Regteren Altena, C.O.1
  • 43
    • 0037367981 scopus 로고    scopus 로고
    • Effect of dichlorvos on cholinesterase activity of the European sea bass (Dicentrarchus labrax)
    • Varo I., Navarro J.C., Amat F., and Guilhermino L. Effect of dichlorvos on cholinesterase activity of the European sea bass (Dicentrarchus labrax). Pestic. Biochem. Physiol. 75 (2003) 61-72
    • (2003) Pestic. Biochem. Physiol. , vol.75 , pp. 61-72
    • Varo, I.1    Navarro, J.C.2    Amat, F.3    Guilhermino, L.4
  • 45
    • 84953314429 scopus 로고    scopus 로고
    • Birds
    • Calow P. (Ed), Blackwell Science, Oxford, U.K
    • Walker C.H. Birds. In: Calow P. (Ed). Handbook of Ecotoxicology (1998), Blackwell Science, Oxford, U.K 326-338
    • (1998) Handbook of Ecotoxicology , pp. 326-338
    • Walker, C.H.1
  • 47
    • 0018823599 scopus 로고
    • Variables affecting body burdens of lead, zinc and cadmium in a road side population of the snail Cepaea hortensis Müller
    • Williamson P. Variables affecting body burdens of lead, zinc and cadmium in a road side population of the snail Cepaea hortensis Müller. Oecologia 44 (1980) 213-220
    • (1980) Oecologia , vol.44 , pp. 213-220
    • Williamson, P.1
  • 48
    • 0036288810 scopus 로고    scopus 로고
    • Acetylcholinesterase of the California red scale Aonidiella aurantii Mask.: catalysis, inhibition, and reactivation
    • Yerushalmi N., and Cohen E. Acetylcholinesterase of the California red scale Aonidiella aurantii Mask.: catalysis, inhibition, and reactivation. Pestic. Biochem. Physiol. 72 (2002) 133-141
    • (2002) Pestic. Biochem. Physiol. , vol.72 , pp. 133-141
    • Yerushalmi, N.1    Cohen, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.