Studies on glutathione S-transferase in molluscs

Balabaskaran, Shanmuoam; Chew, Sophie; Muniandy, Sekaran

doi:10.1016/0305-0491(86)90241-5

Cited by 15 publications

(9 citation statements)

References 24 publications

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“…Only a few studies have investigated the occurrence of xenobiotic-metabolizing enzymes [55,[56][57][58] and the effects of environmental contaminants on their activities [59][60][61][62] in freshwater molluscs. The opportunity of using biotransformation enzymes (e.g., microsomal monooxygenases and GSTs) as biomarkers of chemical stress in these organisms therefore remained to be explored.…”

Section: Discussionmentioning

confidence: 99%

BENZO[a]PYRENE HYDROXYLASE AND GLUTATHIONE S-TRANSFERASE ACTIVITIES AS BIOMARKERS IN LYMNAEA PALUSTRIS (MOLLUSCA, GASTROPODA) EXPOSED TO ATRAZINE AND HEXACHLOROBENZENE IN FRESHWATER MESOCOSMS

Baturo¹,

Lagadic²

1996

Environ Toxicol Chem

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Abstract-Freshwater pond mesocosms were used to validate xenobiotic-metabolizing enzymes as biomarkers of contamination by atrazine and hexachlorobenzene (HCB) in a basommatophoran gastropod, Lymnaea palustris (Müller). Over long-term (21-d) exposure to 5, 25, and 125 g/L atrazine and to 0.5, 1.25, and 5 g/L HCB, the uptake and internal concentration of both pesticides were followed, and the activities of benzo[a]pyrene hydroxylase (BaPH) and glutathione S-transferases (GSTs) of pesticide-exposed snails were compared with those of control animals maintained in untreated mesocosms. Internally recovered HCB concentrations were much higher than internal atrazine concentrations, but the uptake of atrazine was faster than that of HCB. Although it affected the integrity of microsomal membranes, HCB had no relevant effects on BaPH and GST activities at concentrations which affected growth and fecundity, thus confirming the low inducibility of mollusc xenobiotic-metabolizing enzymes by chlorinated compounds. In contrast, atrazine markedly inhibited BaPH and both postmitochondrial and cytosolic GSTs at the same concentrations, which had no effects on growth or reproduction. Enzyme inhibition was negatively correlated with the maximal internal amount of atrazine and positively correlated with the bioconcentration factor, suggesting that effects on xenobiotic-metabolizing enzymes may affect pharmacokinetics of atrazine within the snail body. Correlation between the bioconcentration factor and enzyme inhibition may serve as a descriptor of the physiological status of animals and can also be used to indirectly estimate the pesticide concentration in the environment. Laboratory data were considered for the interpretation of results obtained in the mesocosms. In the biomarker context, BaPH and GST activities are proposed, along with other biochemical markers already identified in atrazine-and HCB-exposed L. palustris, as elements of a multiparametric approach of the ecotoxicological effects of pesticides on freshwater ecosystems.

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Section: Discussionmentioning

confidence: 99%

BENZO[a]PYRENE HYDROXYLASE AND GLUTATHIONE S-TRANSFERASE ACTIVITIES AS BIOMARKERS IN LYMNAEA PALUSTRIS (MOLLUSCA, GASTROPODA) EXPOSED TO ATRAZINE AND HEXACHLOROBENZENE IN FRESHWATER MESOCOSMS

Baturo¹,

Lagadic²

1996

Environ Toxicol Chem

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“…Toxic electrophiles found in marine waters include a variety of xenobiotics, such as the organophosphorus insecticides. GST occurs in cytosol of tissues in a number of marine invertebrates (Tate & Herf 1978, James et al 1979, Balabaskaran et al 1986.…”

Section: Introductionmentioning

confidence: 99%

Glutathione S-transferase in marine invertebrates from Langesundfjord

Lee¹

1988

Mar. Ecol. Prog. Ser.

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Glutathione S-transferase (GST), an enzyme system which conjugates glutathione to a vanety of xenobiotics with electrophllic centres was found dunng the GEEP Workshop m the digesbve glands of the s n d httorina httorea and the mussel Myllus edulis, and in the hepatopancreas of the crab Carcinus maenas GST activity was significantly higher in crabs from 2 polluted sites m Langesundfjord Norway relative to reference-slte crabs but no such differences were found for n~ussels in spite of large differences In PAH and PCB hssue concentrations between the sites In a mesocosm expenment lnvolvlng diesel 011 and copper doslng no significant effects were observed on crab and mussel GST acbvlty though L httorea showed sign~flcantly higher GST activ~ty at the highest contaminant dose Slnce few studles have been done on GST induchon In manne invertebrates it is not clear how dfferences In GST achvlty In crabs from the field sites can be related to the pollutants present

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“…It appears that B. globosus expresses only neutral GST isozymes, as there was no detectable GST activity in the fractions obtained when a KCl gradient of up to 1.0M was used to elute bound proteins on both the anion and cation-exchange columns. Th e concentration of GST in the hepatopancreas of this organism, especially when the organism is under aestivation is quite high with a specifi c activity of 1.3 units/mg protein which is four times higher than the specifi c activity of a comparable extract from land snail Archachatina maginata (0.36 units/mg protein; Ajele and Afolayan, 1992 ), and between 4 to 50 times higher than crude GST extract in a range of molluscsfrom fresh water, marine or terrestrial (Balabaskaran, et al , 1986); It is also higher than crude GST extracts from many invertebrates e.g grasshopper-Zonocerus variegatus (0.049 units/mg protein), river prawn-Macrobrachium vollenhovenii (0.29 units/mg protein), aphids-Aulacorthum solani (0.06 units/mg protein) and Acyrthosiphon pisum (0.12 units/mg protein), to name but a few (Adewale and Afolayan, 2006 ;Adewale and Afolayan, 2004 ;Francis et al , 2001 ). However the molecular weight of 41.5 kDa is within the range previously established for other cytosolic GST isoenzymes.…”

Section: Discussionmentioning

confidence: 90%

“…Th ese include the giant African land snail, Archachatina maginata (Ajele and Afolayan, 1992 ) and Achatina fulica (Balabaskaran and Segaran, 1986). Abdalla et al , ( 2006 ) have also recently showed the presence and some properties of GST in Bulinus truncatus a related species of Bulinus globosus .…”

Section: Introductionmentioning

confidence: 99%

Alteration in the status of glutathione transferase of the water snail, Bulinus globosus, during aestivation and recovery

Adewale

Ojopagogo

2010

Animal Biol

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Th e varying status of glutathione transferases (GSTs) in water snail, Bulinus globosus , an intermediate host of disease-causing Schistosoma haematobium (Bilharz 1852) has been investigated. Th e expression of GST isoenzymes in the water snail appears seasonal with about three isoenzymes appearing during raining season, when the organism is active, which may reduce to a single peak of one isoenzyme during aestivation, when the organism is inactive. GST isoenzyme is present in high concentration in all the tissues investigated namely: haemolymph, foot muscle and hepatopancreas with specifi c activities of 0.006 ± 0.002, 0.45 ± 0.021 and 1.33 ± 0.103 units/mg protein respectively for 1-chloro-2,4-dinitrobenzene (CDNB) as substrate. With this substrate, the specifi c activity of GST from the hepatopancreas appears higher than the specifi c activities that have been previously reported for GSTs from molluscs. Partial purifi cation of the isoenzymes using Tris acrylic acid-based resins enabled us to observe that GST appears to be the major protein in the hepatopancreas of this organism. We also found indications for the presence of an endogenous GST inhibitor in the cytosol, whose function is yet unknown. All the traditional GST inhibitors such as cibacron blue, hematin, bromosulfophthalein and S-hexylglutathione were able to inhibit the isoenzymes eff ectively, with cibacron blue being the most potent. Th e isoenzymes however have narrow substrate specifi city. We conclude that diff erent isoenzymes of GST are expressed in the same class of molluscs, even when they belong to the same genus or species, and that the expression may depend on whether the snails are on aestivation or not.

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Studies on glutathione S-transferase in molluscs

Cited by 15 publications

References 24 publications

BENZO[a]PYRENE HYDROXYLASE AND GLUTATHIONE S-TRANSFERASE ACTIVITIES AS BIOMARKERS IN LYMNAEA PALUSTRIS (MOLLUSCA, GASTROPODA) EXPOSED TO ATRAZINE AND HEXACHLOROBENZENE IN FRESHWATER MESOCOSMS

BENZO[a]PYRENE HYDROXYLASE AND GLUTATHIONE S-TRANSFERASE ACTIVITIES AS BIOMARKERS IN LYMNAEA PALUSTRIS (MOLLUSCA, GASTROPODA) EXPOSED TO ATRAZINE AND HEXACHLOROBENZENE IN FRESHWATER MESOCOSMS

Glutathione S-transferase in marine invertebrates from Langesundfjord

Alteration in the status of glutathione transferase of the water snail, Bulinus globosus, during aestivation and recovery

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