Commenced in January 2007
Frequency: Monthly
Edition: International
Paper Count: 3

GST Related Abstracts

3 Evaluation of Acetylcholinesterase, Glutathione S-Transferase and Catalase Activities in the Land Snail Helix aspersa Exposed to Thiamethoxam

Authors: Ait Hamlet Smina, Bensoltane Samira, Djekoun Mohamed, Berrebbah Houria

Abstract:

In Algeria, the use of insecticides and other phytosanitary products are considerably spreading with the development of agriculture. But, the analyses of the residues of pesticides are not systematically made. In this context, we estimated through an experimental study, the effect of a neonicotinoid insecticide, the thiamethoxam which is used as a commercial preparation on the land snail Helix aspersa. This snail is one of the most abundant gastropod in North-East Algeria. Little information is available in the literature concerning the study of the biochemical markers of mollusks which are exposed to insecticides and especially, thiamethoxam.In this work, adult snails Helix aspersa were used to estimate the effect of a neonicotinoid insecticide (thiamethoxam) on the acetylcholinesterase (AChE), glutathione S-transferase (GST) and catalase (CAT) activities in this gastropod after a treatment of 6 weeks. During this period, snails were exposed by ingestion and contact to fresh lettuce leaves which were soaked with an insecticide solution. The thiamethoxam test solutions were 0, 25, 50, 100 and 200 mg/L, which are lower or equal to the concentrations that are applied in field. The results showed that the enzymatic activities of AChE and GST and CAT increased significantly with a dose-dependent manner. These results confirmed the toxic effect of thiamethoxam on snails exposed to the lettuce contaminated with this neonicotinoid insecticide, likely to be used as biomarker of exposure, at first to thiamethoxam then to other insecticides belonging to the same chemical family, currently present in the environment.

Keywords: Cat, insecticide, helix aspersa, thiamethoxam, AChE, GST

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2 Nanoparticles on Biological Biomarquers Models: Paramecium Tetraurelia and Helix aspersa

Authors: M. Djekoun, M. R. Djebar, H. Djebar, L. Khene, M. Boucenna, M. N. Khebbeb

Abstract:

Currently in toxicology, use of alternative models permits to understand the mechanisms of toxicity at different levels of cells. Objectives of our research concern the determination of NPs ZnO, TiO2, AlO2, and FeO2 effect on ciliate protist freshwater Paramecium sp and Helix aspersa. The result obtained show that NPs increased antioxidative enzyme activity like catalase, glutathione –S-transferase and level GSH. Also, cells treated with high concentrations of NPs showed a high level of MDA. In conclusion, observations from growth and enzymatic parameters suggest on one hand that treatment with NPs provokes an oxidative stress and on the other that snale and paramecium are excellent alternatives models for ecotoxicological studies.

Keywords: Toxicity, catalase, MDA, GST, NPS, GSH, snale and paramecium

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1 Molecular Characterisation and Expression of Glutathione S-Transferase of Fasciola Gigantica

Authors: S. Samanta, J. Adeppa, O. K. Raina

Abstract:

Fasciolosis is a widespread economically important parasitic infection throughout the world caused by Fasciola hepatica and F. gigantica. In order to identify novel immunogen conferring significant protection against fasciolosis, currently, research has been focused on the defined antigens viz. glutathione S-transferase, fatty acid binding protein, cathepsin-L, fluke hemoglobin, paramyosin, myosin and F. hepatica- Kunitz Type Molecule. Among various antigens, GST which plays a crucial role in detoxification processes, i.e. phase II defense mechanism of this parasite, has a unique position as a novel vaccine candidate and a drug target in the control of this disease. For producing the antigens in large quantities and their purification to complete homogeneity, the recombinant DNA technology has become an important tool to achieve this milestone. RT- PCR was carried out using F. gigantica total RNA as template, and an amplicon of 657 bp GST gene was obtained. TA cloning vector was used for cloning of this gene, and the presence of insert was confirmed by blue-white selection for recombinant colonies. Sequence analysis of the present isolate showed 99.1% sequence homology with the published sequence of the F. gigantica GST gene of cattle origin (accession no. AF112657), with six nucleotide changes at 72, 74, 423, 513, 549 and 627th bp found in the present isolate, causing an overall change of 4 amino acids. The 657 bp GST gene was cloned at BamH1 and HindIII restriction sites of the prokaryotic expression vector pPROEXHTb in frame with six histidine residues and expressed in E. coli DH5α. Recombinant protein was purified from the bacterial lysate under non-denaturing conditions by the process of sonication after lysozyme treatment and subjecting the soluble fraction of the bacterial lysate to Ni-NTA affinity chromatography. Western blotting with rabbit hyper-immune serum showed immuno-reactivity with 25 kDa recombinant GST. Recombinant protein detected F. gigantica experimental as well as field infection in buffaloes by dot-ELISA. However, cross-reactivity studies on Fasciola gigantica GST antigen are needed to evaluate the utility of this protein in the serodiagnosis of fasciolosis.

Keywords: Fasciola hepatica, GST, fasciola gigantic, RT- PCR

Procedia PDF Downloads 44