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Diethyl Maleate (diethyl + maleate)
Selected AbstractsExpression and regulation of L-cystine transporter, system xc,, in the newly developed rat retinal Müller cell line (TR-MUL)GLIA, Issue 3 2003Masatoshi Tomi Abstract The purpose of the present study was to elucidate the expression and regulation of the L-cystine transporter, system xc,, in Müller cells. In this study, newly developed conditionally immortalized rat Müller cell lines (TR-MUL) from transgenic rats harboring the temperature-sensitive SV 40 large T-antigen gene were used as an in vitro model. TR-MUL cells express large T-antigen and grow well at 33°C with a doubling time of 30 h, but do not grow at 39°C. TR-MUL cells express typical Müller cell markers such as S-100, glutamine synthetase, and EAAT1/GLAST, whereas EAAT2/GLT-1 and EAAT5 are not detected. TR-MUL cells also exhibit little or no expression of glial fibrillary acidic protein. We found that TR-MUL5 cells exhibited [14C]L-cystine uptake activity and expressed xCT and 4F2hc, which involve system xc,. The uptake of [14C]L-cystine was significantly inhibited by L-glutamic acid and L-aspartic acid, whereas L-leucine had no effect. Following diethyl maleate (DEM) treatment, the glutathione concentration in TR-MUL5 cells was reduced in the first 24 h, then gradually recovered for more than 24 h. The L-cystine uptake rate and the xCT expression level in TR-MUL5 cells were enhanced by DEM treatment. In contrast, the 4F2hc expression level was unchanged. In conclusion, TR-MUL cells have the properties of Müller cells and exhibit system xc, -mediated L-cystine uptake activity. The oxidative stress conditions following DEM treatment activate L-cystine transport in TR-MUL cells due to the enhanced transcription of the xCT gene. GLIA 9999:000,000, 2003. © 2003 Wiley-Liss, Inc. [source] Mechanisms of resistance to spinosad in the western flower thrip, Frankliniella occidentalis (Pergande) (Thysanoptera: Thripidae)INSECT SCIENCE, Issue 2 2008Shu-Yun Zhang Abstract Cross-resistance, resistance mechanisms, and mode of inheritance of spinosad resistance were studied in the western flower thrip, Frankliniella occidentalis (Pergande). Spinosad (naturalyte insecticide) showed low cross-resistance to prothiophos (organophosphorus insecticide) and chlorphenapyr (respiratory inhibitor) showed some cross-resistance to thiocyclam (nereistoxin). The synergists PBO (piperonyl butoxide), DEM (diethyl maleate), and DEF (s, s, s-tributyl phosphorotrithioate) did not show any synergism on the toxicity of spinosad in the resistant strain (ICS), indicating that metabolic-mediated detoxification was not responsible for the spinosad resistance, suggesting that spinosad may reduce sensitivity of the target site: the nicotinic acetylcholine receptor and GABA receptor. Following reciprocal crosses, dose-response lines and dominance ratios indicated that spinosad resistance was incompletely dominant and there were no maternal effects. The results of backcross showed that spinosad resistance did not fit a single-gene hypothesis, suggesting that resistance was influenced by several genes. [source] Studies on some enzymes involved in insecticide resistance in fenitrothion-resistant and -susceptible strains of Musca domestica L. (Dipt, Muscidae)JOURNAL OF APPLIED ENTOMOLOGY, Issue 9 2002S. Ahmed Co-administration of fenitrothion with three synergists, namely piperonyl butoxide (PBO), tributylphosphorotrithioate (DEF) and diethyl maleate (DEM) was investigated, respectively, at 1 : 5, 1 : 5 and 1 : 10 ratio. This co-administration of fenitrothion with PBO, DEF and DEM caused a decrease in the doses which produced 50% lethality (LD50s) in 571ab but had no synergistic effect on fenitrothion toxicity was observed in the Cooper strain. The effect of topical application of fenitrothion alone and in combination with PBO, DEF and DEM at the LD50 level on some enzyme activities in 571ab and Cooper strains was examined. The application of fenitrothion alone and in combination with DEF and DEM at LD50 level caused a significant decrease in activities of total esterases, acetylcholinesterase (AChE) and glutathione S-transferase (GST) in the 571ab strain. The decrease in GST activity was not significant in treated flies of the Cooper strain when compared with GST activity of control flies. A non-significant effect on total cytochrome P450 level was observed with fenitrothion alone and the fenitrothion + PBO treatment. No increase in activity level of total esterases, AChE and GST was found, which might suggest that changes in activity level of these enzymes are not related to fenitrothion resistance in the 571ab strain. [source] Changes in the levels of glutathione after cellular and cutaneous damage induced by squalene monohydroperoxideJOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, Issue 3 2001Katsuyoshi Chiba Abstract Squalene monohydroperoxide (Sq-OOH), the initial product of ultraviolet-peroxidated squalene, was used to investigate the effect of peroxidative challenge upon the glutathione contents in rabbit ear skin and primary-cultured fibroblasts derived from rabbit ear skin. The cellular reduced glutathione (GSH) contents decreased during 30-minute incubations in vitro with Sq-OOH, and oxidized glutathione (GSSG) was formed concomitantly, indicating that Sq-OOH had a potential for GSH-depleting activity in vitro. When Sq-OOH was applied topically to the skin in vivo, only GSSG contents increased significantly within 30 minutes. Moreover, pretreatment with the GSH depletors, DL -buthionine sulfoximine (BSO) and diethyl maleate (DEM), could potentiate the cytotoxicity and comedogenicity induced by Sq-OOH. These findings suggest that the endogenous antioxidant, glutathione, is quite sensitive to Sq-OOH and may be an important material for protecting cells and/or tissues against the oxidative stress induced by Sq-OOH treatment. © 2001 John Wiley & Sons, Inc. J Biochem Mol Toxicol 15:150,158, 2001 [source] Intracellular glutathione mediates the denitrosylation of protein nitrosothiols in the rat spinal cordJOURNAL OF NEUROSCIENCE RESEARCH, Issue 3 2009Jorge M. Romero Abstract Protein S-nitrosothiols (PrSNOs) have been implicated in the pathophysiology of neuroinflammatory and neurodegenerative disorders. Although the metabolically instability of PrSNOs is well known, there is little understanding of the factors involved in the cleavage of S-NO linkage in intact cells. To address this issue, we conducted chase experiments in spinal cord slices incubated with S-nitrosoglutathione (GSNO). The results show that removal of GSNO leads to a rapid disappearance of PrSNOs (t½ , 2 hr), which is greatly accelerated when glutathione (GSH) levels are raised with the permeable analogue GSH ethyl ester. Moreover, PrSNOs are stable in the presence of the GSH depletor diethyl maleate, indicating that GSH is critical for protein denitrosylation. Inhibition of GSH-dependent enzymes (glutathione S-transferase, glutathione peroxidase, and glutaredoxin) and enzymes that could mediate denitrosylation (alcohol dehydrogense-III, thioredoxin and protein disulfide isomerase) do not alter the rate of PrSNO decomposition. These findings and the lack of protein glutathionylation during the chase indicate that most proteins are denitrosylated via rapid transnitrosylation with GSH. The differences in the denitrosylation rate of individual proteins suggest the existence of additional structural factors in this process. This study is relevant to our recent discovery that PrSNOs accumulate in the central nervous system of patients with multiple sclerosis. © 2008 Wiley-Liss, Inc. [source] Cross-resistance study and biochemical mechanisms of thiamethoxam resistance in B-biotype Bemisia tabaci (Hemiptera: Aleyrodidae)PEST MANAGEMENT SCIENCE (FORMERLY: PESTICIDE SCIENCE), Issue 3 2010Yuntao Feng Abstract BACKGROUND: B-biotype Bemisia tabaci (Gennadius) has invaded China over the past two decades. To understand the risks and to determine possible mechanisms of resistance to thiamethoxam in B. tabaci, a resistant strain was selected in the laboratory. Cross-resistance and the biochemical mechanisms of thiamethoxam resistance were investigated in the present study. RESULTS: A 66.3-fold thiamethoxam-resistant B. tabaci strain (TH-R) was established after selection for 36 generations. Compared with the susceptible strain (TH-S), the selected TH-R strain showed obvious cross-resistance to imidacloprid (47.3-fold), acetamiprid (35.8-fold), nitenpyram (9.99-fold), abamectin (5.33-fold) and carbosulfan (4.43-fold). No cross-resistance to fipronil, chlorpyrifos or deltamethrin was seen. Piperonyl butoxide (PBO) and triphenyl phosphate (TPP) exhibited significant synergism on thiamethoxam effects in the TH-R strain (3.14- and 2.37-fold respectively). However, diethyl maleate (DEM) did not act synergistically with thiamethoxam. Biochemical assays showed that cytochrome P450 monooxygenase activities increased 1.21- and 1.68-fold respectively, and carboxylesterase activity increased 2.96-fold in the TH-R strain. However, no difference was observed for glutathione S -transferase between the two strains. CONCLUSION: B-biotype B. tabaci develops resistance to thiamethoxam. Cytochrome P450 monooxygenase and carboxylesterase appear to be responsible for the resistance. Reasonable resistance management that avoids the use of cross-resistance insecticides may delay the development of resistance to thiamethoxam in this species. Copyright © 2009 Society of Chemical Industry [source] Biochemical mechanisms of methoxyfenozide resistance in the cotton leafworm Spodoptera littoralisPEST MANAGEMENT SCIENCE (FORMERLY: PESTICIDE SCIENCE), Issue 7 2009Hadi Mosallanejad Abstract BACKGROUND: Methoxyfenozide is a lepidopteran-specific insecticide that belongs to a new group of insecticides, the non-steroidal ecdysteroid agonists, also called moulting accelerating compounds (MACs). To investigate the risk of resistance and possible mechanisms conferring resistance to methoxyfenozide, the authors selected in the laboratory for a resistant strain of the cotton leafworm Spodoptera littoralis (Boisd.), which is a representative lepidopteran model and an important pest in cotton and vegetables worldwide, with a high risk for resistance development. RESULTS: After selection with methoxyfenozide during 13 generations, toxicity data showed that the selected strain developed fivefold resistance to methoxyfenozide in comparison with the susceptible strain. Measurement of the detoxification enzymes demonstrated that the monooxygenase (MO) activity was 2.1 times higher in the selected strain, whereas there was no change for esterases and glutathione- S -transferases. When the inhibitors piperonyl butoxide (PBO), S,S,S -tributyl phosphorotrithioate (DEF) and diethyl maleate were tested as synergists, the respective synergistic ratios were 0.97, 0.96 and 1.0 for the susceptible strain, and 2.2, 0.96 and 1.1 for the resistant strain. The significant synergistic effect by PBO concurs with the increased MO activity in the selected strain. CONCLUSION: Taken overall, the present study supports the importance of MO-mediated metabolism in resistance to methoxyfenozide, directing tactics to fight against resistance development for this novel group of insecticides. Copyright © 2009 Society of Chemical Industry [source] Insecticide toxicity and synergism by enzyme inhibitors in 18 species of pest insect and natural enemies in crucifer vegetable cropsPEST MANAGEMENT SCIENCE (FORMERLY: PESTICIDE SCIENCE), Issue 5 2007Gang Wu Abstract The toxicities of three enzyme inhibitors and their synergistic effects on four insecticides were studied by using the dry film method on field populations of 18 species of insects collected in Jianxin and Shanjie, China, from 2003 to 2005. Meanwhile, the inhibitory effects of these enzyme inhibitors on the activities of acetylcholinesterases (AChE), carboxyesterases (CarE) and glutathione- S -transferases (GST), in vivo, were also studied. In general, triphenyl phosphate (TPP) and diethyl maleate (DEM) showed low toxicities to six herbivorous pest insects, four ladybirds and eight parasitoids. Piperonyl butoxide (PB) exhibited low toxicities to the herbivorous pest insects and ladybirds, but high toxicities to the eight parasitoids. The tolerance to the insecticides in 11 pest insects and natural enemies was mainly associated with the tolerance to PB. PB showed the highest synergism on methamidophos, fenvalerate, fipronil and avermectin in nine species of pest insects and natural enemies. In general, TPP and DEM showed significant synergisms to these four insecticides in four parasitoid species. However, in contrast to their effects on the parasitoids, the synergistic effects of TPP and DEM on the four insecticides by TPP and DEM against four pest insects and one ladybird varied depending on the insect species and enzyme inhibitor. Activity of AChE, CarE or GST could be strongly inhibited, in vivo, by PB, TPP or DEM, depending on the insect species and enzyme inhibitors. From the results obtained in this study, mixed-function oxidase (MFO) was thought to play the most critical role in insect tolerances to the tested insecticides in the field. Low competition existed in the evolution of insecticide resistance in the field populations of parasitoids, as compared with herbivorous pest insects and ladybirds. Possible causes of the high synergistic effects of PB on the four classes of insecticides, based on multiattack on the activity of CarE, GST or AChE in the insect species, are also discussed. Copyright © 2007 Society of Chemical Industry [source] Functionalized polypropylenes in the compatibilization and dispersion of clay nanocompositesPOLYMER COMPOSITES, Issue 4 2006C. Varela The preparation of polypropylene (PP) nanocomposites was studied using clay and three types of modified PP (m-PP) as compatibilizers: diethyl maleate grafted PP (PP- g -DEM), maleic anhydride grafted PP (PP- g -MA), and PP grafted with carbamyl maleamic acid (PP- g -UMA). The clay was made organophylic by an acid treatment with octadecylamine. PP functionalization and blending were carried out in an internal mixer. Blends of PP containing 20 and 40 wt% each of the modified PP and 5 wt% of organophilic clay (IMt), in each case, were prepared. Samples were characterized by transmission electron microscopy (TEM), differential scanning calorimetry (DSC), optical microscopy, and mechanical testing. The presence of tactoid, intercalated and exfoliated structures was observed by TEM in all the samples containing clay and modified PP, which also showed improved mechanical properties with tensile modulus as much as three times that of PP. Melting temperature did not vary significantly with the addition of clay. However, because of the clay's nucleating effect, an increase in the crystallization temperature was observed, accompanied by a slight decrease in the degree of crystallinity. The best results were obtained when PP- g -MA was used as the compatibilizer; intermediate results were obtained with the use of PP- g -UMA, followed by the results obtained when PP- g -DEM was used. Property enhancements were obtained when a higher percentage of modified PP was employed. POLYM. COMPOS., 27:451,460, 2006. © 2006 Society of Plastics Engineers [source] Nanostructured polyolefins/clay composites: role of the molecular interaction at the interfacePOLYMERS FOR ADVANCED TECHNOLOGIES, Issue 6 2008Elisa Passaglia Abstract The extent of interphase interactions between polymer phase and inorganic particles is the driving force addressing the preparation/properties design in the field of the corresponding micro- and nanocomposites. In the case of preparation of nanocomposites based on polyolefins (POs) and inorganic compounds as potentially nanodispersed phase, the use of a PO with proper functional groups is necessary for the interface adhesion and stabilization of the nanostructured morphology. According to this approach, ethylene/propylene copolymers with a different propylene content were used for the preparation of nanocomposites through melt mixing with organophilic montmorillonites (OMMT). By taking into account the important role of functionalities grafted onto POs, two different synthetic approaches were compared here: (1) the dispersion of the inorganic filler was obtained by using previously functionalized POs bearing carboxylate groups as matrices; (2) the nanocomposites were prepared by performing contemporaneously the functionalization of POs (by using maleic anhydride (MAH) and/or diethyl maleate (DEM)) and the dispersion of the filler in a one-step process. The morphology of the nanocomposites as well as the variation of solubility and glass transition temperature (Tg) of the PO matrix were evaluated and tentatively discussed with reference to functionalization degrees, structure of PO, and preparation procedure. Copyright © 2008 John Wiley & Sons, Ltd. [source] Mechanisms of organophosphate resistance in a field population of oriental migratory locust, Locusta migratoria manilensis (Meyen)ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 1 2009M.L. Yang Abstract The susceptibilities to three organophosphate (OP) insecticides (malathion, chlorpyrifos, and phoxim), responses to three metabolic synergists [triphenyl phosphate (TPP), piperonyl butoxide (PBO), and diethyl maleate (DEM)], activities of major detoxification enzymes [general esterases (ESTs), glutathione S -transferases (GSTs), and cytochrome P450 monooxygenases (P450s)], and sensitivity of the target enzyme acetylcholinesterase (AChE) were compared between a laboratory-susceptible strain (LS) and a field-resistant population (FR) of the oriental migratory locust, Locusta migratoria manilensis (Meyen). The FR was significantly resistant to malathion (57.5-fold), but marginally resistant to chlorpyrifos (5.4) and phoxim (2.9). The malathion resistance of the FR was significantly diminished by TPP (synergism ratio: 16.2) and DEM (3.3), but was unchanged by PBO. In contrast, none of these synergists significantly affected the toxicity of malathion in the LS. Biochemical studies indicated that EST and GST activities in the FR were 2.1- to 3.2-fold and 1.2- to 2.0-fold, respectively, higher than those in the LS, but there was no significant difference in P450 activity between the LS and FR. Furthermore, AChE from the FR showed 4.0-fold higher activity but was 3.2-, 2.2-, and 1.1-fold less sensitive to inhibition by malaoxon, chlorpyrifos-oxon, and phoxim, respectively, than that from the LS. All these results clearly indicated that the observed malathion resistance in the FR was conferred by multiple mechanisms, including increased detoxification by ESTs and GSTs, and increased activity and reduced sensitivity of AChE to OP inhibition. Arch. Insect Biochem. Physiol. 2009. © 2008 Wiley-Liss, Inc. [source] Susceptibility of four field populations of the diamondback moth Plutella xylostella L. (Lepidoptera: Yponomeutidae) to six insecticides in the Sydney region, New South Wales, AustraliaAUSTRALIAN JOURNAL OF ENTOMOLOGY, Issue 4 2008Vincent Y Eziah Abstract Concerns about the failure of insecticides to control the diamondback moth (DBM) Plutella xylostella in the Sydney region of New South Wales, Australia, necessitated the current investigation to establish the susceptibility of four field populations of the DBM to six insecticides. These include two each of organophosphates (OPs), and synthetic pyrethroid insecticides as well as two new products with different modes of action, spinosad and indoxacarb, currently recommended for DBM control in the region. Topical application of the insecticides to the third-instar larvae showed high resistance to pyrethroids (permethrin and esfenvalerate) of 35.0- to 490.0-fold. Resistance to the OPs (methamidophos and chlorpyrifos) and indoxacarb ranged from 12.1- to 36.2-fold and from 11.4- to 34.6-fold, respectively. However, the field populations were susceptible to spinosad (resistance factors only two- to threefold compared with the susceptible strain). A 2 h pre-treatment of the esfenvalerate-resistant strain with the synergists piperonyl butoxide and diethyl maleate increased the toxicity of esfenvalerate by 30.0- and 1.9-fold, respectively, suggesting the involvement of esterases and/or monooxygenases as the key mechanism(s) of insecticide resistance with glutathione S-transferases playing a minor role. [source] |