Glutathione S-transferase in adult Dirofilaria immitis and Brugia pahangi

Jaffe, Julian J.; Lambert, Roger A.

doi:10.1016/0166-6851(86)90032-0

Cited by 59 publications

(18 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We studied GST activity in the life cycle stages of Brugia spp. Our results obtained with adult worm extracts and anity-puri®ed fractions agree with those previously reported (Jae and Lambert 1986). The high GST activity we observed in L3, L4, and ES products, compared with that in adult worms, suggests that this enzyme is ubiquitous in all stages of the parasite's life cycle.…”

Section: Discussionsupporting

confidence: 82%

“…These results con®rm the previous observations of Jae and Lambert (1986) and indicate GST activity in the glutathione-binding proteins of adult Brugia worms. The cytosol fraction of jird liver, a positive control which was used separately in this colorimetric assay, showed 92.7 lmol min )1 mg )1 protein GST activity.…”

Section: Gst Activity In Soluble Extracts Of Life Cycle Stages Of Brugiasupporting

confidence: 92%

“…The glutathione-binding protein(s) was further puri®ed from the soluble fraction by anity chromatography on a GSH-coupled-Sepharose 4B column (Sigma; Simons and Vander Jagt 1971;Habig and Jakoby 1981). Enzyme assay for GSTs was performed spectrophotometrically using the extracts of Mf, male, female, L3, L4, or a mixture of male and female worms, ES, or anity puri®ed glutathione-binding proteins and 1-chloro-2,4-dinitrobenzene (CDNB) as a substrate (Habig et al 1974;Jae and Lambert 1986). A typical reaction mixture for assay of GST contained the parasite protein, reduced GSH (2.5 mM), and CDNB (1.0 mM).…”

Section: Parasites and Extractsmentioning

confidence: 99%

See 2 more Smart Citations

Identification and localization of glutathione S-transferase as a potential target enzyme in Brugia species

Rao

Salinas

Mehta

et al. 2000

Parasitology Research

View full text Add to dashboard Cite

Brugia filarial nematodes are pathogenic lymphatic-dwelling parasites that, like other helminths, may modify the host's defense mechanisms by a major detoxification process involving glutathione-binding proteins such as glutathione S-transferases (GSTs). In the present study, soluble extracts of third-stage larvae, adult male and female worms, microfilariae of either B. pahangi or B. malayi or the adult worm excretory-secretory products of B. malayi were used to determine GST activity. These extracts and affinity-purified fractions of B. pahangi adult worms had a specific enzymatic activity when 1-chloro-2,4-dinitrobenzene was used as a substrate. The observance of this enzyme in all life cycle stages of Brugia spp. demonstrates its ubiquitous nature. Lavage of intraperitoneally infected jirds, but not that of uninfected jirds, also showed increased enzymatic activity, suggesting that GST is secreted in vivo. Soluble proteins of both Brugia spp. were strongly recognized by antibodies in sera from rabbits immunized with affinity-purified native GST of Onchocerca volvulus. Immunohistochemical studies localized these proteins in adult worms, demonstrating cross-reactivity between the GST of these two filarial nematodes. The effect of this enzyme on the motility and viability of adult worms, microfilariae, and larvae was tested in vitro using a battery of known GST inhibitors. Of all those tested, ethacrynic acid, N-ethylmalemide, 4-nitropyridine-oxide, or 1-chloro-2,4-dinitrobenzene at micromolar concentrations reduced the viability and motility of microfilariae, third-stage larvae, and adult worms. These results suggest that Brugia GSTs are major metabolic enzymes and may play an important role in the parasite's survival.

show abstract

Section: Discussionsupporting

confidence: 82%

Section: Gst Activity In Soluble Extracts Of Life Cycle Stages Of Brugiasupporting

confidence: 92%

Section: Parasites and Extractsmentioning

confidence: 99%

See 1 more Smart Citation

Identification and localization of glutathione S-transferase as a potential target enzyme in Brugia species

Rao

Salinas

Mehta

et al. 2000

Parasitology Research

View full text Add to dashboard Cite

show abstract

“…In addition to superoxide dismutase (SOD), alpha-glutathione transferase (GST) has been identified as a potential protective mechanism in hookworms (Brophy and Prichard 1994). This group of compounds has been identified and purified in many helminths (Jaffe and Lambert 1986;Brophy et al 1989Brophy and Barrett 1990;Barrett 1995;Cervi et al 1999), including T. spiralis (Rojas et al 1997). This group of compounds has been identified and purified in many helminths (Jaffe and Lambert 1986;Brophy et al 1989Brophy and Barrett 1990;Barrett 1995;Cervi et al 1999), including T. spiralis (Rojas et al 1997).…”

Section: Introductionmentioning

confidence: 96%

Changes in the activity of glutathione-S-transferase in muscles and sera from mice infected with Trichinella spiralis after treatment with albendazole and levamisole

Derda¹,

Boczoń²,

Wandurska-Nowak³

et al. 2003

Parasitol Res

View full text Add to dashboard Cite

In this study, changes in GST activity before and after treatment with antiparasitic drugs were measured in muscles and sera from mice infected with Trichinella spiralis between the 2nd and 9th weeks postinfection (wpi). Levamisole and albendazole, two anthelmintics with a different mode of action, were used. An about twofold stimulation of GST activity in the 2nd wpi and in the later muscular phase (6-7 wpi) was observed in muscles from animals treated with albendazole. In addition, a statistically significant stimulation of GST activity was observed after levamisole treatment, however, only from the 2nd to the 4th wpi. Neither drugs changed the GST activity in serum. These results suggest that both anthelmintics seem to increase the total activity of GST participating in oxygen free radical-based biochemical defence against Trichinella infection.

show abstract

“…1-Chloro-2,4-dinitrobenzene (CDNB) was used as the standard substrate at 30°C [9]. Assays for the conjugation of other second substrates were carried out as described in the literature [6,9,10]. Protein was determined using a Coomassie blue binding assay [11].…”

Section: Methodsmentioning

confidence: 99%

Glutathione transferase in the free‐living nematode Panagrellus redivivus

et al. 1989

View full text Add to dashboard Cite

The free-living nematode Panagrellus redivivus was found to have relatively high cytosolic glutathione transferase activity.Chromatofocusing indicated that at least four GSH transferase forms were present in the nematode cytosol. An endogenous molecular factor interfered with the binding of the cytosolic GSH transferases to a glutathione affinity matrix and binding only occurred after a partial purification step. The major resolved GSH transferase form B was a basic enzyme that showed no biochemical homology to the three mammalian multigene GSH transferase families and appeared to interact with plant phenols, possible natural substrates. A minor GSH transferase form AT showed a biochemical relationship to the mammalian ct family including catalytic activity with a model lipid hydroperoxide substrate.

show abstract

Glutathione S-transferase in adult Dirofilaria immitis and Brugia pahangi

Cited by 59 publications

References 26 publications

Identification and localization of glutathione S-transferase as a potential target enzyme in Brugia species

Identification and localization of glutathione S-transferase as a potential target enzyme in Brugia species

Changes in the activity of glutathione-S-transferase in muscles and sera from mice infected with Trichinella spiralis after treatment with albendazole and levamisole

Glutathione transferase in the free‐living nematode Panagrellus redivivus

Contact Info

Product

Resources

About