scholarly journals Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth

2021 ◽  
Vol 12 ◽  
Author(s):  
Hongmin Liu ◽  
Yin Tang ◽  
Qinying Wang ◽  
Hongzhong Shi ◽  
Jian Yin ◽  
...  
Keyword(s):  
Detection System ◽  
Pcr Analysis ◽  
Host Volatiles ◽  
Glutathione S Transferase ◽  
Stored Grain ◽  
Indian Meal Moth ◽  
Indian Meal ◽  
Glutathione S Transferases ◽  
Exogenous Compounds

Insect glutathione-S-transferases (GSTs) play essential roles in metabolizing endogenous and exogenous compounds. GSTs that are uniquely expressed in antennae are assumed to function as scavengers of pheromones and host volatiles in the odorant detection system. Based on this assumption, antennae-specific GSTs have been identified and functionally characterized in increasing number of insect species. In the present study, 17 putative GSTs were identified from the antennal transcriptomic dataset of the Indian meal moth, Plodia interpunctella, a severe stored-grain pest worldwide. Among the GSTs, only PiGSTd1 is antennae-specific according to both Fragments Per Kilobase Million (FPKM) and quantitative real-time PCR (qRT-PCR) analysis. Sequence analysis revealed that PiGSTd1 has a similar identity as many delta GSTs from other moths. Enzyme kinetic assays using 1-chloro-2,4-dinitrobenzene (CDNB) as substrates showed that the recombinant PiGSTd1 gave a Km of 0.2292 ± 0.01805 mM and a Vmax of 14.02 ± 0.2545 μmol·mg−1·min−1 under the optimal catalytic conditions (35°C and pH = 7.5). Further analysis revealed that the recombinant PiGSTd1 could efficiently degrade the sex pheromone component Z9-12:Ac (75.63 ± 5.52%), as well as aldehyde volatiles, including hexanal (89.10 ± 2.21%), heptanal (63.19 ± 5.36%), (E)-2-octenal (73.58 ± 3.92%), (E)-2-nonenal (75.81 ± 1.90%), and (E)-2-decenal (61.13 ± 5.24%). Taken together, our findings suggest that PiGSTd1 may play essential roles in degrading and inactivating a variety of odorants, especially sex pheromones and host volatiles of P. interpunctella.

scholarly journals Purification and characterization of prostaglandin-H E-isomerase, a sigma-class glutathione S-transferase, from Ascaridia galli

1996 ◽  
Vol 313 (1) ◽  
pp. 223-227 ◽  
Author(s):  
David J. MEYER ◽  
Richmond MUIMO ◽  
Michael THOMAS ◽  
David COATES ◽  
R. Elwyn ISAAC
Keyword(s):  
Parasitic Nematode ◽  
Helminth Parasites ◽  
Ascaridia Galli ◽  
Glutathione S Transferase ◽  
Purification And Characterization ◽  
Parasitic Helminths ◽  
Accessory Cells ◽  
Glutathione S Transferases ◽  
Prostaglandin H

Comparison of partial primary sequences of sigma-class glutathione S-transferases (GSH) of parasitic helminths and a GSH-dependent prostaglandin (PG)-H D-isomerase of rat immune accessory cells suggested that some of the helminth enzymes may also be involved in PG biosynthesis [Meyer and Thomas (1995) Biochem. J. 311, 739-742]. A soluble GSH transferase of the parasitic nematode Ascaridia galli has now been purified which shows high activity and specificity in the GSH-dependent isomerization of PGH to PGE, comparable to that of the rat spleen enzyme in its isomerization of PGH to PGD, and similarly stimulates the activity of prostaglandin H synthase. The enzyme subunit is structurally related to the rat spleen enzyme and sigma-class GSH transferases of helminths according to the partial primary sequence. The data support the hypothesis that some sigma-class GSH transferases of helminth parasites are involved in PG biosynthesis which, in the case of PGE, is likely to be associated with the subversion or suppression of host immunity. A PG-H E-isomerase of comparable specificity and activity has not previously been isolated.

scholarly journals Variability of Glutathione S-Transferase α in Human Liver and Plasma

1999 ◽  
Vol 45 (3) ◽  
pp. 355-359 ◽  
Author(s):  
Theo PJ Mulder ◽  
Daniel A Court ◽  
Wilbert HM Peters
Keyword(s):  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Human Liver ◽  
Organ Donors ◽  
Healthy Controls ◽  
Plasma Samples ◽  
Glutathione S Transferase ◽  
Glutathione S Transferases ◽  
The Mean ◽  
Exogenous Compounds

Abstract Background: Glutathione S-transferases are a family of enzymes involved in the binding, transport, and detoxification of a wide variety of endogenous and exogenous compounds. Little information is available about the variability of class α glutathione S-transferases in human liver, where they are highly expressed, or in serum. Methods: Both total class α glutathione S-transferase (GST-α, composed of GSTA1-1, GSTA1-2, and GSTA2-2) as well as GSTA1-1 concentrations were measured by specific and sensitive ELISA in liver cytosols of 35 organ donors and in plasma samples of 350 healthy controls. Results: The mean total GST-α and GSTA1-1 in liver cytosols were 25.1 ± 9.4 and 10.7 ± 5.3 μg/mg protein, respectively, and did not correlate with activities of aspartate aminotransferase or alanine aminotransferase. The mean total GST-α in liver was significantly higher in females compared with males (28.8 ± 10.0 vs 22.0 ± 7.8 μg/mg protein; P <0.05). In contrast, the median total GST-α in plasma was lower in females compared with males (2.0 and 2.8 μg/L, respectively; P <0.0001). The median ratios for GSTA1-1/total GST-α in liver and plasma were 0.42 and 0.58, respectively. Conclusions: GSTA1-1 constitutes approximately one-half of the total amount of α class GSTs in human plasma and liver. Total GST-α values are higher in female liver but lower in plasma compared with the respective values in males.

scholarly journals Characterization of glutathione S-transferases in rat kidney. Alteration of composition by cis-platinum

1988 ◽  
Vol 252 (1) ◽  
pp. 127-136 ◽  
Author(s):  
G M Trakshel ◽  
M D Maines
Keyword(s):  
Specific Activity ◽  
Rat Kidney ◽  
Male Rats ◽  
Glutathione S Transferase ◽  
Aberrant Form ◽  
Glutathione S Transferases ◽  
Exchange Matrix ◽  
Rat Kidney Cytosol

We have developed chromatographic and mathematical protocols that allowed the high resolution of glutathione S-transferase (GST) subunits, and the identification of a previously unresolved GST monomer in rat kidney cytosol; the monomer was identified tentatively as subunit 6. Also, an aberrant form of GST 7-7 dimer appeared to be present in the kidney. This development was utilized to illustrate the response of rat kidney GST following cis-platinum treatment in vivo. Rat kidney cytosol was separated into three ‘affinity families’ of GST activity after elution from a GSH-agarose matrix. The affinity peaks were characterized by quantitative differences in their subunit and dimeric compositions as determined by subsequent chromatography on a cation-exchange matrix and specific activity towards substrates. By use of these criteria, the major GST dimers of affinity peaks were tentatively identified. The major GST dimers in peak I were GST 1-1 and 1-2, in affinity peak II it was GST 2-2, and in peak III they were GST 3-3 and 7-7. GST 3-6 and/or 4-6, which have not been previously resolved in kidney cytosol, were also present in peak II. Alterations in the kidney cytosolic GST composition of male rats were detected subsequent to the administration of cis-platinum (7.0 mg/kg subcutaneously, 6 days). This treatment caused a pronounced alteration in the GST profile, and the pattern of alteration was markedly different from that reported for other chemicals in the kidney or in the liver. In general, the cellular contents of the GSTs of the Alpha and the Mu classes decreased and increased respectively. It is postulated that the decrease in the Alpha class of GSTs by cis-platinum treatment may be related to renal cortical damage and the loss of GSTs in the urine. The increase in the Mu class of GSTs could potentially stem from a lowered serum concentration of testosterone; the latter is a known effect of cis-platinum treatment.

scholarly journals Differential induction of class Alpha glutathione S-transferases in mouse liver by the anticarcinogenic antioxidant butylated hydroxyanisole. Purification and characterization of glutathione S-transferase Ya1Ya1

1989 ◽  
Vol 263 (2) ◽  
pp. 393-402 ◽  
Author(s):  
L I McLellan ◽  
J D Hayes
Keyword(s):  
Female Mouse ◽  
Mouse Liver ◽  
Normal Mouse ◽  
Butylated Hydroxyanisole ◽  
Glutathione S Transferase ◽  
Purification And Characterization ◽  
Glutathione S Transferases ◽  
Differential Induction ◽  
Carcinogenic Compound

A novel cytosolic Alpha class glutathione S-transferase (GST) that is not normally expressed in mouse liver was found to be markedly induced (at least 20-fold) by the anti-carcinogenic compound butylated hydroxyanisole. This enzyme (designated GST Ya1 Ya1) did not bind to either the S-hexylglutathione-Sepharose or the glutathione-Sepharose affinity matrices, and purification was achieved by using bromosulphophthalein-glutathione-Sepharose. The purified isoenzyme, which comprises subunits of Mr 25,600, was characterized, and its catalytic, electrophoretic, immunochemical and structural properties are documented. GST Ya1 Ya1 was shown to be distinct from the Alpha class GST that is expressed in normal mouse liver and is composed of 25,800-Mr subunits; the Alpha class isoenzyme that is constitutively expressed in the liver is now designated GST Ya3 Ya3. Hepatic concentrations of GST Ya3 Ya3 were not significantly affected when mice were treated with butylated hydroxyanisole. Both Pi class GST (subunit Mr 24,800) and Mu class GST (subunit Mr 26,400) from female mouse liver were induced by dietary butylated hydroxyanisole. By contrast, hepatic concentrations of microsomal GST (subunit Mr 17,300) were unaffected.

Antibiotics as Inhibitor of Glutathione S-transferase: Biological Evaluation and Molecular Structure Studies

2021 ◽  
Vol 22 ◽  
Author(s):  
Adnan Ayna ◽  
Luqman Khosnaw ◽  
Yusuf Temel ◽  
Mehmet Ciftci
Keyword(s):  
Biochemical Characterization ◽  
Specific Activity ◽  
Biological Evaluation ◽  
Glutathione S Transferase ◽  
Scopolamine Butylbromide ◽  
Glutathione S Transferases ◽  
Concentration Graphs ◽  
Compound Concentration

Background: The glutathione S-transferases (GSTs) are family of enzymes that are notable for their role in phase II detoxification reactions. Antibiotics have been reported to have several adverse effects on the activity of the enzymes in mammals. Aim: The aim of this study was structural and biochemical characterization of rat erythrocyte GST and understanding the effects of gentamicin, clindamycin, cefazolin, ampicillin and scopolamine butylbromide on the activity of human erythrocyte GST using rat as a model. Methods: The enzyme was purified by GSH-agarose affinity chromatography. In vitro GST enzyme activity was measured at 25°C using CDNB as a model substrate. IC50 of drugs were measured by activity %–vs compound concentration graphs. Lineweaver–Burk graphs were drawn to determine the inhibition type and Ki constants for the drugs. The structure of the enzyme was predicted via Protein Homology/analogY Recognition Engine. Results: In this study, GST was purified from rat erythrocyte with a specific activity of 6.3 EU/mg protein, 44 % yield and 115 fold. Gentamicin and clindamycin inhibited the enzymatic activity with IC50 of 1.69 and 6.9 mM and Ki of 1.70 and 2.36 mM, respectively. Ampicillin and scopolamine butylbromide were activator of the enzyme while the activity of the enzyme was insensitive to cefazolin. The enzyme was further characterized by homology modeling and sequence alignment revealing similarities with human GST. Conclusion: Collectively, it could be concluded that gentamicin and clindamycin are the inhibitors of erythrocyte GST.

scholarly journals Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver

1987 ◽  
Vol 244 (1) ◽  
pp. 55-61 ◽  
Author(s):  
P K Stockman ◽  
L I McLellan ◽  
J D Hayes
Keyword(s):  
Glutathione Peroxidase ◽  
Human Liver ◽  
Catalytic Properties ◽  
Peptide Mapping ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Tryptic Peptides ◽  
Glutathione S Transferases ◽  
Tributyltin Acetate

The basic glutathione S-transferases in human liver are composed of at least two immunochemically distinct polypeptides, designated B1 and B2. These subunits exist as homodimers, but can hybridize to form the B1B2 heterodimer [Stockman, Beckett & Hayes (1985) Biochem. J. 227, 457-465]. Although these basic glutathione S-transferases possess similar catalytic properties, the B2 subunit exhibits significantly greater selenium-independent glutathione peroxidase activity than subunit B1. The use of the ligands haematin, tributyltin acetate and Bromosulphophthalein as inhibitors of 1-chloro-2,4-dinitrobenzene-GSH-conjugating activity clearly discriminate between the B1 and B2 subunits and should help facilitate their identification. Peptide mapping experiments showed that B1 and B2 are structurally distinct, but related, subunits; subunit B1 yielded 43 tryptic peptides, seven of which were unique, whereas subunit B2 yielded 40 tryptic peptides, four of which were unique.

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