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PubMed2003

Induction of glutathione S-transferases activities in Drosophila melanogaster exposed to phenol.

Studying the toxic effects of long-term exposing fruit flies to phenol is the object of this study. The induction of the glutathione S-transferases enzymatic activities, the change in the amount of mRNA related to phenol exposure, the change in survival rate of adult fruit flies, and the chemical interaction between phenol and benzene were the problems to be investigated. Glutathione S-transferases were separated by affinity chromatography and the mRNAs levels were quantified by reverse-transcription polymerase chain reaction. Long-term feeding phenol to wild type fruit flies had caused some toxic effects included increasing the resistance to phenol toxicity, lowering the benzene toxicity, and induction of glutathione S-transferases enzymatic activities. But no significant change in the amount of glutathione S-transferases GstD1 and GstD5 mRNAs had occurred. From these results, we concluded that fruit flies could develop resistance to phenol by decreasing its toxicity; phenol was a inducer of glutathione S-transferases; phenol could increase the glutathione S-transferases enzymatic activities by increasing the amount of proteins; phenol exposure could decrease the benzene toxicity; no new glutathione S-transferase isozyme subunit was induced; and the level of GstD1 and GstD5 mRNAs did not significantly increase in phenol-treated strain.

Animals↗
PubMed1993

Erythromycin binding is reduced in ribosomes with conformational alterations in the 23 S rRNA peptidyl transferase loop.

The antibiotic erythromycin inhibits protein synthesis by binding to the 50 S ribosomal subunit, where the drug interacts with the unpaired bases 2058A and 2059A in the peptidyl transferase loop of 23 S rRNA. We used a chemical modification approach to analyse conformational changes that are induced by mutations in the peptidyl transferase loop, and to determine how these changes affect drug interaction. Mutations at positions 2057 (G-->A) and 2058 (A-->G, or -->U), all of which confer drug resistance, induce a more open conformation in the peptidyl transferase loop. Erythromycin still protects against chemical modification in the mutant peptidyl transferase loops, but the affinity of the drug interaction is reduced 20-fold in the 2057A mutant, 10(3)-fold in the 2058U mutant and 10(4)-fold in the 2058G mutant. Single mutations at position 2032 in the adjacent hairpin loop, which have previously been shown to alter drug tolerances, gave no detectable effects on the structure of the peptidyl transferase loop or on erythromycin binding. Dual mutations at positions 2032 and 2058, however, induce a marked change in the rRNA conformation with opening of the phylogenetically conserved base-pair 2063C.2447G, and confer a slow growth, drug-sensitive phenotype. The data suggest that the target site of erythromycin lies within the peptidyl transferase loop, and that limited disruption of the conformation of this site reduces drug binding, and consequently confers resistance. In addition, there is structurally and functionally important interaction between the drug target site in the peptidyl transferase loop and position 2032.

Base Sequence↗
PubMed1994

Glutathione transferase gene family from the housefly Musca domestica.

Three new glutathione transferase (GST) genes from the housefly Musca domestica are described. These genes, identified as MdGST-2, -3, and -4, were from cDNA clones obtained from a cDNA bank in phage lambda. The bank was prepared using poly(A)+ RNA from a housefly that is highly resistant to organophosphate insecticides because of enhanced expression of multiple members of the glutathione transferase gene family. The DNA sequence of each is reported and has a complete open reading frame that specified an amino acid sequence similar to other dipteran glutathione transferases. Based on phylogenetic analysis, we can conclude that the insect glutathione transferase gene family falls into two groups, each of which evolves at a different rate, presumably due to differences in functional constraints. We show that MdGST-1 (and their homologues from Drosophila and Lucilia) evolve at a significantly slower rate than the other members of the gene family. Each housefly GST cDNA was inserted into a bacterial plasmid expression system and a glutathione transferase activity was expressed in Escherichia coli. The transcription pattern of each of these glutathione transferases was examined in a variety of different housefly strains that are known to differ in their resistance to organophosphate insecticides due to different patterns of glutathione transferase expression. We found that the level of transcription for two of our clones was positively correlated with the level of organophosphate resistance.

Amino Acid Sequence↗
PubMed2002

The elusive roles of bacterial glutathione S-transferases: new lessons from genomes.

Glutathione S-transferases constitute a large family of enzymes which catalyze the addition of glutathione to endogenous or xenobiotic, often toxic electrophilic chemicals. Eukaryotic glutathione S-transferases usually promote the inactivation, degradation or excretion of a wide range of compounds by formation of the corresponding glutathione conjugates. In bacteria, by contrast, the few glutathione S-transferases for which substrates are known, such as dichloromethane dehalogenase, 1,2-dichloroepoxyethane epoxidase and tetrachlorohydroquinone reductase, are catabolic enzymes with an essential role for growth on recalcitrant chemicals. Glutathione S-transferase genes have also been found in bacterial operons and gene clusters involved in the degradation of aromatic compounds. Information from bacterial genome sequencing projects now suggests that glutathione S-transferases are present in large numbers in proteobacteria. In particular, the genomes of three Pseudomonas species each include at least ten different glutathione S-transferase genes. Several of the corresponding proteins define new classes of the glutathione S-transferase family and may also have novel functions that remain to be elucidated.

Biotechnology↗
PubMed1992

Activation of rat liver microsomal glutathione S-transferase by hydrogen peroxide: role for protein-dimer formation.

The mechanism of oxygen radical-dependent activation of hepatic microsomal glutathione S-transferase by hydrogen peroxide was studied. Glutathione S-transferase activity in liver microsomes was increased 1.5-fold by incubation with 0.75 mM hydrogen peroxide at 37 degrees C for 10 min, and the increase in activity was reversed by incubation with dithiothreitol. Purified glutathione S-transferase was also activated by hydrogen peroxide after incubation at room temperature, and the increase in the activity was also reversed by dithiothreitol. Immunoblotting with anti-microsomal glutathione S-transferase antibodies after sodium dodecyl sulfate-polyacrylamide gel electrophoresis of hydrogen peroxide-treated microsomes or purified glutathione S-transferase revealed the presence of a glutathione S-transferase dimer. These results indicate that the hydrogen peroxide-dependent activation of the microsomal glutathione S-transferase is associated with the formation of a protein dimer.

Animals↗
PubMed1981

Affinity chromatography of hepatic glutathione S-transferases on omega-aminoalkyl sepharose derivatives of glutathione.

Rat liver glutathione S-transferases (RX: glutathione R-transferase, EC 2.5.1.18) were found to adsorb S-carbamidomethyl glutathione linked to Sepharose CL-4B via lysyl or aliphatic diamine spacers of various carbon chain lengths (-NH-(CH2)n-NH-, n = 2, 4, 5, 6, 8 and 10). Proteins were eluted specifically by reduced glutathione. The affinity of the enzymes for the adsorbent increased with increase in the carbon chain length of aliphatic diamine spacers used. Adsorbent having a free carboxyl group within the spacer moiety had high capacity and was specific for glutathione S-transferases. The transferases were specifically eluted from the column in high yield by low concentrations of glutathione. Enzymes purified by the lysyl spacer adsorbent were homogeneous in sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and contained most of the hepatic glutathione S-transferase isozymes in isoelectric focusing. Oxidized glutathione and S-methyl glutathione were equally effective as reduced glutathione in eluting glutathione S-transferases from the adsorbent, but gamma-glutamylcysteinylglycineamide or gamma-glutamylcysteinylglycine-1-methyl ester were not effective. These data suggested that the free carboxyl group of glycyl moiety of glutathione might also be important for the specific binding of the transferases to this adsorbent.

Animals↗
PubMed1984

Glutathione S-transferase isozymes of mouse intestine: differential induction by 2(3)-tert-butyl-4-hydroxyanisole.

Electrofocusing of mouse small intestine mucosal cytosol yielded two prominent peaks of glutathione S-transferase activity, at pH 8.7 and pH 9.0. These intestinal transferases were indistinguishable from corresponding liver transferases in immunological reactivities and in several other properties. Dietary t-butyl-4-hydroxyanisole increased intestine cytosol protein immunologically identical to the liver transferase with pI of 8.7 and also elevated markedly and preferentially the intestinal transferase activity peak at pH 8.7. Thus, the predominant transferases of mouse intestine appear identical to two of the liver isozymes, and t-butyl-4-hydroxyanisole enhances intestinal transferase activity mainly by increasing the quantity of the isozyme(s) of pI 8.7.

Animals↗
PubMed1990

Immunodetection with a monoclonal antibody of glutathione S-transferase mu in patients with and without carcinomas.

Several monoclonal antibodies against human liver glutathione S-transferase mu were developed. One of these monoclonal antibodies, called GST-3H4 was further characterized and used in this study. In hepatic tissue, after immunoblotting, GST-3H4 strains a 27 kDa protein with a pI value of 6.2. GST-3H4 recognizes other human class-mu glutathione S-transferases, but does not detect acidic or basic glutathione S-transferases. By immunodetection with this monoclonal antibody, glutathione S-transferase mu can be demonstrated in human breast, stomach, liver, small and large intestine, mononuclear blood cells, kidney and placenta. A 100% correlation is found in the distribution of glutathione S-transferase mu when different tissues or mononuclear blood cells from the same individuals are investigated. In 62.5% of the mononuclear blood cells from controls, glutathione S-transferase mu is present. In patients with polyposis coli, breast cancer or colon cancer a similar distribution is found. Therefore no important role for glutathione S-transferase mu deficiencies in the aetiology of these diseases is suggested.

Animals↗
PubMed1990

Reversible inhibition of rat hepatic glutathione S-transferase 1-2 by bilirubin.

The inhibition of rat hepatic glutathione (GSH) S-transferase 1-2 by bilirubin exhibited pseudo first-order kinetics with k(obs) values of 0.0214 +/- 0.0005 and 0.040 +/- 0.008 sec-1 at 4 and 8 microM bilirubin, when followed to 72 and 84% completion respectively. These correspond to calculated second-order rate constants of 5.3 +/- 0.1 x 10(3) and 5.0 +/- 1.0 x 10(3)/M.sec. The extent of inhibition of the transferase increased with bilirubin concentration, with half-maximal inhibition at 4 microM bilirubin. Inhibition was reversed by 10-fold dilution of bilirubin or by increasing the pH from 6.0 to 7.4. Premixing 0.2 to 0.5 microM albumin, hemoglobin or aldolase with bilirubin prevented inhibition of GSH S-transferase 1-2. Protection by these proteins occurred at a selected high concentration (0.2 to 0.4 microM) at which they reduced free bilirubin to concentrations (less than 0.5 microM) that did not inhibit isoenzyme 1-2 significantly. No protection was afforded by a selected low protein concentration (0.001 to 0.01 microM) which did not strikingly reduce bilirubin levels in solution. We conclude that bilirubin inhibition of GSH S-transferase 1-2 appears to be a second-order process; the reaction is clearly first-order with respect to GSH S-transferase and appears also to be first-order with respect to bilirubin. It is proposed that (a) inhibition of GSH S-transferase 1-2 results from slow, reversible bilirubin binding, and (b) added proteins appear to prevent GSH S-transferase inhibition by binding high molar ratios of bilirubin.

Albumins↗
PubMed1991

Effect of the aging process on the gender and phenobarbital dependent expression of glutathione S-transferase subunits in brown Norway rat liver.

The effect of age, gender and phenobarbital treatment on the hepatic cytosolic glutathione S-transferase subunit composition was studied in Brown Norway rats. Affinity chromatography followed by reversed phase HPLC was used in order to separate the various glutathione S-transferase subunits. Corresponding steady-state mRNA levels were measured by Northern Blot analysis using cDNA clones hybridizing to mRNA encoding glutathione S-transferase subunits 1/2, 3/4 and 7, respectively. In all the age groups studied (15, 25, 53, 99, 112 and 136 weeks) the total amount of glutathione S-transferase protein was in untreated rats significantly higher in males (132 micrograms/mg cytosolic protein) than in females (91 micrograms/mg cytosolic protein) and significant gender dependent differences in the subunit composition were demonstrated. Aging seemed to be of minor importance in untreated as well as in phenobarbital treated rats. Under control conditions, the subunit composition of male rats between 15 and 136 weeks old consisted of 28, 12, 11 and 49% of subunits 1, 2, 3 and 4 respectively and of female animals of the same age groups of 38, 26, 7 and 30%, respectively. In all the age groups studied phenobarbital administration (45 mg/kg body weight, i.p., once a day for 7 days) doubled total glutathione S-transferase protein in both genders and affected the subunit composition in a significant way, emphasizing the already existing differences between genders. Subunits 1, 2 and 3, especially, were increased in male rats in comparison to females resulting in the observation that levels of glutathione S-transferase subunits studied became higher in males than in their female counterparts. The HPLC results were confirmed by steady-state mRNA analysis. In untreated rats, higher levels of mRNA encoding glutathione S-transferase subunits 1/2 and 3/4 were present in male than in female livers. Phenobarbital treatment increased mRNA levels in both genders. Subunit 7 was never detected. These effects were demonstrated in both young and old rats.

Aging↗
PubMed1993

Evidence that rat liver microsomal glutathione transferase is responsible for glutathione-dependent protection against lipid peroxidation.

Evidence that rat liver microsomal glutathione transferase is responsible for the glutathione-dependent inhibition of lipid peroxidation in liver microsomes has been obtained. Activation of the microsomal glutathione transferase in microsomes by cystamine renders this organelle even more resistant to lipid peroxidation in the presence of glutathione compared with untreated microsomes. Upon examining the effect of seven glutathione analogues on lipid peroxidation, it was found that only those that serve as good substrates for the microsomal glutathione transferase (Glutaryl-L-Cys-Gly and alpha-L-Glu-L-Cys-Gly) can inhibit lipid peroxidation. The lack of inhibition by the other five analogues (alpha-D-Glu-L-Cys-Gly, gamma-D-Glu-L-Cys-Gly, beta-L-Asp-L-Cys-Gly, alpha-L-Asp-L-Cys-Gly and alpha-D-Asp-L-Cys-Gly) shows the specificity of the protection and rules out any non-enzymic component. Inhibitors of selenium-dependent glutathione peroxidase (mercaptosuccinate at 50 microM) and phospholipid hydroperoxide glutathione peroxidase (iodoacetate, 1 mM + glutathione, 0.5 mM) do not inhibit the glutathione-dependent protection of rat liver microsomes against lipid peroxidation. Purified microsomal glutathione transferase, NADPH-cytochrome P450 reductase and cytochrome P450 were reconstituted in microsomal phospholipid vesicles by cholate dialysis. The resulting membranes contained functional enzymes and did display enzymic lipid peroxidation induced by 75 microM NADPH and 10 microM Fe-EDTA (2:1). This model system was used to investigate whether microsomal glutathione transferase could inhibit lipid peroxidation in a glutathione-dependent manner. The results show that 5 mM glutathione did inhibit lipid peroxidation when functional microsomal glutathione transferase was included. This was not the case when the enzyme had been pre-inactivated with diethylpyrocarbonate. Furthermore, the protective effect of glutathione could be partly reversed by an inhibitor (100 microM bromosulphophtalein) of the enzyme. Apparently, rat liver microsomal glutathione transferase has the capacity to inhibit lipid peroxidation in a reconstituted system.

Amino Acid Sequence↗
PubMed1989

Purification of cytosolic glutathione transferases from Schistocephalus solidus (plerocercoid): interaction with anthelmintics and products of lipid peroxidation.

Glutathione (GSH) transferase isoenzymes have been partially resolved from the cytosol of Schistocephalus solidus (plerocercoid) by GSH affinity chromatography and chromatofocusing at pH 7-5. The presence of isomeric forms was also suggested by analytical isoelectric focusing and high-performance liquid chromatography (HPLC). Gel filtration and sodium dodecyl sulphate-polyacrylamide gel electrophoresis indicated that GSH transferase forms were dimers with a subunit size of approximately 24 kDa. The major GSH transferase form in S. solidus (plerocercoid) showed greater biochemical relationship to the Mu family of mammalian GSH transferase compared to the mammalian Alpha or Pi families. The major subunit purified by GSH affinity chromatography and reversed-phase HPLC also showed high N-terminal homology with the Mu family. A minor GSH transferase form appeared more biochemically related to the Alpha family with respect to substrate specificity and inhibitor sensitivity. The major GSH transferase was inhibited by haematin-related compounds, bile acids and a number of anthelmintics including members of the benzimidazole and phenol-based class of compounds. The major GSH transferase had conjugating activity with members of the trans, trans-2,4-alkadienal and trans-2-alkenal series, secondary products of lipid peroxidation.

Amino Acid Sequence↗
PubMed1989

Role of a partially purified glutathione S-transferase from rat liver nuclei in the inhibition of nuclear lipid peroxidation.

Glutathione protects isolated rat liver nuclei against lipid peroxidation by inducing a lag period prior to the onset of peroxidation. This GSH-dependent protection was abolished by exposing isolated nuclei to the glutathione S-transferase inhibitor S-octylglutathione. In incubations containing 0.2 mM S-octylglutathione, the GSH-induced lag period was reduced from 30 to 5 min. S-Octylglutathione (0.2 mM) also completely inhibited nuclear glutathione S-transferase activity and reduced glutathione peroxidase activity by 85%. About 70% of the glutathione S-transferase activity associated with isolated nuclei was solubilized with 0.3% Triton X-100. This solubilized glutathione S-transferase activity was partially purified by utilizing a S-hexylglutathione affinity column. The partially purified nuclear glutathione S-transferase exhibited glutathione peroxidase activity towards lipid hydroperoxides in solution. The data from the present study indicate that a glutathione S-transferase associated with the nucleus may contribute to glutathione-dependent protection of isolated nuclei against lipid peroxidation. Evidence was obtained which indicates that this enzyme is distinct from the microsomal glutathione S-transferase.

Animals↗
PubMed1991

Selective release of glutathione transferase subunits from primary cultured rat hepatocytes by carbon tetrachloride and deoxycholic acid.

The change in the activity of glutathione (GSH) transferases by carbon tetrachloride or deoxycholic acid, which induced hepatotoxicity, was studied using primary cultured rat hepatocytes. The activity of GSH transferases in the hepatocytes was decreased after the treatment with carbon tetrachloride or deoxycholic acid in their concentration- and incubation time-dependent manners. On the other hand, these compounds elicited the release of the activity of GSH transferases into the medium. Glycyrrhizin, an antihepatotoxic agent, inhibited the release of both aspartate transaminase (AST) and GSH transferases induced by carbon tetrachloride or deoxycholic acid. All subunits comprised of GSH transferases could not be released by these compounds. The main subunits of GSH transferases released by hepatotoxicity were identified as 3 and 4. These results indicate that hepatotoxicity is accompanied by the selective release of GSH transferase isozymes (class mu) following the loss of the enzymes activity in the cells.

Animals↗
PubMed1980

Induction of glutathione S-transferases A, B and C in rat liver cytosol by trans-stilbene oxide.

The cytoplasmic glutathione S-transferase activity of rat liver has been shown to increase to 300--400% of control values after treatment of the animals with trans-stilbene oxide and this phenomenon has been further characterized in the present study. Quantitative immunological determinations showed that the content of glutathione S-transferases A, B and C together constituted 4.5% of the soluble proteins in the hepatic cytoplasm of untreated rats. The content rose to 12.9 and 17.4% after treatment with trans-stilbene oxide or a combination of trans-stilbene oxide, 3-methylcholanthrene and phenobarbital, respectively. It was demonstrated that the cytosolic fraction from induced liver contains 4.2 times as much antigen which can be precipitated with antiglutathione S-transferase B antiserum as does control cytosol. Antiglutathione S-transferase C, which intereacts with transferases A and C, precipitates 3.3 times as much protein from the induced cytosol compared with control. Crossed immunoelectrophoresis and purification demonstrated that both A and C are increased in amount after treatment with trans-stilbene oxide. Thus, cytosolic glutathione S-transferases A, B, and C in liver are all induced by treatment of rats with trans-stilbene oxide. Immunological crossreaction, similar behavior during chromatography on CM-cellulose and hydroxyapatite and similar specific activities suggest that the control and induced enzymes are essentially identical, trans-Stilbene oxide was found to serve as a relatively poor second substrate for glutathione S-transferases A, B and C and can thus be said to cause substrate induction of these enzymes.

Animals↗
PubMed1989

Site-directed inactivation of human lung acidic glutathione S-transferase by 1-chloro-2,4-dinitrobenzene in the absence of glutathione.

Human lung acidic glutathione S-transferase is irreversibly inhibited by 1-chloro-2,4-dinitrobenzene (CDNB) in the absence of the co-substrate glutathione (GSH). The time-dependent inactivation is pseudo-first-order and demonstrates saturation kinetics, suggesting that inactivation occurs from an EI complex. The Ki was 0.14 mM; and kobs was 0.32 min-1 at 0.6 mM CDNB. The enzyme was protected against CDNB inactivation by GSH. The other two classes of glutathione S-transferase, the basic and near-neutral, are not significantly inactivated by CDNB. Incubation with [14C]CDNB indicated covalent binding to all three classes of transferase. One peptide fraction was found to be radiolabelled in both the basic and acidic transferases when these were incubated with [14C]CDNB and GSH, cleaved with cyanogen bromide, and chromatographed by HPLC. Incubation in the absence of GSH yielded one and two additional labelled peptide fractions for the basic and acidic transferases, respectively. Our results suggest that while CDNB arylates all three classes of human transferases, only the acidic transferase possesses a specific GSH-sensitive CDNB binding site, binding to which leads to time-dependent inactivation.

Binding Sites↗
PubMed1988

Acidic glutathione transferase from human heart. Characterization and N-terminal sequence determination.

The anionic glutathione transferase of human heart has been purified to homogeneity by using DEAE-cellulose, affinity chromatography, and FPLC. The enzyme has an isoelectric point at pH 4.75 and has an electrophoretic mobility on SDS-PAGE identical to placental transferase pi, indicating that the heart enzyme is formed by two similar subunits of 23,000 Mr. Upon isoelectric focusing on ampholine PAG plates the enzyme recovered from FPLC gave two bands of activity at pH 4.75 and 4.9 which were reduced to essentially a single band at pH 4.75 after incubation with dithiothreitol. In the immunodiffusion experiment, the heart enzyme gave a positive precipitin line with the antibodies against transferase pi but not with antibodies prepared against the "basic" transferase of human skin or against the "near-neutral" transferase of human uterus. The substrate specificities, the sensitivities to characteristic inhibitors, the amino acid composition, together with the immunological studies, strongly indicate that the anionic enzyme of human heart is closely related to the transferase pi of human placenta. The N-terminal amino acid sequence of the first 48 residues was determined and compared with the N-terminal region of other reported human glutathione transferase sequences. The heart enzyme differs from the placental enzyme in a single residue (Trp instead of Arg in the 28th position) further supporting their similarity.

Amino Acid Sequence↗
PubMed1998

Plasma glutathione S-transferase alpha 1-1: a more sensitive marker for hepatocellular damage than serum alanine aminotransferase in hypertensive disorders of pregnancy.

OBJECTIVE: Our purpose was to investigate the value of plasma glutathione S-transferase Alpha 1-1 measurements in the assessment of hepatocellular damage in hypertensive disorders of pregnancy. STUDY DESIGN: Patients were recruited at the Department of Obstetrics and Gynecology of the University Hospital, Nijmegen, The Netherlands. Five groups of patients were studied: normotensive pregnancy (n = 87), pregnancy-induced hypertension (n = 48), preeclampsia (n = 79), the syndrome of hemolysis, elevated liver enzymes, and low platelets (n = 39), and serially studied normotensive pregnancy (n = 21). Blood was collected for assessment of plasma glutathione S-transferase Alpha 1-1 levels and serum alanine aminotransferase activity. Levels in hypertensive pregnancies were compared with levels in normotensive pregnancy by the Mann-Whitney U test. Patients were categorized according as to whether their values are below (normal) or above (elevated) the upper normal reference level. The difference in relative magnitude of elevation between the two factors was determined by the Wilcoxon matched-pairs signed-rank test. RESULTS: Plasma levels in the longitudinally studied normotensive pregnancy group did not differ between gestational ages and were not significantly different from those of the normotensive control group. Median levels of glutathione S-transferase Alpha 1-1 and alanine aminotransferase were significantly increased (p < 0.01, p < 0.0001, respectively) in all subgroups of hypertensive pregnancies compared with normotensive pregnancies. When both levels were elevated, the relative magnitude of the increase of glutathione S-transferase Alpha 1-1 levels was significantly higher than that of alanine aminotransferase activity in preeclampsia (p < 0.01) and the syndrome of hemolysis, elevated liver enzymes, and low platelets (p < 0.0001). Almost half the patients with preeclampsia showed elevated levels of alanine aminotransferase and/or glutathione S-transferase Alpha 1-1. CONCLUSION: Plasma glutathione S-transferase Alpha 1-1 measurements may provide a more sensitive indicator of acute hepatic damage in preeclampsia and the syndrome of hemolysis, elevated liver enzymes, and low platelets compared with the assessment of aminotransferase activity and therefore may allow earlier recognition of these syndromes. The clinical benefits of plasma measurements of glutathione S-transferase Alpha 1-1 for monitoring the hepatic condition in the management of these patients need to be elucidated in further studies.

Adolescent↗