scholarly journals Quantification of human hepatic glutathione S-transferases

1990 ◽  
Vol 269 (3) ◽  
pp. 609-613 ◽  
Author(s):  
B van Ommen ◽  
J J P Bogaards ◽  
W H M Peters ◽  
B Blaauboer ◽  
P J van Bladeren
Keyword(s):  
Genetic Polymorphism ◽  
Hepatic Tissue ◽  
Glutathione S Transferase ◽  
Interindividual Differences ◽  
Alpha Subunits ◽  
Trans Stilbene ◽  
Hepatic Glutathione ◽  
Basic Class ◽  
Glutathione S Transferases ◽  
Tissue Specimens

Human hepatic glutathione S-transferase (GST) subunits were characterized and quantified with the aid of a recently developed h.p.l.c. method. In 20 hepatic tissue specimens the absolute amounts of the basic Class Alpha subunits B1 and B2, the near-neutral Class Mu subunits mu and psi and the acidic subunit pi were determined. The average total amount of GST was 37 micrograms/mg of cytosolic protein, with the Class Alpha GST being the predominant class (84% of total GSTs), and pi as the sole representative of the Class Pi GSTs present in the lowest concentration (4% of total GSTs). Large interindividual differences were observed for all subunits, with variations up to 27-fold, depending on the subunit. For the Class Alpha GST-subunits B1 and B2, a biphasic ratio was observed. The genetic polymorphism of the subunits mu and psi was confirmed by h.p.l.c. analysis, and correlated with the enzymic glutathione conjugation of trans-stilbene oxide and with Western blotting of cytosols, using a monoclonal anti-(Class Mu GST) antibody. Of the 20 livers examined, ten contained only mu, whereas the occurrence of psi alone, and the combination of mu and psi, were found in only one liver each.

scholarly journals Purification and characterization of hepatic glutathione S-transferases of rhesus monkeys. A family of enzymes similar to the human hepatic glutathione S-transferases

1988 ◽  
Vol 251 (1) ◽  
pp. 81-88 ◽  
Author(s):  
R M Hoesch ◽  
T D Boyer
Keyword(s):  
Peroxidase Activity ◽  
Rhesus Monkeys ◽  
Affinity Column ◽  
Terminal Sequence ◽  
Glutathione S Transferase ◽  
Substrate Specificities ◽  
High Affinity ◽  
Human Enzyme ◽  
Hepatic Glutathione ◽  
Glutathione S Transferases

Thirteen forms of glutathione S-transferase were purified from the livers of female rhesus monkeys (Macaque mulatta). Most (74.7%) of the activity in the hepatic cytosol adhered well to the GSH affinity column and could be eluted only with the addition of GSH to the eluting buffer. The predominant isoenzymes (n = 5) in this ‘high-affinity’ fraction had alkaline pI values (greater than 9.0) and contained a subunit with an Mr value of 24,000. All of these isoenzymes had high organic peroxidase activity and, on the basis of amino acid analysis, substrate specificities and affinity for non-substrate ligands, appear to belong to the family of glutathione S-transferases that have been termed alpha [Mannervik, Alin, Guthenberg, Jensson, Tahir, Warholm & Jörnvall (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7202-7206]. Also within the high-affinity fraction was an isoenzyme with an acidic (5.8) pI value. This acidic isoenzyme was composed of a unique subunit (Mr 23,000). The N-terminal sequence (ten residues) of this acidic enzyme was identical with that of a human form that is referred to as pi. The predominant form of enzyme in the ‘low-affinity’ (eluted from the GSH affinity column with an increase in buffer pH) fraction was a homodimer of a 26,000-Mr subunit. It had an alkaline pI (greater than 9.0) but it lacked organic peroxidase activity. The N-terminal sequence (ten residues) of this enzyme was identical with that of a human enzyme referred to as mu. The substrate specificities and affinity for non-substrate ligands of this monkey enzyme also were similar to those of the human enzyme. In conclusion, the liver cytosol of rhesus monkeys contains a number of glutathione S-transferase isoenzymes that are very similar to the human hepatic enzymes.

scholarly journals The hypothalamic–hypophyseal–gonadal regulation of hepatic glutathione S-transferases in the rat

1981 ◽  
Vol 198 (1) ◽  
pp. 211-217 ◽  
Author(s):  
Coral A. Lamartiniere
Keyword(s):  
Adult Male ◽  
Sexual Differentiation ◽  
Male Rats ◽  
Adult Males ◽  
Glutathione S Transferase ◽  
Glutathione Conjugation ◽  
Inhibiting Factor ◽  
Hepatic Glutathione ◽  
Hypophysectomized Rats ◽  
Glutathione S Transferases

Hepatic glutathione S-transferase activities were determined with the substrates 1,2-dichloro-4-nitrobenzene and 1-chloro-2,4-dinitrobenzene. Sexual differentiation of glutathione S-transferase activities is not evident during the prepubertal period, but glutathione conjugation with 1,2-dichloro-4-nitrobenzene is 2–3-fold greater in adult males than in females. Glutathione conjugation with 1-chloro-2,4-dinitrobenzene is slightly higher in adult males than adult females. No change in activity was observed after postpubertal gonadectomy of males or females. Neonatal castration of males results in a significant decrease in glutathione conjugation with 1,2-dichloro-4-nitrobenzene. Hypophysectomy, or hypophysectomy followed by gonadectomy did result in significantly higher glutathione S-transferase activities in both sexes. These increases can be reversed by implanting an adult male or female pituitary or four prepubertal pituitaries under the kidney capsule. Postpubertal sexual differentiation of glutathione S-transferase activities is neither dependent on pituitary sexual differentiation nor pituitary maturation. Prolactin concentrations are inversely related to glutathione S-transferase activities in hypophysectomized rats with or without ectopic pituitaries. Somatotropin exogenously administered to hypophysectomized rats results in decreased glutathione S-transferase activities, whereas prolactin has no effect. Adult male rats treated neonatally with monosodium l-glutamate to induce arcuate nucleus lesions of the hypothalamus have decreased glutathione S-transferase activities towards 1,2-dichloro-4-nitrobenzene and decreased somatotropin concentrations. Our experiments suggests that sexual differentiation of hepatic glutathione S-transferase is a result of a hypothalamic inhibiting factor in the male (absent in the female). This postpubertally expressed inhibiting factor acts on the pituitary to prevent secretion of a pituitary inhibiting factor (autonomously secreted by the female), resulting in higher glutathione S-transferase activities in the adult male than the adult female.

scholarly journals Developmental aspects of glutathione S-transferase B (ligandin) in rat liver

1976 ◽  
Vol 160 (2) ◽  
pp. 231-236 ◽  
Author(s):  
B F Hales ◽  
A H Neims
Keyword(s):  
The Other ◽  
Male Rats ◽  
Transferase Activity ◽  
Sprague Dawley ◽  
Glutathione S Transferase ◽  
Sprague Dawley Rats ◽  
Hepatic Glutathione ◽  
Glutathione S Transferases ◽  
Parallel Fashion ◽  
Induction By Phenobarbital

The postnatal development in male Sprague-Dawley rats of hepatic glutathione S-transferase B (ligandin) in relation to the other glutathione S-transferases is described. The concentration of glutathione S-transferase B in 1-day-old male rats is about one-fifth of that in adult animals. The enzyme reaches adult concentrations 4-5 weeks later. When assessed by substrate specificity or immunologically, the proportion of transferase B relative to the other glutathione S-transferases is high during the first week after birth. At this age, 67.5% of the transferase activity towards 1-chloro-2,4-dinitrobenzene is immunoprecipitable by anti-(transferase B), compared with about 50% in adults and older pups. Between the second and the fifth postnatal week, the fraction of transferase B increases in parallel fashion with the other transferases in hepatic cytosol. Neither L-thyroxine nor cortisol induce a precocious increase in glutathione S-transferase activity. Phenobarbital did induce transferase activity towards 1-chloro-2,4-dinitrobenzene and 1,2-dichloro-4-nitrobenzene in both pups and adults. The extent of induction by phenobarbital was a function of basal activity during development such that the percentage stimulation remained constant from 5 days postnatally to adulthood.

Analysis of glutathione S-transferase genes polymorphisms and the risk of schizophrenia in a sample of Iranian population

2011 ◽  
Vol 7 (2-4) ◽  
pp. 199-203 ◽  
Author(s):  
Farah Lotfi Kashani ◽  
Dor Mohammad Kordi-Tamandani ◽  
Roya Sahranavard ◽  
Mohammad Hashemi ◽  
Farzaneh Kordi-Tamandani ◽  
...  
Keyword(s):  
Genomic Dna ◽  
Case Control Study ◽  
Gene Interaction ◽  
Case Control ◽  
Glutathione S Transferase ◽  
Chain Reaction ◽  
Healthy Control ◽  
Glutathione S Transferases ◽  
Polymerase Chain ◽  
Control Study

Glutathione S-transferases (GSTs) are major intracellular antioxidants, which, impaired in their function, are involved in the progress of schizophrenia (SCZ). The aim of this case-control study was to investigate the association between the polymorphism of glutathione S-transferases M1 (GSTM1), T1 (GSTT1), the glutathione S-transferase P1 gene (GSTP1) and SCZ. We isolated genomic DNA from peripheral blood of 93 individuals with SCZ and 99 healthy control subjects' genotypes analyzing them for GSTM1, GSTT1 and GSTP1 using polymerase chain reaction. The analysis of the gene–gene interaction between GSTs indicated that the magnitude of the association was greater for the combined AG/GSTT1 & GSTM1 genotypes (OR = 2.51; 95% CI: 1.13–5.63, P = 0.02). The AG and combined AG + GG genotypes of GSTP1 increased the risk of SCZ (OR = 1.83; 95% CI: 0.94–3.75 and OR = 1.71; 95% CI: 0.92–3.19, respectively). The genotypes of GSTT/NULL, NULL/GSTM and NULL/NULL increased the risk of SCZ (OR = 2.05; 95% CI: 0.9–4.74; OR = 2.0; 95% CI: 1.68–2.31; and OR = 1.8; 95% CI: 0.57–2.46, respectively). The present study supports previous data that suggest that impairment in the function of GSTs genes may increase the risk of SCZ.

scholarly journals Genetic polymorphism of epoxide hydrolase and glutathione S-transferase in COPD

2004 ◽  
Vol 23 (6) ◽  
pp. 818-824 ◽  
Author(s):  
S‐L. Cheng ◽  
C‐J. Yu ◽  
C‐J. Chen ◽  
P‐C. Yang
Keyword(s):  
Genetic Polymorphism ◽  
Epoxide Hydrolase ◽  
Glutathione S Transferase
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