Rat spleen glutathione transferases. A new acidic form belonging to the Alpha class

Tsuchida, Shigeki; Sato, Kei

doi:10.1042/bj2660461

Cited by 11 publications

(6 citation statements)

References 30 publications

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“…Therefore rGSTA6* and Y1 are probably different proteins. Whether subunit A6* is the equivalent of GST A(6) from liver [11] or subunit pl 5.8 from spleen [49] remains to be investigated.…”

Section: Ms and Sequencing Analysis Of Rgsta6*mentioning

confidence: 99%

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Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-Alpha GST, rGSTA6*, in rat testis

Hsieh

Tsai

Yeh

et al. 1997

Biochemical Journal

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Cytosolic glutathione S-transferases (GSTs) from rat ovaries and testis were purified by a combination of GSH and S-hexylglutathione affinity chromatography. The isolated GSTs were subjected to reverse-phase HPLC, electrospray MS and Nterminal peptide sequencing analysis. The major GST isoenzymes expressed in ovaries are subunits A3, A4, M1, M2 and P1. Other isoenzymes detected are subunits A1, M3 and M6*. In rat testis, the major GST isoenzymes expressed are subunits A3, M1, M2, M3, M5* and M6*. Subunits A1, A4 and P1 are expressed in lesser amounts. We could not detect post-translational

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“…Therefore rGSTA6* and Y1 are probably different proteins. Whether subunit A6* is the equivalent of GST A(6) from liver [11] or subunit pl 5.8 from spleen [49] remains to be investigated.…”

Section: Ms and Sequencing Analysis Of Rgsta6*mentioning

confidence: 99%

“…protein with pl 5.8 from spleen [49]. We have reanalysed the male rat kidney and liver GSTs isolated by the coupled affinity chromatography method.…”

Section: Ms and Sequencing Analysis Of Rgsta6*mentioning

confidence: 99%

Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-Alpha GST, rGSTA6*, in rat testis

Hsieh

Tsai

Yeh

et al. 1997

Biochemical Journal

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“…Cytosolic GSTs are present in most mammalian organs and exist as dimeric proteins consisting of two identical or closely related subunits from the same class (LY, p, K, 8;Mannervik and Danielson, 1988;Meyer et al, 199 1). Rat tissues contain at least 20 dimers made up of 15 different subunits (Tu et al, 1983;Ketterer et al, 1988;Mannervik and Danielson, 1988;Kispert et al, 1989;Hayes et al, 1990a,b;Hiratsuka et al, 1990;Tsuchida and Sato, 1990;Harris et al, 199 1;Hayes et al, 199 1;Meyer et al, 199 1). Microsomal GST is a homotrimer consisting of a subunit that is structurally distinct from the cytosolic enzymes (Morgenstern and DePierre, 1985;Morgenstern et al, 1985).…”

mentioning

confidence: 99%

Glutathione S-transferase isoenzymes in rat brain neurons and glia

et al. 1993

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The glutathione S-transferases (GSTs) constitute a family of cytosolic isoenzymes and a structurally unrelated microsomal enzyme that is involved in the detoxication of electrophilic xenobiotics. These enzymes also participate in the intracellular binding and transport of a broad range of lipophilic compounds including bilirubin, and hormones such as the glucocorticoids and thyroid hormones. The present investigation demonstrates that GSTs are present in neurons of the brainstem, forebrain, and cerebellum. An isoenzyme-specific distribution of GSTs was found in cytoplasm, nuclei, and nucleoli. The regional and cellular distribution of cytosolic GSTs in the brain was studied by immunohistochemistry, spectrophotometric enzyme assay, and reverse-phase HPLC. Polyclonal antibody against microsomal GST was strongly reactive with Purkinje cells throughout the cerebellar cortex, and with neurons in the brainstem and hippocampus. Nuclei of Purkinje cells and of neurons in the brainstem, hippocampus, and cerebral cortex were immunopositive for alpha-class GST 1-1 (YaYa), whereas alpha-class GST 2-2 (YcYc) antibody was consistently immunoreactive with the nucleolus, but not with the nucleus or soma. All alpha-class GST antibodies studied were reactive, to various degrees, with astrocytes and choroid plexus; however, ependymal cells of the subventricular zones were immunonegative. alpha-class GST 8-8 (YkYk) immunoreactivity was specifically localized to endothelial cells and/or astrocytic end feet associated with blood vessels. Reverse-phase HPLC indicated that there were also substantial regional differences in the pattern of alpha-, mu-, and pi-class GST subunit expression. For example, the thalamus/hypothalamus had the highest GST activity and greatest concentration of total GST protein and mu-class GST subunit 6 (Yb3), whereas the brainstem had the greatest concentration of pi-class GST subunit (Yp). This regional variation in GST expression may be reflective of regional differences in cell populations. In cerebellar cortex, the concentration of mu-class GST subunit 4 (Yb2) was greatest in the flocculus and lowest in the vermis. This is of clinical interest because the pattern of expression of mu-class GST subunit 4 (Yb2) in the cerebellum coincides with the known regional susceptibility of this structure to degeneration after exposure to toxic or metabolic insults. The vermis is most susceptible to these insults, whereas the lateral lobes and flocculus are most resistant.(ABSTRACT TRUNCATED AT 400 WORDS)

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“…Cytosolic GSTs are dimeric proteins consisting of two identical or closely related subunits from the same class (Alpha, Mu, Pi or Theta; Mannervik and Danielson, 1988;Meyer et al, 1991). These enzymes are present in most mammalian organs, and rat tissues contain at least 20 dimers of 15 different subunits (Tu et al, 1983;Mannervik and Danielson, 1988;Ketterer et al, 1988;Kispert et al, 1989;Hayes et al, 1990aHayes et al, ,b, 1991Hiratsuka et al, 1990;Tsuchida and Sato, 1990;Meyer et al, 1991;Harris et al, 1991). GST isoenzyme profiles are altered in preneoplastic foci, tumour tissue and multidrugresistant cell lines (Satoh et al, 1985;Cowan et al, 1986;Moscow et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Effects of hyperbilirubinaemia on glutathione S-transferase isoenzymes in cerebellar cortex of the Gunn rat

Johnson

Hayward

Kornguth

et al. 1993

Biochemical Journal

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The glutathione S-transferases (GSTs) are a family of isoenzymes involved in the detoxication of a variety of electrophilic xenobiotics. The present investigation demonstrates that GST activity and the concentration of cytosolic GSTs in cerebellar cortex of Gunn rats were increased in hyperbilirubinaemic animals compared with non-jaundiced controls. Age-dependent and region-specific increases in GST isoenzymes were seen in three regions of the cerebellar cortex of jaundiced Gunn rats, whereas GST concentrations were not altered in the brainstem, thalamus/hypothalamus, cortex or liver. Cytosolic GST activity was increased 1.3-fold in the flocculus and lateral hemispheres of 20-day-old and 1.7-fold in the flocculus, lateral hemispheres and vermis of 60-day-old jaundiced (jj; homozygous) Gunn rats compared with non-jaundiced (Jj; heterozygous) Gunn rats. H.p.l.c. was used to determine the GST subunit protein concentrations in cytosolic fractions isolated from liver and brain regions of jaundiced and non-jaundiced animals. In all regions of the cerebellum from 20-day-old animals, the levels of Alpha-class GST subunits 2 (Yc1; 3.0-fold) and 8 (Yk; 2.0-fold) were increased in jaundiced rats. In 60-day-old animals, the concentrations of Alpha-class GST subunits 2 (Yc1; 5.0-fold) and 8 (Yk; 3.0-fold), Mu-class subunit 11 (Yo; 2.5-fold) and Pi-class subunit 7 (Yp; 2.0-fold) were increased in all regions of cerebellar cortex of jaundiced animals. In cerebellum of 10-, 20- and 60-day-old non-jaundiced and jaundiced Gunn rats, the flocculus had the highest concentration of Mu-class GST subunit 4 (Yb2) and vermis the lowest; hyperbilirubinaemia increased the concentration of subunit 4 (Yb2; 3- to 5-fold) in the flocculus and lateral hemispheres, but not the vermis, of 20- and 60-day-old rats. Intraperitoneal injection of sulphadimethoxine, a long-acting sulphonamide which displaces bilirubin from its albumin-binding sites and increases the bilirubin levels in tissues, further increased the already elevated concentrations of GST subunits in the lateral regions of cerebellar cortex of hyperbilirubinaemic rats. For example, the concentration of subunit 4 (Yb2) was increased 2.2-fold (compared with non-jaundiced controls) in Gunn rats injected with saline and 7.4-fold in rats injected with 100 mg of sulphadimethoxine/kg body weight. In contrast, GSTs in the vermis of jaundiced animals were not affected by sulphadimethoxine injection. Sulphadimethoxine had no effect on GST concentrations in lateral regions and vermis of heterozygous (Jj) Gunn rats.(ABSTRACT TRUNCATED AT 400 WORDS)

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Rat spleen glutathione transferases. A new acidic form belonging to the Alpha class

Cited by 11 publications

References 30 publications

Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-Alpha GST, rGSTA6*, in rat testis

Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-Alpha GST, rGSTA6*, in rat testis

Glutathione S-transferase isoenzymes in rat brain neurons and glia

Effects of hyperbilirubinaemia on glutathione S-transferase isoenzymes in cerebellar cortex of the Gunn rat

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