Tissue distribution of enzymic methylation of glutathione <i>S</i>-transferase and its effects on catalytic activity. Methylation of glutathione <i>S</i>-transferase 11-11 inhibits conjugating activity towards 1-chloro-2,4-dinitrobenzene

Johnson, Jeffrey A.; Finn, K A; Siegel, Frank L.

doi:10.1042/bj2820279

Cited by 50 publications

(32 citation statements)

References 53 publications

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“…In all three (mouse, rat, human) species studied these forms were found primarily in testis and to a lesser extent in brain (12)(13)(14)(15). Other tissues are virtually devoid of this GST isoform (12).…”

Section: Discussionmentioning

confidence: 99%

“…Indeed, this study establishes that a labile and poorly characterized rat subunit previously designated as Yo or GST 11 (14,16,17) and mouse mGSTM5 are similar to the human hGSTM3 subunit in terms of structure, catalytic mechanisms, tissueselective expression patterns, and other unique properties.…”

mentioning

confidence: 99%

“…Mammalian GSTs are expressed in discrete tissue-specific patterns. For instance livers of some species are rich in Alphaand some Mu-class GSTs but do not contain Pi, yet some Mu subunits not present in liver are major components in certain extrahepatic tissues (12)(13)(14).…”

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confidence: 99%

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Rationale for Reclassification of a Distinctive Subdivision of Mammalian Class Mu Glutathione S-Transferases That Are Primarily Expressed in Testis

Rowe¹,

Patskovsky

Patskovska

et al. 1998

Journal of Biological Chemistry

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A rat testicular Mu-class glutathione S-transferase (GST) resolved by reversed-phase high performance liquid chromatography cross-reacted with peptide sequence-specific antisera raised against the human hGSTM3 subunit. Electrospray ionization mass spectrometry indicated that this rat GST subunit (designated rGSTM5 in this report) has a significantly greater molecular mass (26,541 Da) than the other rat GST subunits. The mouse homologue (mGSTM5 subunit) was also identified and characterized by high performance liquid chromatography and electrospray ionization mass spectrometry. Sequence analysis of rGSTM5 peptide fragments and the sequence deduced from a cDNA clone showed that the protein is highly homologous to the hGSTM3 and murine mGSTM5 subunits. All three GSTs of this subclass have N-and C-terminal extensions with Cterminal cysteine residues, but the two penultimate amino acids near the C terminus are divergent in the three species. The proteins of this class Mu subfamily have similar catalytic specificities and mechanisms, are all cysteine rich, are found mainly in testis, and share characteristics that distinguish them from other GSTs. Moreover, the rGSTM5 subunit isolated from rat testis was not found in heterodimeric combination with other common Mu-class GST subunits. As the rGSTM5, mGSTM5, and hGSTM3 subunits are structurally more closely related to each other than they are to other Mu GSTs, it is proposed that they be considered a functionally distinct and separate subfamily within class Mu. The identification of this unique mammalian GST subclass could advance strategies for interspecies comparisons of GSTs and provides a rodent model for studies on functions and regulatory mechanisms for human GSTs.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Rationale for Reclassification of a Distinctive Subdivision of Mammalian Class Mu Glutathione S-Transferases That Are Primarily Expressed in Testis

Rowe¹,

Patskovsky

Patskovska

et al. 1998

Journal of Biological Chemistry

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“…Cytosolic rat liver GSTs were phosphorylated by a Ca 2ϩ -phospholipid-dependent protein kinase from rabbit brain (Taniguchi and Pyerin, 1989). In vitro, calmodulinstimulated (Johnson et al, 1990) and methyltransferasecatalyzed methylation (Johnson et al, 1992) of rat liver cytosolic GSTs has been reported. There is one report of glycosylated GSTs in mammals.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of GlutathioneS-Transferase Isozymes from Sorghum1

1998

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Two glutathione S-transferase (GST) isozymes, A1/A1 and B1/B2, were purified from etiolated, O-1,3-dioxolan-2-yl-methyl-2,2,2,-trifluoro-4 -chloroacetophenone-oxime-treated sorghum (Sorghum bicolor L. Moench) shoots. GST A1/A1, a constitutively expressed homodimer, had a subunit molecular mass of 26 kD and an isoelectric point of 4.9. GST A1/A1 exhibited high activity with 1-chloro-2, 4,dinitrobenzene (CDNB) but low activity with the chloroacetanilide herbicide metolachlor. For GST A1/A1, the random, rapidequilibrium bireactant kinetic model provided a good description of the kinetic data for the substrates CDNB and glutathione (GSH). GST B1/B2 was a heterodimer with subunit molecular masses of 26 kD (designated the B1 subunit) and 28 kD (designated the B2 subunit) and a native isoelectric point of 4.8. GST B1/B2 exhibited low activity with CDNB and high activity with metolachlor as the substrate. The kinetics of GST B1/B2 activity with GSH and metolachlor fit a model describing a multisite enzyme having two binding sites with different affinities for these substrates. Both GST A1/A1 and GST B1/B2 exhibited GSH-conjugating activity with ethacrynic acid and GSH peroxidase activity with cumene hydroperoxide, 9-hydroperoxy-trans-10,cis-12-octadecadienoic acid and 13-hydroperoxy-cis-9,trans-11-octadecadienoic acid. Both GST A1/A1 and GST B1/B2 are glycoproteins, as indicated by their binding of concanavalin A. Polyclonal antibodies raised against GST A1/A1 exhibited cross-reactivity with the B1 subunit of GST B1/B2. Comparisons of the N-terminal amino acid sequences of the GST A1, B1, and B2 subunits with other type I -GSTs indicated a high degree of homology with the maize GST I subunit and a sugarcane GST.GSTs (EC 2.5.1.18) are dimeric enzymes found in mammals, insects, plants, and microbes that catalyze nucleophilic attack by the thiolate anion of GSH at electrophilic centers of hydrophobic molecules (Mannervik and Danielson, 1988). In addition to catalyzing GSH conjugation, GSTs also exhibit GSH peroxidase activity and ligandbinding functions (Mannervik and Danielson, 1988;Marrs, 1996). Mammalian GSTs compose a multigene family; in rat liver at least 13 different cytosolic GST subunits are found as either heterodimers or homodimers . Mammalian cytosolic GSTs have been divided into four classes (␣, , , and ) based on immunological, biochemical, and sequence similarities (Buetler and Eaton, 1992). It is well established that mammalian GSTs play an important role in the detoxification of electrophilic xenobiotics (Mannervik and Danielson, 1988). Although endogenous substrates for mammalian GSTs have not been clearly defined, there is evidence that ␣-GSTs protect against oxidative stress by detoxifying reactive products generated by lipid peroxidation (Ålin et al., 1985;Ketterer and Coles, 1991;Singhal et al., 1992).In general, plant GSTs have not been as well characterized as mammalian GSTs. Plant cytosolic GSTs belong to the archaic class of GSTs (Meyer et al., 1991;Marrs, 1996). This class, which is very heterog...

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“…Tissue-specific differences in the post-translational modifications, such as glycosylation, phosphorylation, and carboxymethylation have been associated with tissue-dependent activities of some GSTs (Johnson et al, 1992), but studies done with electrospray mass spectrometry identified N-terminal acetylation of GSTs as the only natural modification of a variety of GSTs (Rowe et al, 1997). The amino acid sequence of GSTZ1-1 contains putative glycosylation and phosphorylation sights, but no evidence for post-translational modification of hepatic GSTZ1-1 has been presented (Tong et al, 1998a).…”

Section: Fig 9 Immunohistochemical Detection Of Gstz1-1 In Rat Adrementioning

confidence: 99%

Immunohistochemical Localization and Activity of Glutathione Transferase Zeta (GSTZ1–1) in Rat Tissues

Lantum

Baggs²,

Krenitsky³

et al. 2002

Drug Metabolism and Disposition

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ABSTRACT:Glutathione transferase zeta (GSTZ1-1) catalyzes the biotransformation of a range of ␣-haloacids, including dichloroacetic acid (DCA), and the penultimate step in the tyrosine degradation pathway. DCA is a rodent carcinogen and a common drinking water contaminant. DCA also causes multiorgan toxicity in rodents and dogs. The objective of this study was to determine the expression and activities of GSTZ1-1 in rat tissues with maleylacetone and chlorofluoroacetic acid as substrates. GSTZ1-1 protein was detected in most tissues by immunoblot analysis after immunoprecipitation of GSTZ1-1 and by immunohistochemical analysis; intense staining was observed in the liver, testis, and prostate; moderate staining was observed in the brain, heart, pancreatic islets, adrenal medulla, and the epithelial lining of the gastrointestinal tract, airways, and bladder; and sparse staining was observed in the renal juxtaglomerular regions, skeletal muscle, and peripheral nerve tissue. These patterns of expression corresponded to GSTZ1-1 activities in the different tissues with maleylacetone and chlorofluoroacetic acid as substrates. Specific activities ranged from 258 ؎ 17 (liver) to 1.1 ؎ 0.4 (muscle) nmol/min/mg of protein with maleylacetone as substrate and from 4.6 ؎ 0.89 (liver) to 0.09 ؎ 0.01 (kidney) nmol/min/mg of protein with chlorofluoroacetic acid as substrate. Rats given DCA had reduced amounts of immunoreactive GSTZ1-1 protein and activities of GSTZ1-1 in most tissues, especially in the liver. These findings indicate that the DCA-induced inactivation of GSTZ1-1 in different tissues may result in multiorgan disorders that may be associated with perturbed tyrosine metabolism.Glutathione transferases (GST 1 ) are a multigene family of phase II drug-metabolizing enzymes that catalyze the conjugation of glutathione with a range of endogenous and exogenous substrates (Armstrong, 1997;Salinas and Wong, 1999). Soluble and membrane-bound GSTs are expressed in many tissues, and soluble GSTs constitute 1 to 5% of total cytosolic protein (Morgenstern et al., 1984;Sundberg et al., 1993;Rowe et al., 1997). Activities with model substrates and the subcellular localization of GSTA, GSTM, GSTP, GSTT, and GSTO class GSTs and of microsomal GST1 have been previously characterized (Meyer et al., 1991;Hiratsuka et al., 1994;Mannervik and Widersten, 1995;Armstrong, 1997;Otieno et al., 1997;Yin et al., 2001).The expression of GSTs is regulated pre-and post-translationally in a tissue-specific manner resulting in protein products that differ quantitatively in different tissues (Tu et al., 1983;Rozell et al., 1993;Rowe et al., 1997). Testes express the highest amount of total GST protein per milligram cytosolic protein followed by the liver, brain, pancreas, adrenals, heart, and lung (DePierre and Morgenstern, 1983;Listowsky et al., 1998). Major GST-expressing tissues are the principal sites for drug and chemical metabolism indicative of the role of GSTs in the biotransformation of xenobiotics (Pabst et al., 1973;Armstrong, 1997). Studies...

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Tissue distribution of enzymic methylation of glutathione S-transferase and its effects on catalytic activity. Methylation of glutathione S-transferase 11-11 inhibits conjugating activity towards 1-chloro-2,4-dinitrobenzene

Cited by 50 publications

References 53 publications

Rationale for Reclassification of a Distinctive Subdivision of Mammalian Class Mu Glutathione S-Transferases That Are Primarily Expressed in Testis

Rationale for Reclassification of a Distinctive Subdivision of Mammalian Class Mu Glutathione S-Transferases That Are Primarily Expressed in Testis

Isolation and Characterization of GlutathioneS-Transferase Isozymes from Sorghum1

Immunohistochemical Localization and Activity of Glutathione Transferase Zeta (GSTZ1–1) in Rat Tissues

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