Molecular cloning and amino acid sequencing of rat liver class theta glutathione S-transferase Yrs-Yrs inactivating reactive sulfate esters of carcinogenic arylmethanols

Ogura, K.; Nishiyama, Takahito; Okada, Takahito; Kajita, Jiro; Narihata, Hiroyuki; Watabe, Tetsuro; Hiratsuka, Akira; Watabe, Tadashi

doi:10.1016/0006-291x(91)92079-y

Cited by 53 publications

(35 citation statements)

References 25 publications

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“…The calculated molecular mass of the subunit encoded by MT1a (27 356 Da) is very similar to the molecular masses of rGSTT2 (26 000-27 311 Da ; [9,12]) and hGSTT2 (25 100-27 489 Da ; [5,7]), and slightly higher than those estimated for the mGSTT1 [15] and mGSTT2 [17] subunits reported recently. The discrepancies between the calculated and estimated molecular masses of mGSTT1 probably reflect migrational variation of the subunits in SDS\PAGE, however they fall within the expected experimental range.…”

Section: Properties Of the Encoded Proteinmentioning

confidence: 75%

“…Deduced amino acid sequences of the mouse subunits encoded by MT1a and mGSTT2 are compared with those of subunits rGSTT1 [11], rGSTT2 [12], hGSTT1 [6] and hGSTT2 [7] using the Bestfit program as described in the text. …”

Section: Table 1 Amino Acid Sequence Identity (%) Between Mammalian Tmentioning

confidence: 99%

“…The Theta class can be divided into two orthologous subfamilies in humans [2,[5][6][7][8], rats [2,[9][10][11][12][13] and mice [14][15][16][17]. Subfamily 1 isoenzymes (GSTT1-1) are typically active towards dichloromethane (DCM) and 1,2-epoxy-3-(pnitrophenoxy)propane (EPNP) while subfamily 2 isoenzymes (GSTT2-2) are active towards 1-menaphthyl sulphate (MS).…”

Section: Introductionmentioning

confidence: 99%

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Gene structure, expression and chromosomal localization of murine Theta class glutathione transferase mGSTT1-1

Whittington

Vichai

Webb

et al. 1998

Biochemical Journal

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We have isolated and characterized a cDNA and partial gene encoding a murine subfamily 1 Theta class glutathione transferase (GST). The cDNA derived from mouse GSTT1 has an open reading frame of 720 bp encoding a peptide of 240 amino acids with a calculated molecular mass of 27356 Da. The encoded protein shares only 51% deduced amino acid sequence identity with mouse GSTT2, but greater than 80% deduced amino acid sequence identity with rat GSTT1 and human GSTT1. Mouse GSTT1-1 was expressed in Escherichia colias an N-terminal 6× histidine-tagged protein and purified using immobilized-metal affinity chromatography on nickel-agarose. The yield of the purified recombinant protein from E. coli cultures was approx. 14 mg/l. Recombinant mouse GSTT1-1 was catalytically active towards 1,2-epoxy-3-(p-nitrophenoxy)propane, 4-nitrobenzyl chloride and dichloromethane. Low activity towards 1-menaphthyl sulphate and 1-chloro-2,4-dinitrobenzene was detected, whereas mouse GSTT1-1 was inactive towards ethacrynic acid. Recombinant mouse GSTT1-1 exhibited glutathione peroxidase activity towards cumene hydroperoxide and t-butyl hydroperoxide, but was inactive towards a range of secondary lipid-peroxidation products, such as the trans-alk-2-enals and trans,trans-alka-2,4-dienals. Mouse GSTT1 mRNA is most abundant in mouse liver and kidney, with some expression in intestinal mucosa. Mouse GSTT1 mRNA is induced in liver by phenobarbital, but not by butylated hydroxyanisole, β-napthoflavone or isosafrole. The structure of mouse GSTT1 is conserved with that of the subfamily 2 Theta class GST genes mouse GSTT2 and rat GSTT2, comprising five exons interrupted by four introns. The mouse GSTT1 gene was found, by in situ hybridization, to be clustered with mouse GSTT2 on chromosome 10 at bands B5–C1. This region is syntenic with the location of the human Theta class GSTs clustered on chromosome 22q11.2. Similarity searches of a mouse-expressed sequence tag database suggest that there may be two additional members of the Theta class that share 70% and 88% protein sequence identity with mouse GSTT1, but less than 55% sequence identity with mouse GSTT2.

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Section: Properties Of the Encoded Proteinmentioning

confidence: 75%

Section: Table 1 Amino Acid Sequence Identity (%) Between Mammalian Tmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Gene structure, expression and chromosomal localization of murine Theta class glutathione transferase mGSTT1-1

Whittington

Vichai

Webb

et al. 1998

Biochemical Journal

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“…In Fig. 2 the amino acid sequence of P. mirabilis GST is compared with the corresponding sequences of yeast (Zssa-tchenkia orientalis) 161, plant (maize transferase I) [7], and insect (Muscu domestica) [9] GST, as well as with those of four mammalian enzymes taken as representative of the Alpha (rat subunit la) [17], Mu (rat subunit 3a) [18], Pi (pig) [19] and Theta (rat) [20] classes. A number of gaps have been inserted into the sequences to optimize the alignment.…”

Section: Resultsmentioning

confidence: 99%

The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes

Mignogna¹,

Allocati

Aceto

et al. 1993

European Journal of Biochemistry

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The complete amino acid sequence of glutathione transferase from Proteus mirabilis was determined. The sequence was reconstructed by analysis of peptides obtained after cleavage by trypsin, Glu-C and Asp-N endoproteinases. The enzyme subunit is composed of 203 amino acid residues corresponding to a molecular mass of 22856 Da. Comparison of this sequence with other known primary structures of the corresponding enzyme from different sources shows a low level of identity (17-26%) with only seven conserved residues in all the sequences considered. This novel glutathione transferase could represent the prototype of a new class, possibly including other bacterial enzymes.The cytosolic glutathione S-transferases (GST) constitute a family of multifunctional dimeric proteins that catalyse the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST are also involved in intracellular binding and transport of hydrophobic molecules, including heme, bile acids, bilirubin and polycyclic hydrocarbons, participate in the synthesis of prostaglandins and leukotrienes, and may play a key role in the elimination of toxic organic hydroperoxides [l -41. The structure and function of mammalian cytosolic GST have been the subject of numerous investigations and the various forms so far characterized from different tissues of the same organism or from different organisms can be grouped into at least four distinct classes, Alpha, Mu, Pi and Theta [5]. The complete primary structures for many members of these classes are available, mostly deduced by analysis of cDNA. GST isoenzymes belonging to the same class show 70-80% identity in their primary structure, whereas GST belonging to different classes have less than 30 % sequence identity [2]. The amino acid sequences deduced from the cDNA of yeast [6], plant [7] and insect [8, 91 GST have also been determined. Recently, the three-dimensional structure of the Piclass GST from pig lung has been determined [lo] and the geometry of glutathione site (G site) has also been elucidated.

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“…Ch 7-oxy radical Smith, 1981;van Lier, 1988 Ch 7-OOHs Wendel, 1980;Flohe, 1982;Ursini et al, 1991;Rapoport and Müller 1974;Bao et al, 1997 GSH S-transferase GST Ketterer et al, 1986, Ketterer andMeyer, 1989 Alpha A Mu M Pi P Hayes and Pulford 1995 Theta T Hiratsuka et al, 1990;Meyer et al, 1991;Ogura et al, 1991 Table 2 Clone 9 HNE GSH S 1/50 Table 3 GST Clone 9 rGSTA4 -4 HNE GSH…”

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confidence: 99%

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Hiratsuka¹

2004

Environ. Mutagen Res.

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SummaryLevels of cholesterol 7α-and 7β -hydroperoxides Ch 7-OOHs in the skin of rats were investigated under different conditions in vivo such as aging or UVB -irradiation, and the results suggest that Ch 7-OOHs are good markers for lipid peroxidation. In the rat of any age, liver had no detectable level of Ch 7-OOHs. The Ch 7-OOHs were glutathione GSH -dependently reduced to the corresponding alcohols by GSH peroxidase GSH Px and only by the Alpha -class GSH S -transferases GSTs A1-1 and A1-3 among all isoforms of the GSTs occurring in the liver. On the other hand, rat skin had a very low level of GSH Px compared with the liver and lacked the subunit A1-bearing GSTs. Therefore, the absence or the presence of low levels of the enzyme systems which scavenge the cholesterol hydroperoxides in the skin of rats appears to be one of the main reasons for 1 the presence of Ch 7-OOHs in the skin of rats, 2 the increase in the levels of Ch 7-OOHs with age of rats or by UVB -irradiation to rats.Enzyme, Western blot, and immunohistochemical analyses indicated that rat skin cytosol contained no detectable level of the Alpha -class GSTA4 -4 which catalyzes the GSH conjugation of the toxic product, 4-hydroxy-2 E -nonenal HNE , nonenzymatically formed from n-6 polyunsaturated fatty acid residues of lipids by lipid peroxidation. Rats irradiated with single doses 4,000 -24,000 mJ/cm 2 of UVB markedly expressed rGSTA4 -4 in the skin at a level one-fifth that of the liver; at a single dose of 24,000 mJ/cm 2 , there was apparent specific activity toward HNE. The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase was irreversibly and S -selectively inactivated by the enantiomers of racemic HNE. Also, S -HNE was a much more potent agent than R -HNE for cell growth inhibition and induction of apoptosis. In rat liver cytosol, the HNE was detoxified 2.5-fold more S -selectively by GSH conjugation. The minor GST isoforms, A4 -4, had a major role in the cytosolic S -selective GSH conjugation in the rat liver.

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Molecular cloning and amino acid sequencing of rat liver class theta glutathione S-transferase Yrs-Yrs inactivating reactive sulfate esters of carcinogenic arylmethanols

Cited by 53 publications

References 25 publications

Gene structure, expression and chromosomal localization of murine Theta class glutathione transferase mGSTT1-1

Gene structure, expression and chromosomal localization of murine Theta class glutathione transferase mGSTT1-1

The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes

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