Studies on the glutathione <i>S</i>-transferase activity associated with rat liver mitochondria

Ryle, C M; Mantle, Timothy J.

doi:10.1042/bj2220553

Cited by 13 publications

(6 citation statements)

References 19 publications

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“…A minor form of glutathione S-transferase has been reported to be bound to mitochondrial outer membranes [37] and to have a molecular mass of 17 kDa, remarkably similar to the subunit of the acceptor which can be photolabelled. However, there is considerably more of this glutathione S-transferase isoenzyme associated with liver microsomal membranes [38] than with mitochondria, and as this is not the case for the peripheral benzodiazepine acceptor, then their being identical seems unlikely.…”

Section: Discussionmentioning

confidence: 99%

Two subcellular locations for peripheral‐type benzodiazepine acceptors in rat liver

O'beirne

Woods

Williams

1990

European Journal of Biochemistry

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Subcellular fractionation of rat liver by differential centrifugation showed the mitochondrial fractions to have the greatest enrichment of ‘peripheral‐type’ benzodiazepine acceptor. Two peaks of acceptor sites were found on isopycnic density‐gradient centrifugation, one peak (ϱ= 1.19 g/ml) corresponding to the peak of mitochondria as judged by marker enzyme distribution and by transmission electron microscopy, and the other peak (ϱ= 1.17 g/ml) which is not mitochondrial as judged by the lack of mitochondrial enzyme markers. Whereas the density of the mitochondrial acceptor was sensitive to sonication and was shown to have an outer‐membrane location, the density of the non‐mitochondrial acceptor was insensitive to sonication. The non‐mitochondrial acceptor was shown not to be associated with Golgi, lysosomes, rough endoplasmic reticular microsomes, peroxisomes, or some type of plasma membranes, as jugged by differences in the distribution of marker activities. No enrichment of benzodiazepine acceptor was found in the purified nuclear fraction. Both acceptors were shown to be peripheral‐type high‐affinity acceptors as judged by ligand specificities and by photoaffinity labelling.

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Section: Discussionmentioning

confidence: 99%

Two subcellular locations for peripheral‐type benzodiazepine acceptors in rat liver

O'beirne

Woods

Williams

1990

European Journal of Biochemistry

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“…GST activity has been observed in mitochondrial preparations (Wahllander et al, 1979;Jocelyn & Cronshaw, 1985;Botti et al, 1989) and the purification and partial characterization of three mitochondrial GSTs has been reported by Kraus (1980). However, Ryle & Mantle (1984) have suggested that these activities may be the result of cytoplasmic contamination. GST activity in the mitochondria, like that of the cytoplasm, might be present to protect against genotoxic and cytotoxic electrophiles.…”

Section: Introductionmentioning

confidence: 99%

A novel glutathione transferase (13–13) isolated from the matrix of rat liver mitochondria having structural similarity to class theta enzymes

Harris

Meyer

Coles

et al. 1991

Biochemical Journal

109

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A rat liver mitochondrial-matrix fraction was prepared and shown to have 1-chloro-2,4-dinitrobenzene(CDNB)-metabolizing glutathione transferase (GST) activity. Further fractionation by sequential gel filtration, isoelectric focusing or chromatofocusing and hydroxyapatite chromatography yielded three GSTs of pI 9.3, 8.9 and 7.5, none of which bound to a GSH-agarose affinity matrix. Most of the activity was associated with the pI-9.3 form, which was selected for further study. Its activity was tested with the following potential substrates in addition to CDNB: 1,2-dichloro-4-nitrobenzene, p-nitrobenzyl chloride, trans-4-phenylbut-3-en-2-one, 1,2-epoxy-3-(p-nitrophenoxy)propane, ethacrynic acid, menaphthyl sulphate, cumene hydroperoxide, linoleic acid hydroperoxide and 4-hydroxynon-2-enal. Appreciable activity was obtained only with CDNB and ethacrynic acid (82 and 26 mumol/min per mg of protein respectively). The apparent Km for GSH, using 1 mM-CDNB, was 1.9 mM. The enzyme is a dimer of subunit Mr 26,500. It has a free N-terminus, which has enabled the first 33 amino acids to be sequenced. This portion of primary structure has a sequence in common with members of the Theta class of GSTs (eg. 36% identity with subunit 12) and also a sequence which might function as a mitochondrial import signal. It is novel and has been named 'GST 13-13'.

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“…When we applied the long development step employed by Lungu et al to ganglion sections stained with preimmune rabbit IgG, NBT-BCIP was deposited in pigment granules (data not shown). Antibodies derived from GST fusion constructs can exhibit cross-reactivity with endogenous GSTs; anti-GST reactivity may be especially problematic in aging neurons where mitochondrial GSTs are less efficiently degraded and where oxidatively modified GSTs may accumulate in response to certain neurological diseases associated with aging (5,12,37,38,(40)(41)(42).…”

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confidence: 99%

Expression of Varicella-Zoster Virus Immediate-Early Regulatory Protein IE63 in Neurons of Latently Infected Human Sensory Ganglia

Zerboni

Sobel

Ramachandran

et al. 2010

J Virol

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Varicella-zoster virus (VZV) causes varicella and establishes latency in sensory nerve ganglia, but the characteristics of VZV latency are not well defined. Immunohistochemical detection of the VZV immediateearly 63 (IE63) protein in ganglion neurons has been described, but there are significant discrepancies in estimates of the frequency of IE63-positive neurons, varying from a rare event to abundant expression. We examined IE63 expression in cadaver ganglia using a high-potency rabbit anti-IE63 antibody and corresponding preimmune serum. Using standard immunohistochemical techniques, we evaluated 10 ganglia that contained VZV DNA from seven individuals. These experiments showed that neuronal pigments were a confounding variable; however, by examining sections coded to prevent investigator bias and applying statistical analysis, we determined that IE63 protein, if present, is in a very small proportion of neurons (<2.8%). To refine estimates of IE63 protein abundance, we modified our protocol by incorporating a biological stain to exclude the pigment signal and evaluated 27 ganglia from 18 individuals. We identified IE63 protein in neurons within only one ganglion, in which VZV glycoprotein E and an immune cell infiltrate were also demonstrated. Antigen preservation was shown by detection of neuronal synaptophysin. These data provide evidence that the expression of IE63 protein, which has been referred to as a latency-associated protein, is rare. Refining estimates of VZV protein expression in neurons is important for developing a hypothesis about the mechanisms by which VZV latency may be maintained.Varicella-zoster virus (VZV), the human alphaherpesvirus that causes varicella during primary infection, establishes a lifelong latency in neurons of the sensory ganglia along the cerebrospinal axis (7). Sensory ganglia are composed of heterogeneous populations of neurons surrounded by satellite cells and other nonneuronal cells; axons extend from these neurons to innervate the skin and mucous membranes (50). Herpes zoster (shingles) results from reactivation of latent virus within ganglion cells and transfer of newly synthesized infectious particles to the skin via axonal transport (7).The number and type of neural cells that harbor latent virus are fundamental to the question of VZV latency. Studies to address this question have used methods to detect viral DNA, RNA, and proteins in cadaver ganglia. Although RNA is especially vulnerable to RNA-degrading enzymes during the postmortem interval between death and fixation of histological specimens at autopsy, DNA and proteins are reasonably stable (16). Nevertheless, reports using either VZV DNA or protein detection to assess the numbers of cells that contain VZV in human cadaver ganglia have yielded estimates that are extremely variable. By in situ hybridization and PCR methods, VZV DNA has been reported in as few as 1.5% of neurons exclusively (none in satellite cells) to as many as 30% of ganglion cells (neurons as well as satellite cells) (24, 26). Most recently,...

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Studies on the glutathione S-transferase activity associated with rat liver mitochondria

Cited by 13 publications

References 19 publications

Two subcellular locations for peripheral‐type benzodiazepine acceptors in rat liver

Two subcellular locations for peripheral‐type benzodiazepine acceptors in rat liver

A novel glutathione transferase (13–13) isolated from the matrix of rat liver mitochondria having structural similarity to class theta enzymes

Expression of Varicella-Zoster Virus Immediate-Early Regulatory Protein IE63 in Neurons of Latently Infected Human Sensory Ganglia

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