Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione <i>S</i>-transferase B

Hayes, John D.; Strange, Richard C.; Percy‐Robb, I. W.

doi:10.1042/bj1810699

Cited by 99 publications

(60 citation statements)

References 25 publications

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“…All three families of GSH S-transferase (a, (i, 7c) have been found to be inducible in liver and certain other tissues [8][9][10][11][12][13][14][15][16], We tested four of these classical inducers, at the limits of their solubility, for their ability to induce GSH S-transferase activity in cultured human kératinocytes. The inducers tested were: phé nobarbital, propylthiouracil, TSO and BHA.…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, we have treated cells with butylated hydroxyanisole (BHA), phénobarbital, propylthiouracil, and transstilbenc oxide (TSO). In studies of liver, phé nobarbital has been reported to induce a [8][9][10][11][12] , g [8][9][10][11][12] and t c [ 12] forms: TSO, the a [9,13] and g [13] forms; propylthiouracil the aform [14], and BHA the g-form [15,16]. We have also tested the effect of these inducers on the activity of GSH peroxidase and GSH reductase.…”

Section: Introductionmentioning

confidence: 99%

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Effect of Inducers on the Activity of Glutathione S-Transferase and Other Enzymes of the Glutathione Pathway in Cultured Human Keratinocytes

Vessey

Lee

Blacker

et al. 1993

Skin Pharmacol Physiol

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Known inducers of the hepatic glutathione (GSH) S-transferases were tested at the limits of their solubility as inducers of the enzyme in cultured human keratinocytes. Neither phenobarbital, trans-stilbene oxide, propylthiouracil, nor butylated hydroxyanisole increased GSH S-transferase activity or led to the appearance of α- or μ-forms of the enzyme, as judged by Western blotting. Only the π-form of the enzyme was found before and after all treatments. Thus, the enzyme is not indu-cible in keratinocytes. However, 4 mM propylthiouracil did lead to a 50% increase in GSH reductase activity, and phenobarbital at 4 mM completely abolished GSH peroxidase and GSH reductase activity and led to a significant loss of viability.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effect of Inducers on the Activity of Glutathione S-Transferase and Other Enzymes of the Glutathione Pathway in Cultured Human Keratinocytes

Vessey

Lee

Blacker

et al. 1993

Skin Pharmacol Physiol

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“…GSH transferases A, C, D and E are all Yb homodimers, GSH transferase AA is a Y, homodimer [ll] while GSH transferase B has been separated into two forms, one of which is a Y, homodimer and the other a Yay, heterodimer [12,13]. The high-affinity binding site is associated with the Y, monomer [14,15] while GSH peroxidase activity is associated with both Y, and Y, monomers [ll].…”

mentioning

confidence: 99%

Evidence that the Y_a and Y_c Subunits of Glutathione Transferase B (Ligandin) are the Products of Separate Genes

Beale

Ketterer

Carne

et al. 1982

European Journal of Biochemistry

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A study of the structure of glutathione transferase B (ligandin) has been made with a view to understanding the relationship between the structures of the subunits of which it is composed. It consists of a mixture of a homodimer (Ya Ya) and a heterodimer (Ya Yc) in which the monomers are denned by their apparent molecular weights, that of Ya being 22000 and Yc 25000. Soluble tryptic peptides from the native homodimer Ya Ya have been compared with those from an artificial homodimer Yc Yc produced by rehybridization of native Ya Yc. Approximately 10 peptides specific to Ya Ya, 12 specific to Yc Yc and 21 common to both have been detected. Some of the above peptides are derived from variants of the monomers themselves. Ya Ya and Yc Yc have two C termini which are the same in both dimers, namely phenylalanine and lysine. Also there are four cysteinyl peptides, of which three are common to Ya Ya and Yc Yc and one specific to each. These results suggest that Ya and Yc are derived from at least two different but related genes.

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“…GSTs were separated by ion-exchange chromatography (Hayes et al, 1979). Cytosols were prepared as described using sucrose-phosphate buffer.…”

Section: Separation Ofglutathione S-transferases (Gsts) In Hepatic Cymentioning

confidence: 99%

Dibromosulphophthalein: its pharmacokinetics and binding to hepatic cytosol proteins in rats with acute renal failure

Silberstein

Bowmer²,

Yates³

1988

British J Pharmacology

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1 The pharmacokinetics, biliary excretion and binding of dibromosulphophthalein (DBSP) to plasma proteins and hepatic cytosol proteins have been studied in male rats with glycerol-induced acute renal failure (ARF). 2 The rate constants for hepatic uptake, efflux from liver to plasma and excretion into bile were all significantly decreased in rats with ARF. Furthermore, the plasma clearance of DBSP was also reduced. 3 The initial (0-10min) and maximum biliary excretion rates of DBSP were both diminished in animals with ARF. The maximum excretion rate occurred between 5-10min in control rats and 10-15 min in rats with ARF. However, there was no statistically significant change in the percentage dose recovered from bile after 30 min. 4 The plasma-protein binding of DBSP was decreased in rats with ARF and this change was due to a significant reduction in the association constant for the primary binding sites. 5 The binding of DBSP to ligandin (Y protein) was reduced by about 38% in rats with ARF but no change was noted in binding to Z protein. Reduced binding to ligandin was accompanied by decreased total liver glutathione S-transferase (GST) activity and a 36% reduction in the GST activity of ligandin. 6 The results support the contention that altered hepatic handling of cholephilic dyes in rats with ARF may be due to reduced binding to ligandin.

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Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S-transferase B

Cited by 99 publications

References 25 publications

Effect of Inducers on the Activity of Glutathione S-Transferase and Other Enzymes of the Glutathione Pathway in Cultured Human Keratinocytes

Effect of Inducers on the Activity of Glutathione S-Transferase and Other Enzymes of the Glutathione Pathway in Cultured Human Keratinocytes

Evidence that the Y_a and Y_c Subunits of Glutathione Transferase B (Ligandin) are the Products of Separate Genes

Dibromosulphophthalein: its pharmacokinetics and binding to hepatic cytosol proteins in rats with acute renal failure

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Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S-transferase B

Cited by 99 publications

References 25 publications

Effect of Inducers on the Activity of Glutathione S-Transferase and Other Enzymes of the Glutathione Pathway in Cultured Human Keratinocytes

Effect of Inducers on the Activity of Glutathione S-Transferase and Other Enzymes of the Glutathione Pathway in Cultured Human Keratinocytes

Evidence that the Ya and Yc Subunits of Glutathione Transferase B (Ligandin) are the Products of Separate Genes

Dibromosulphophthalein: its pharmacokinetics and binding to hepatic cytosol proteins in rats with acute renal failure

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Evidence that the Y_a and Y_c Subunits of Glutathione Transferase B (Ligandin) are the Products of Separate Genes