Studies of the oestrogen sulphatase and arylsulphatase C activities of rat liver

Dolly, J. Oliver; Dodgson, K. S.; Rose, F. A.

doi:10.1042/bj1280337

Cited by 64 publications

(27 citation statements)

References 34 publications

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“…Of the three arylsulphatase enzymes (A, B, and C), arylsulphatase C has been suggested to be identical with oestrone sulphatase (2,5). This type of en zyme activity has been reported to be present in different mammalian tissues, e.g., liver (2,5), placenta (12), kidney (8), brain (10), and pituitary (13).…”

Section: Resultsmentioning

confidence: 99%

“…Zuckerman and Hagerman (8) used for their assays debris-free homogenates in 0.2 M sodium phosphate buffer, pH 8.0, obtained by centrifugation at 600 g for 10 min. On the other hand, the study of Dolly et al (2) was carried out in a crude whole tissue homogenate pre pared in ice-cold water.…”

Section: Resultsmentioning

confidence: 99%

“…Since several tissues contain the enzymes necessary to transform this conjugate to the biologically active steroid, 170-oestradiol (2,3), there are reasons to be lieve that oestrone sulphate acts in the organism as a potential oestrogen which can be partly activated by hydrolysis and reduction, particularly in the liver, but possibly also in other tissues including the target organs (4). It was, therefore, decided to carry out a study of the oestrone sulphatase activity in rat uteri.…”

Section: Introductionmentioning

confidence: 99%

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Oestrone Sulphatase Activity of the Rat Uterus in Different Hormonal States

Utaaker¹,

Støa²

1980

Horm Res

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Oestrone sulphatase activity was determined in the 12,500 g supernatant of rat uterus homogenates. The conditions used were 0.5 mM oestrone sulphate and 30 min incubation at pH 8.0 and 37 °C. The enzyme activity in uteri from normal animals was found to be 5.1 ± 0.7 nmol (mg protein)^-1h-¹. In ovariectomized and hypophysectomized animals the values were significantly higher, whereas subcutaneous administration of 17β-oestradiol to such rats resulted in significantly decreased oestrone sulphatase activities. Progesterone increased the enzyme activity of intact rats. It is concluded that the uterine tissue of rats contains oestrone sulphatase which may be of biological importance and which is inhibited by oestrogen.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Oestrone Sulphatase Activity of the Rat Uterus in Different Hormonal States

Utaaker¹,

Støa²

1980

Horm Res

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“…Studies in vitro showed that both diethylstilboestrol monosulphate and diethylstilboestrol disulphate are desulphated by a rat liver microsomal enzyme, arylsulphatase C, which has been shown to be identical with oestrogen sulphatase (Dolly et al, 1972). Presumably desulphation of diethylstilboestrol disulphate occurs in the liver to yield the monosulphate derivative, which has a free hydroxyl group available for conjugation with glucuronic acid.…”

Section: Experiments With Diethylstilboestrolmono[35s]sulphatementioning

confidence: 99%

Metabolic fates of diethylstilboestrol sulphates in the rat

Barford¹,

Olavesen²,

Curtis³

et al. 1977

Biochemical Journal

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The metabolic fates and modes of excretion of diethylstilboestrol mono [35S] Diethylstilboestrol has been used as a synthetic oestrogen in humans and in food-producing animals. It has been shown to have carcinogenic properties in a number of animal species (Umberger, 1975) and its use has been associated with the occurrence of tumours in humans (Herbst et al., 1972).The metabolic fate of diethylstilboestrol has been studied in several animal species (Abou-EI-Makarem et al., 1967) and it has been shown that biliary excretion as a glucuronic acid conjugate represents a major pathway for elimination (Klaasen, 1973). The disulphate ester of diethylstilboestrol, which is approximately half as active as diethylstilboestrol itself with respect to oestrogenic activity (Bishop et al., 1951), has been used as a water-soluble form of the synthetic oestrogen. Nevertheless, the metabolism of sulphated forms of diethylstilboestrol has not been reported.

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“…The aim of this study was to determine intra-tumoural oestrone sulphatase activity in NMU-induced mammary tumours that regress with endocrine manipulation and in tumours which progress under oestrogenic stimulation. Previously, the rat and human oestrone sulphatase have been shown to be membrane-bound (Kawano et al, 1989;MacIndoe et al, 1988;Dolly et al, 1972) In both experiments the tumours and liver were harvested from all rats, immediately frozen in liquid nitrogen and stored at -70C. Tumour volumes were calculated using the formula in (d, x d2) i Tissue preparation All procedures were carried out at 0-4°C.…”

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confidence: 99%

Oestrone sulphatase activity in mammary tumours and the liver of N-nitrosomethylurea treated rats

Evans

Chander²,

Rowlands³

et al. 1992

Br J Cancer

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Summary Oestrone sulphatase may be an important means of production of intra-tumoural oestrogens in breast cancer cells. The N-nitrosomethylurea induced rat mammary tumours, which is a good model of human breast carcinoma, was utilised to examine the significance of intra-tumoural oestrone sulphatase levels. The particular fraction (100,000 g pellet) was prepared from both the liver and the tumour of NMU treated rats and assayed for sulphatase activity. (Segaloff, 1978;Kirschner, 1979). Plasma levels of oestrone and oestradiol in postmenopausal women are very low, however the oestrogen concentration in breast tumour tissues is an order of magnitude higher than in the plasma (Millington, 1975;Edery et al., 1981;Fishman et al., 1977;Thorsen et al., 1982;van Landeghem et al., 1985;Thijssen & Blankenstein, 1989), suggesting local intra-tumoural production of oestrogens in breast tumour cells from precursor substrates. A comparative study of intra-tumoural aromastase and oestrone sulphatase activities has demonstrated that the sulphatase appears to be at least ten times more active than the aromatase enzyme in the production of intra-tumoural oestrogens from their respective precursor substrates (Santner et al., 1984). Therefore the sulphatase pathway is likely to be an important means of local production of biologically active oestrogens in human breast carcinoma tissue.The N-nitrosomethylurea-induced mammary gland carcinoma in rat is a good model of human breast carcinoma (Gullino et al., 1975). It is a hormone dependent model that regresses on oophorectomy and responds to anti-endocrine agents (Williams et al., 1981;Wilkinson et al., 1986). When these mammary tumours are grown in soft agar, colony formation is stimulated by oestrone sulphate. This is accompanied by the conversion of oestrone sulphate to oestradiol (Santner et al., 1986). An in vivo study demonstrated that oestrone sulphate can stimulate the growth of NMU-induced mammary tumour in castrate animals (Santner et al., 1990). This tumour contains levels of oestrone sulphatase activity similar to human tumours (Santner et al., 1984). The The animals in the oestrogen-treated group were injected with oestradiol at a dose of 0. Ijg kg-' in 0.2 ml of 0.9% NaCl subcutaneously daily for 5 days every week of the experiment. The rats in the control groups were similarly injected with 0.2 ml of 0.9% NaCl on the same days. The experiment was terminated by sacrificing all animals after 4 weeks.

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Studies of the oestrogen sulphatase and arylsulphatase C activities of rat liver

Cited by 64 publications

References 34 publications

Oestrone Sulphatase Activity of the Rat Uterus in Different Hormonal States

Oestrone Sulphatase Activity of the Rat Uterus in Different Hormonal States

Metabolic fates of diethylstilboestrol sulphates in the rat

Oestrone sulphatase activity in mammary tumours and the liver of N-nitrosomethylurea treated rats

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