Estrone and dehydroepiandrosterone sulfatase activities in guinea-pig uterus and liver: Estrogenic effect of estrone sulfate

Moutaouakkil, M; Prost, O.; Dahan, Nicole; Adessi, G. L.

doi:10.1016/0022-4731(84)90286-3

Cited by 24 publications

(10 citation statements)

References 25 publications

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“…Lam and Polani (57) used exogenous testosterone treatment and concluded that STS induction is, in part, controlled by the male hormones in the mouse. Moutaouakkil et al (58) observed that STS was highest in the uteri of pregnant guinea pigs compared with that in the uteri of fetal, castrated, or mature females, suggesting estrogenic regulation. The possibility of substrate induction of in vivo STS activity in liver and white blood cells in ovariectomized rats was confirmed by administration of exogenous E1S to ovariectomized rats (59).…”

Section: B Steroidsmentioning

confidence: 96%

Steroid Sulfatase: Molecular Biology, Regulation, and Inhibition

et al. 2005

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Steroid sulfatase (STS) is responsible for the hydrolysis of aryl and alkyl steroid sulfates and therefore has a pivotal role in regulating the formation of biologically active steroids. The enzyme is widely distributed throughout the body, and its action is implicated in physiological processes and pathological conditions. The crystal structure of the enzyme has been resolved, but relatively little is known about what regulates its expression or activity. Research into the control and inhibition of this enzyme has been stimulated by its important role in supporting the growth of hormone-dependent tumors of the breast and prostate. STS is responsible for the hydrolysis of estrone sulfate and dehydroepiandrosterone sulfate to estrone and dehydroepiandrosterone, respectively, both of which can be converted to steroids with estrogenic properties (i.e., estradiol and androstenediol) that can stimulate tumor growth. STS expression is increased in breast tumors and has prognostic significance. The role of STS in supporting tumor growth prompted the development of potent STS inhibitors. Several steroidal and nonsteroidal STS inhibitors are now available, with the irreversible type of inhibitor having a phenol sulfamate ester as its active pharmacophore. One such inhibitor, 667 COUMATE, has now entered a phase I trial in postmenopausal women with breast cancer. The skin is also an important site of STS activity, and deficiency of this enzyme is associated with X-linked ichthyosis. STS may also be involved in regulating part of the immune response and some aspects of cognitive function. The development of potent STS inhibitors will allow investigation of the role of this enzyme in physiological and pathological processes.

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Section: B Steroidsmentioning

confidence: 96%

Steroid Sulfatase: Molecular Biology, Regulation, and Inhibition

et al. 2005

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“…Moreover, the oestrone sulphate assay demonstrates that a sulphotransferase activity is also present in cell culture, which converts oestrone into a sulphoconjugated derivative. The oestrone and DHEA sulphatase activi¬ ties previously characterized by Moutaouakkil et al (1984) in the uterus and liver of female guinea-pigs have been demonstrated and measured in the epithelial cell culture. The three enzymes interfering with oestrogen metabolism are present in our epithelial cell culture and their patterns in epithelial cells cultured in vitro resembled that of fresh endometrium.…”

Section: Morphological Resultsmentioning

confidence: 91%

“…Laure & Pasqualini (1983) have demonstrated that oestradiol-17ß increased the RNA polymerase in fetal uterus. Moutaouakkil, Prost, Dahan & Adessi (1984) have studied sulphatase activities in the uterus, and a metabolic pathway of oestrogens in pregnant female guinea-pigs has been proposed (Adessi, Tran Quang Nhuan & Prost, 1981;Adessi, Tran Quang Nhuan & Vingler, 1982).…”

Section: Introductionmentioning

confidence: 99%

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Culture of epithelial and stromal cells of guinea-pig endometrium and the effect of oestradiol-17 on the epithelial cells

Chaminadas¹,

Propper²,

Royez³

et al. 1986

Reproduction

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“…appears to function as a steroid sulfatase (STS; sterylsulfate sulfohydrolase EC 3.1.6.2) [3]; however, arylsulfatase (estrone sulfate; E1S) and alkylsulfatase (déhydroépiandros térone sulfate; DHEAS) activities may reside in separate proteins [4], or their hydrolysis may require the action of two or more sites within the same enzyme [5] from certain spe cies.…”

Section: Introductionmentioning

confidence: 99%

Comparison of Arylsulfatase C and Steroid Sulfatase from Human Placenta and Liver

Daniel

Chang²

1990

Enzyme

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Human placental and hepatic arylsulfatase C (ASC) were purified to homogeneity and about 1,000-fold, respectively. Placental ASC hydrolyzed sterol sulfates at the same active site, whereas the major hepatic ASC did not. This major hepatic ASC isozyme was more thermolabile than placental ASC and steroid sulfatase from both placenta and liver. It was not precipitated by anti-bovine ASC IgG which quantitatively precipitated both placental ASC and steroid sulfatase activities from placenta and liver. A minor hepatic ASC isozyme with similar electrophoretic mobility to the placental enzyme copurified with the major hepatic ASC and is likely responsible for the steroid sulfatase activity in this organ. Hence, placental ASC and steroid sulfatase are biochemically and antigenically identical to hepatic steroid sulfatase. In contrast, the major hepatic ASC is a distinct protein whose catalytic and structural properties differ from all the above enzymes.

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Estrone and dehydroepiandrosterone sulfatase activities in guinea-pig uterus and liver: Estrogenic effect of estrone sulfate

Cited by 24 publications

References 25 publications

Steroid Sulfatase: Molecular Biology, Regulation, and Inhibition

Steroid Sulfatase: Molecular Biology, Regulation, and Inhibition

Culture of epithelial and stromal cells of guinea-pig endometrium and the effect of oestradiol-17 on the epithelial cells

Comparison of Arylsulfatase C and Steroid Sulfatase from Human Placenta and Liver

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