Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.6.1 (sulfatase)
3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arylsulfatase C (aryl-sulfate sulfohydrolase, EC 3.1.6.1) from sheep brain acetone powder was solubilized with the chaotropic agent, KSCN. Anti-chaotropes such as (NH4)2SO4 or sodium citrate significantly enhanced the activity of the solubilized enzyme indicating that hydrophobicity was an important factor influencing the enzyme activity. Dialysis or gel filtration of the solubilized enzyme resulted in a marked loss of activity. 3a dialyzable activator could reconstitute the activity in the presence of the antichaotropes. The activator was purified partially and preliminary studies indicated it to be a low molecular weight peptide. Arylsulfatase C and estrone sulfatase activities were compared in the solubilized enzyme. Estrone sulfatase activity was also increased in the presence of antichaotropes at lower concentration in comparison to arylsulfatase C. It however did not show a requirement for the dialyzable activator. Kinetic studies showed that elevation of enzyme activity by the antichaotropes and activator in the case of arylsulfatase C and by antichaotropes in the case of estrone sulfatase was due to an increase in V with a decrease in Km.
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PMID:Studies on the chaotropically solubilized arylsulfatase C and estrone sulfatase of sheep brain. 45 22

Estrone sulfatase is an important mechanism of local synthesis of biologically active estrogens in human breast cancer. The human placental microsome and breast carcinoma mitochondrial/microsomal estrone sulfatase activity were characterized and inhibition studies performed. The Km of the placental tissue enzyme was 6.83 microM, Vmax 0.015 nmol/min/mg, and for the breast carcinoma tissue Km was 8.91 microM and Vmax 0.022 nmol/min/mg. Danazol produced a significant inhibition of estrone sulfatase (20% with 50 microM danazol). No significant inhibition was seen in the presence of aminoglutethimide, rogletimide, tamoxifen, 4-hydroxyandrostenedione, stilboestrol, or any metabolites of danazol or tamoxifen. Studies with synthetic and naturally occurring steroids demonstrated that the presence of a sulfate group at the 3 position to be the most important factor in determining inhibition, and the most potent inhibitor was 5 alpha-androstene-3 beta,17 beta-diol-3-sulfate (Ki of 2.0 microM). The naturally occurring 3-sulfated steroids all demonstrated competitive inhibition. These studies could form the basis for the design of a potent estrone sulfatase inhibitor which would have potential therapeutic activity in the management of breast cancer.
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PMID:Inhibition of estrone sulfatase enzyme in human placenta and human breast carcinoma. 191 38

The growth of uterine leiomyoma is regulated not only by the estrogen levels in blood, but also by estrogen production in the tumor itself. In this study, we investigated both the estrone formation (estrone sulfatase activity) and the transformation from estrone to estrone sulfate (estrone sulfotransferase activity) in human leiomyoma tissue. We compared them with those in the myometrium and endometrial tissues overlying and opposite a uterine leiomyoma node. We also measured the tissue concentrations of estrone, estradiol and estrone sulfate. Estrone sulfatase activity in the uterine leiomyoma was 0.49 +/- 0.08 nmol/h/mg protein (Mean +/- SE), and was lower than that in the myometrial tissue (0.76 +/- 0.09). Moreover, the enzyme activity was higher in the endometrium overlying the leiomyoma node (2.62 +/- 0.29) than in the endometrium opposite to it (2.10 +/- 0.24). On the other hand, estrone sulfotransferase activity in the myoma (20.2 +/- 2.4 pmol/h/mg protein) was higher than in myometrial tissue (16.7 +/- 2.3). The concentrations of estrone and estradiol in leiomyoma tissue were lower than in the tissues surrounding the leiomyoma. The tissue concentration of estrone sulfate was higher in leiomyoma tissues. These results suggest that estrone sulfate is hydrolyzed mainly by estrone sulfatase in the endometrium and myometrium surrounding leiomyoma nodes and the estrone formed may affect the growth of leiomyoma.
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PMID:[Study on the local estrogen biosynthesis in human uterine leiomyoma]. 221 23

Estrone sulfatase activity was measured in normal and neoplastic endometrial tissues of human uterus. The tissue homogenates were incubated in air with [3H] estrone sulfate (E1-S, 20 microM) at 37 degrees C for 30 min. After the enzyme reaction was terminated with ethyl ether, the ethyl ether extract was purified by thin-layer chromatography. The apparent Km of sulfatase was 3.0 microM, and the maximum velocity was 14.7 nmol/h/mg protein. Estrone sulfatase activity in endometrial tissues was detected throughout the menstrual cycle with no significant change. Moreover, estrone sulfatase activity in endometrial cells was not stimulated by the addition of progestogen. The enzyme activity in cancer tissue was significantly higher than in normal tissue. Thus we concluded that this enzyme may play a role in regulating the estrogen action by sifting the intracellular equilibrium between free estrogens and estrogen sulfates. We also concluded that in the endometrial cancer tissue, sulfatase appears to act on local production of estrone.
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PMID:Estrone sulfatase activity in normal and neoplastic endometrial tissues of human uterus. 252 75

Estrone sulfate (E1-S) in the serum and tissues of patients with breast cancer or endometrial cancer was measured by a direct radioimmunoassay without hydrolysis. The concentration of E1-S in breast cancer tissue was 1.64 +/- 0.28 ng/g wet wt (+/- SE), lower than in surrounding normal breast tissue (4.46 +/- 1.23). Estradiol-17 beta(E2)/E1-S was higher in endometrial cancer tissue than normal endometrial tissue. Estrone sulfatase activity in breast cancer tissue was 0.81 +/- 0.23 nmol/h/mg protein, higher than in surrounding normal breast tissue (0.35 +/- 0.11). These results suggest that E1-S, which is abundant in the peripheral circulation, is hydrolyzed by sulfatase in breast cancer tissue or endometrial cancer tissue and liberates free estrogens, which may stimulate the growth of these malignant tumors.
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PMID:Estrone sulfate and sulfatase activity in human breast cancer and endometrial cancer. 255 48

Estrone sulfatase activity was characterized in microsomal preparations from rat brain and anterior pituitary. No differences in apparent Km were found in hypothalamic-preoptic area between male (7.5 microM) and female (7.4 microM) rats. Apparent Km's of anterior pituitaries from males (14.5 microM) and females (22.5 microM) were higher than those found in brain. Estrone sulfatase activity was equally inhibited by estradiol-17 beta-3-sulfate, dehydroepiandrosterone-3-sulfate and estrone-3-sulfate indicating a broad range of substrate specificity for this enzyme. Sulfatase activity in female anterior pituitary was found to be twice that of male. Sulfatase activity was distributed similarly in brain tissues between sexes with cerebellum greater than or equal to medial basal hypothalamus greater than preoptic area = cortex. Following gonadectomy, sulfatase activity in anterior pituitary of males was significantly greater than activity found in intact animals (P less than 0.05). This increase in activity, however, was unaffected by treatment with testosterone, dihydrotestosterone or estradiol-17 beta. Gonadectomy did not change sulfatase activity in brains of males or females or in pituitaries of females. However, sulfatase activity in pituitary glands of females changed significantly (P less than 0.05) with stages of the estrous cycle (metestrus less than diestrus less than proestrus less than estrus). These data indicate sulfatase activity in rat anterior pituitary gland may be controlled by gonadal factors while sulfatase activity in brain is regulated differently.
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PMID:Estrone sulfatase activity in rat brain and pituitary: effects of gonadectomy and the estrous cycle. 260 28

The activities of aromatase and estrone sulfatase which are important enzymes involved in the local production of estrogen in breast cancer tissue were measured to examine their availability in endocrine therapy and their clinical significance. The materials obtained were breast cancer tissue, noncancerous mammary gland and breast fat tissue from twenty eight patients with breast cancer, and mammary gland tissue from eight patients with benign breast disease. After centrifugation of homogenized tissue at 1000 X g, the supernatant of breast cancer tissue or mammary gland and the subnatant of breast fat tissue were used as enzyme sources. Aromatase activity was measured by 3H2O release assay using (1 beta-3H) androstenedione as the substrate, while estrone sulfatase activity was estimated from the conversion rate of (6,7-3H)estrone-3-sulfate to estrone. Aromatase activities were 25.1 +/- 12.4 (mean +/- S.D.) fmol/mg protein/h in twenty seven breast cancer tissue specimens, 11.0 +/- 6.1 fmol/mg protein/h in sixteen noncancerous mammary gland tissue specimens, 9.3 +/- 10.0 fmol/mg protein/h in twenty seven breast fat tissue specimens, and 7.7 +/- 5.5 fmol/mg protein/h in eight mammary gland tissue specimens from patients with benign breast disease. The aromatase activity in breast cancer tissue was significantly higher than that in noncancerous mammary gland, breast fat tissue and benign breast lesions (p less than 0.001). Estrone sulfatase activity was 4.0 +/- 3.5 nmol/mg protein/h in nineteen breast cancer tissue specimens, but was almost undetectable in eleven noncancerous mammary tissue specimens and eight benign breast lesions. These results suggest the relatively high local production of estrogen, mediated by aromatase or estrone sulfatase in breast cancer tissue.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Local production of estrogen via aromatase and estrone sulfatase in breast cancer tissue]. 279 62

Estrone sulfatase is a membrane-bound enzyme hydrolysing estrone sulfate. In normal and pathological tissues, estrone sulfatase is required for the conversion of estrone sulfate into physiologically active estrogens. In the hepatic cytosol of Guinea-pig, we have demonstrated the existence of a soluble inhibitor of uterine and hepatic microsomal estrone sulfatase. This inhibitor has approximatively a molecular weight of 7,600 and acts as a non-competitive inhibitor of estrone sulfatase. It seems to be a soluble intra-cellular effector of membrane-bound estrone sulfatase.
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PMID:[Demonstration of a cytosolic inhibitory of membrane estrone sulfatase activity in guinea pig liver]. 308 74

Estrone (E1)-sulfatase and dehydroepiandrosterone (DHEA)-sulfatase activities were studied in human female epidermis. Skin specimens were obtained by abdominal or plantar biopsies. The apparent Michaelis-Menten constants for E1 and DHEA sulfatases were 35.2 microM and 8.7 microM, respectively. A substrate inhibition was only observed for DHEA sulfatase. Both sulfatases had an elevated temperature optimum (65 degrees C). The effect of inorganic salts was also tested. In normal epidermis, E1-sulfatase activity was constantly higher than DHEA-sulfatase activity, but no correlation between these activities was observed. On the other hand, E1- and DHEA-sulfatase activities were lower in plantar than in abdominal epidermis. In plantar epidermis of palmoplantar keratoderma, large variations in E1-sulfatase activity, but no significant variation in DHEA-sulfatase activity, were observed. In human epidermis, the findings were consistent with the existence of two different sulfatases: E1 sulfatase and DHEA sulfatase. It would also appear that sulfatase activities are not linked to the abnormal shedding of plantar stratum corneum in palmoplantar keratoderma.
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PMID:Estrone- and dehydroepiandrosterone-sulfatase activities in human female epidermis. 316 Mar 10

Estrone and estradiol-17 beta concentration in breast cancer tissue are reported to be an order of magnitude higher than those of circulating plasma in breast cancer patients. This high level of estrogen is provided by local production from estrone sulfate (E1-S) through the sulfatase pathway. Then serum E1-S level was determined using direct radioimmunoassay method in order to monitor the estrogen kinetics of post-operative breast cancer patients. Peri-operative sequential E1-S determination was carried out in 10 patients. Among them, extremely higher level, as compared with normal menstruating level of 625-2670pg/ml, was observed just after an administration of tamoxifen (three weeks after operation) in two of 5 pre-menopausal patients. In order to evaluate the effect of tamoxifen on serum level of E1-S in post-operative pre-menopausal patients, serum E1-S level in 42 post-operative outpatients was examined. Although there was no difference in the average level of E1-S in post-menopausal patients treated with or without tamoxifen, average E1-S level in pre-menopausal patients treated with tamoxifen as adjuvant therapy was significantly higher than that in patients without tamoxifen. These results suggests that the administration of tamoxifen to premenopausal patients should be reconsidered from a view point of the estrogen kinetics.
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PMID:[Serum estrone sulfate levels in patients with breast cancer]. 318 94


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