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PubMed2004

Steroid sulfatase and estrogen sulfotransferase in human endometrial carcinoma.

PURPOSE: Intratumoral metabolism and synthesis of estrogens are considered to play important roles in the pathogenesis and/or development of human endometrial carcinoma. Steroid sulfatase hydrolyzes biologically inactive estrogen sulfates to active estrogens, whereas estrogen sulfotransferase sulfonates estrogens to estrogen sulfates. However, the status of steroid sulfatase and/or estrogen sulfotransferase in human endometrial carcinoma has not been examined. EXPERIMENTAL DESIGN: We first examined the expression of steroid sulfatase and estrogen sulfotransferase in 6 normal endometrium and 76 endometrial carcinoma using immunohistochemistry to elucidate the possible involvement of steroid sulfatase and estrogen sulfotransferase. We then evaluated the enzymatic activity and the semiquantitative analysis of mRNA using reverse transcription-PCR in 21 endometrial carcinomas. We correlated these findings with various clinicopathological parameters including the expression of aromatase, 17beta-hydroxysteroid dehydrogenase type 1 and type 2. RESULTS: Steroid sulfatase and estrogen sulfotransferase immunoreactivity was detected in 65 of 76 (86%) and 22 of 76 (29%) cases, respectively. Results of immunoreactivity for steroid sulfatase and estrogen sulfotransferase were significantly correlated with those of enzymatic activity and semiquantitative analysis of mRNA. No significant correlations were detected among the expression of the enzymes involved in intratumoral estrogen metabolism. There was a significant correlation between steroid sulfatase/estrogen sulfotransferase ratio and clinical outcomes of the patients. However, there were no significant differences between steroid sulfatase or estrogen sulfotransferase and estrogen receptor, progesterone receptor, Ki67, histologic grade, or clinical outcomes of the patients. CONCLUSIONS: Results of our study demonstrated that increased steroid sulfatase and decreased estrogen sulfotransferase expression in human endometrial carcinomas may result in increased availability of biologically active estrogens and may be related to estrogen-dependent biological features of carcinoma.

17-Hydroxysteroid Dehydrogenases↗
PubMed1977

Steroid sulfatase deficiency.

Placental steroid sulfatase deficiency is a genetic disorder only recently reported in the medical literature. Most documented cases of placental sulfatase deficiency have been marked by delay in onset of labor, lack of cervical dilatation, and relative refractoriness of oxytocic agents and amniotomy. We have studied the placenta, cultured fibroblasts, and amniotic fluid cells from an affected patient. The activities of estrone sulfatase, pregnenolone sulfatase, dehydroepiandrosterone sulfatase, and arylsulfatase C in the placenta from the patient were severely deficient. Arylsulfatases A and B were present at levels within the normal range for this tissue. Fibroblast dehydroepiandrosterone sulfatase activity was virtually absent in the patient's cells and present at normal levels in individuals with a variety of lysosomal disorders. It would thus appear that the mutation responsible for steroid sulfatase deficiency is genetically and biochemically distinct from those involved in the lysosomal sulfatase deficiency states. The cell culture studies further suggest that the defect is a generalized one which should be detectable in midtrimester of pregnancy and may have phenotypic consequences in later postnatal life.

Estriol↗
PubMed1986

In vitro effects of human prolactin and oxytocin on sulfatase activity in isolated human decidual cells.

Homogeneous preparations of decidual cells were obtained from term decidual tissue adherent to fetal membranes by using a slightly modified version of a technique developed for the isolation of decidual cells from first and second trimester decidua. The effects of human PRL (hPRL) and oxytocin on the kinetics of the hydrolysis of estrone sulfate were determined in decidual cells prepared from tissue obtained before and after the onset of labor. In addition, sulfatase activity in decidual cells isolated from term decidua was compared with those of chorionic cells isolated from chorion leave of the same pregnancy. Chorionic cells had significantly higher (mean, 2.5-fold) levels of sulfatase activity than the corresponding decidual cells. The mean sulfatase activity in decidual cells obtained after normal vaginal delivery [25 +/- 19 (+/- SE) nmol/mg protein X 15 min) was higher than that in decidual cells obtained from patients undergoing cesarean section before the onset of labor (1.7 +/- 0.11). This difference was significant (P less than 0.02, by Mann-Whitney test) in spite of the large variation in activity in preparations from vaginal deliveries. hPRL (500 ng/ml) and oxytocin (0.2 microM) had similar effects on sulfatase activity in decidual cells in a manner dependent on whether the cells were isolated from tissue obtained before or after labor. In cells isolated from fetal membranes obtained before labor (cesarean delivery), hPRL or oxytocin significantly stimulated sulfatase activity, whereas in decidual cells obtained after vaginal delivery, both hPRL and oxytocin significantly inhibited sulfatase activity. The Michaelis constants for the hydrolysis of estrone sulfate (Km, 22 +/- 4.8 microM) were not affected by these hormones. Since the mean sulfatase activity of decidual cells obtained before labor was approximately 10-fold higher than the activity reported for endometrial stromal cells, PRL produced by decidual cells may act in vivo as an autocrine factor to stimulate their sulfatase activity.

Cell Separation↗
PubMed1992

[Biochemical study on steroid sulfatase and its clinical application to the obstetrics and gynecology].

Steroid sulfatase desulfates a number of 3 beta-hydroxysteroid sulfates, converting inactive steroid hormone to the active form. I have developed an enzyme-linked immunosorbent assay (ELISA) using polyclonal antibody against the sulfatase which was purified from human placenta to measure an amount of the enzyme protein in sera of gynecologic cancer patients. By this method, it was found that the serum steroid sulfatase level is significantly elevated in patients with endometrial carcinoma (p less than 0.05) and ovarian carcinoma (p less than 0.01) as compared to that of normal women. Steroid sulfatase deficiency, X-linked ichthyosis (XLI) is an inherited skin disorder. The sulfatase gene and the enzyme protein were examined in patients with XLI. When the first and last (exon 10) exons of the sulfatase gene were amplified by PCR using patients' genomic DNA as templates, no product was detected in all six cases examined. In addition, neither mRNA of the sulfatase nor the enzyme protein was detected in a patient with XLI. These observations suggest that most Japanese XLI patients are caused by an extensive deletion of the steroid sulfatase gene.

Arylsulfatases↗
PubMed1996

In vivo activity of 4-methylcoumarin-7-O-sulfamate, a nonsteroidal, nonestrogenic steroid sulfatase inhibitor.

Steroid sulfatase regulates the formation of estrone from estrone sulfate (E1S) and dehydroepiandrosterone (DHA) from DHA sulfate. DHA can be converted to androstenediol, a steroid with potent estrogenic properties, and inhibition of steroid sulfatase activity is therefore an important therapeutic target. Because nonsteroidal steroid sulfatase inhibitors may offer some advantage for use in the treatment of breast cancer, 4-methylcoumarin-7-O-sulfamate (COUMATE) was synthesized and shown to be active in vitro. In this study, in vitro and in vivo techniques have been used to confirm that COUMATE, in contrast to the steroidal steroid sulfatase inhibitor estrone-3-O-sulfamate, is devoid of estrogenic activity. COUMATE did not stimulate the growth of MCF-7 breast cancer cells or uteri of ovariectomized rats, in contrast to estrone-3-O-sulfamate. COUMATE was orally active in vivo and after multiple dosing (10 mg/kg/day for 7 days) inhibited liver estrone sulfatase activity by 85%. Seven days after single or multiple dosing with COUMATE, liver estrone sulfatase activity was almost fully restored. Measurement of estrone sulfatase activity in WBCs revealed a degree of inhibition similar to that detected in liver samples. COUMATE was able to completely block the ability of E1S to stimulate uterine growth in ovariectomized rats. The development of a potent nonsteroidal, nonestrogenic steroid sulfatase inhibitor should allow the therapeutic potential of this type of therapy to be evaluated.

Animals↗
PubMed1985

Synthesis and stability of arylsulfatase A and B in fibroblasts from multiple sulfatase deficiency.

Fibroblasts from patients with multiple sulfatase deficiency were analyzed for activities of arylsulfatase A and B, iduronate 2-sulfatase and sulfamatase. A group of patients (group I) severely deficient in all sulfatases (residual activities less than or equal to 10% of control) were differentiated from patients (group II) with residual sulfatase activities of up to 90% of control. The synthesis and stability of arylsulfatase A and B were determined in pulse-chase labelling experiments. The apparent rate of synthesis of arylsulfatase A and B varied from 30% to normal in both fibroblasts from group I and II multiple sulfatase deficiency. In group I the molecular activity of the arylsulfatase A and B was more than 10-fold lower than in control fibroblasts. In group II the molecular activity of the arylsulfatase A was twofold to threefold lower and that of arylsulfatase B half of normal. In fibroblasts of both groups the stability of arylsulfatase A polypeptides was significantly diminished. For arylsulfatase B the instability was restricted to the mature 47000-Mr polypeptide and was variable within both groups. These results demonstrate that multiple sulfatase deficiency is a heterogeneous disorder, in which the primary defects can impair both the catalytic properties and the stability of sulfatases.

Affinity Labels↗
PubMed2002

Characterization of iodothyronine sulfatase activities in human and rat liver and placenta.

In conditions associated with high serum iodothyronine sulfate concentrations, e.g. during fetal development, desulfation of these conjugates may be important in the regulation of thyroid hormone homeostasis. However, little is known about which sulfatases are involved in this process. Therefore, we investigated the hydrolysis of iodothyronine sulfates by homogenates of V79 cells expressing the human arylsulfatases A (ARSA), B (ARSB), or C (ARSC; steroid sulfatase), as well as tissue fractions of human and rat liver and placenta. We found that only the microsomal fraction from liver and placenta hydrolyzed iodothyronine sulfates. Among the recombinant enzymes only the endoplasmic reticulum-associated ARSC showed activity toward iodothyronine sulfates; the soluble lysosomal ARSA and ARSB were inactive. Recombinant ARSC as well as human placenta microsomes hydrolyzed iodothyronine sulfates with a substrate preference for 3,3'-diiodothyronine sulfate (3,3'-T(2)S) approximately T(3) sulfate (T(3)S) >> rT(3)S approximately T(4)S, whereas human and rat liver microsomes showed a preference for 3,3'-T(2)S > T(3)S >> rT(3)S approximately T(4)S. ARSC and the tissue microsomal sulfatases were all characterized by high apparent K(m) values (>50 microM) for 3,3'-T(2)S and T(3)S. Iodothyronine sulfatase activity determined using 3,3'-T(2)S as a substrate was much higher in human liver microsomes than in human placenta microsomes, although ARSC is expressed at higher levels in human placenta than in human liver. The ratio of estrone sulfate to T(2)S hydrolysis in human liver microsomes (0.2) differed largely from that in ARSC homogenate (80) and human placenta microsomes (150). These results suggest that ARSC accounts for the relatively low iodothyronine sulfatase activity of human placenta, and that additional arylsulfatase(s) contributes to the high iodothyronine sulfatase activity in human liver. Further research is needed to identify these iodothyronine sulfatases, and to study the physiological importance of the reversible sulfation of iodothyronines in thyroid hormone metabolism.

Animals↗
PubMed1983

Genetic analysis of murine arylsulfatase C and steroid sulfatase.

SWR/J mice possess two- to threefold higher 4-methylumbelliferyl sulfate (4MUS), dehydroepiandrosterone sulfate (DHEAS) and estrone sulfate (E1S) sulfatase activities in liver and kidney extracts than do A/J mice. These interstrain activity differences are maintained throughout the 6- to 45-day postnatal period. Characteristics of the hepatic activities of SWR/J mice suggest that all three activities reside in the same enzyme. Biochemical properties of the SWR/J and A/J enzyme were not significantly different. Expression of hepatic enzyme activity is subject to regulation by an autosomal locus possessing two alleles with additive effects. Postnuclear E1S- and DHEAS-sulfatase activities are primarily microsomal. Although postnuclear hepatic 4MUS-sulfatase activity is predominantly microsomal, renal activity is primarily nonmicrosomal. Only that portion of 4MUS-sulfatase occurring in cell membranes appears capable of hydrolyzing E1S and DHEAS. The hepatic- and renal-specific subcellular distributions of 4MUS-sulfatase activity may reflect tissue differences in enzyme processing. Renal 4MUS-sulfatase activity is also controlled by an autosomal gene with two alleles having additive effects. Positive correlation between hepatic and renal 4MUS-sulfatase activities indicates that both activities are most likely influenced by the same gene.

Alleles↗
PubMed1986

Steroid sulfatase. Biosynthesis and processing in normal and mutant fibroblasts.

Antibodies raised against steroid sulfatase purified from human placenta were used to follow the biosynthesis of this enzyme in human skin fibroblasts. Steroid sulfatase is synthesized as a membrane-bound Mr-63 500 polypeptide with asparagine-linked oligosaccharide chains. Within 2 days, newly synthesized steroid sulfatase is processed to a mature Mr-61 000 form. The decrease in size is due to processing of the oligosaccharide chains, which are cleavable by endoglucosaminidase H in both the early and the mature form of steroid sulfatase. The processing involves mannosidase(s) sensitive to 1-deoxy-manno-nojirimycin. The half-life of the steroid sulfatase polypeptides is 4 days. Synthesis of steroid-sulfatase-related polypeptides and steroid sulfatase activity were not detectable in fibroblasts from four patients with X-linked ichthyosis.

1-Deoxynojirimycin↗
PubMed1996

Specificity studies of bacterial sulfatases by means of structurally defined sulfated oligosaccharides isolated from shark cartilage chondroitin sulfate D.

Chondro-4-sulfatase and chondro-6-sulfatase from Proteus vulgaris and delta-hexuronate-2-sulfatase from Flavobacterium heparinum are potentially useful tools for structural studies of chondroitin sulfate and dermatan sulfate. Their substrate specificities were investigated with various structurally defined, sulfated hexasaccharides isolated from chondroitin sulfate as described in the accompanying report [Sugahara, K., Nadanaka, S., Takeda, K. & Kojima, T. (1996) Eur. J. Biochem. 239, 871-880]. The results indicated that delta-hexuronate-2-sulfatase released an ester sulfate from the C2 position of the delta-hexuronate residue located at the non-reducing terminus, while chondro-6-sulfatase removed an ester sulfate from the C6 position of the GalNAc residue at the reducing end of the hexasaccharides. Chondro-4-sulfatase acted preferentially on an ester sulfate on the C4 position of the GalNAc residue at the reducing end under mild incubation conditions, but also released a sulfate group under harsh conditions from the C4 position of the GalNAc residue at the internal positions of the hexasaccharide chains, unless the GalNAc residue had another ester sulfate on its C6 position. The results demonstrated the usefulness of the sulfatases as tools for the structural characterization of chondroitin sulfate oligosaccharides.

Animals↗
PubMed1984

Stratum corneum lipids in disorders of cornification. Steroid sulfatase and cholesterol sulfate in normal desquamation and the pathogenesis of recessive X-linked ichthyosis.

The pathological scaling in recessive x-linked ichthyosis is associated with accumulation of abnormal quantities of cholesterol sulfate in stratum corneum (J. Clin. Invest. 68:1404-1410, 1981). To determine whether or not cholesterol sulfate accumulates in recessive x-linked ichthyosis as a direct result of the missing enzyme, steroid sulfatase, we quantitated both steroid sulfatase and its substrate, we quantitated both steroid sulfatase and its substrate, cholesterol sulfate, in different epidermal strata, as well as within stratum corneum subcellular fractions obtained from normal human and neonatal mouse epidermis and from patients with recessive x-linked ichthyosis. In normal human and mouse epidermis, steroid sulfatase activity peaked in the stratum granulosum and stratum corneum, and negligible activity was detectable in lower epidermal layers. In contrast, in recessive x-linked ichthyosis epidermis, enzyme levels were virtually undetectable at all levels. In normal human stratum corneum, up to 10 times more steroid sulfatase activity was present in purified peripheral membrane preparations than in the whole tissue. Whereas in normal human epidermis cholesterol sulfate levels were lowest in the basal/spinous layer, and highest in the stratum granulosum, in recessive x-linked ichthyosis the levels were only slightly higher in the lower epidermis, but continued to climb in the stratum corneum. In both normal and in recessive x-linked ichthyosis stratum corneum, cholesterol sulfate appeared primarily within membrane domains, paralleling the pattern of steroid sulfatase localization. Finally, the role of excess cholesterol sulfate in the pathogenesis of recessive x-linked ichthyosis was directly tested by topical applications of this substance, which produced visible scaling in hairless mice in parallel to an increased cholesterol sulfate content of the stratum corneum. These results demonstrate an intimate relationship between steroid sulfatase and cholesterol sulfate in normal epidermis: both are concentrated in the outer epidermis (stratum corneum and stratum granulosum), and both are localized to membrane domains. Presumably, as a result of this distribution pattern, continued enzymatic degradation of substrate occurs in normal epidermis, thereby preventing excessive accumulation of cholesterol sulfate. In contrast, in recessive x-linked ichthyosis, degradation of cholesterol sulfate does not occur and cholesterol sulfate accumulates specifically in the stratum corneum, where it produces visible scale.

Administration, Topical↗
PubMed1986

Association of steroid sulfatase with one of the arylsulfatase C isozymes in human fibroblasts.

When arylsulfatase C, a microsomal membrane-bound enzyme, is assayed with its natural substrates, the 3-beta-hydroxysteroid sulfates, it is also known as steroid sulfatase. Whether arylsulfatase C and steroid sulfatase are identical enzymes or not, however, has long been disputed. We now report that two electrophoretic variants of arylsulfatase C occur in normal human fibroblasts: one has a single anodic band of activity, "s," and the other has an additional faster migrating band, "f". The two types, s and "f + s", occur in cells from either sex. When fibroblast strains with the f + s forms of arylsulfatase C were cloned, two types of primary clones were always obtained: s and f + s. A single f band was never seen. When these primary clones were subcloned, however, the arylsulfatase C phenotype remained unchanged: primary s clones gave rise to s subclones and f + s clones to f + s subclones only. Therefore, these forms were clonal in origin and demonstrated a novel inheritance pattern in human cultured cells. The appearance of increasing amounts of the f band was correlated with up to 4-fold increase of arylsulfatase C activity, whereas the steroid sulfatase activity remained constant, thus demonstrating that arylsulfatase C was not identical with steroid sulfatase activity. Polyclonal antibodies raised against the s form immunoprecipitated activities of the s form of arylsulfatase C and steroid sulfatase but not the f form of arylsulfatase C. Therefore, we conclude that only the s form of arylsulfatase C is immunologically related to steroid sulfatase so that arylsulfatase C per se is not necessarily identical with steroid sulfatase. In addition, a novel form of genetic heterogeneity of isozymes in human fibroblasts is demonstrated.

Antigen-Antibody Complex↗
PubMed1998

A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease.

In multiple sulfatase deficiency, a rare human lysosomal storage disorder, all known sulfatases are synthesized as catalytically poorly active polypeptides. Analysis of the latter has shown that they lack a protein modification that was detected in all members of the sulfatase family. This novel protein modification generates a 2-amino-3-oxopropanoic acid (C alpha-formylglycine) residue by oxidation of the thiol group of a cysteine that is conserved among all eukaryotic sulfatases. The oxidation occurs in the endoplasmic reticulum at a stage when the nascent polypeptide is not yet folded. The aldehyde is part of the catalytic site and is likely to act as an aldehyde hydrate. One of the geminal hydroxyl groups accepts the sulfate during sulfate ester cleavage leading to the formation of a covalently sulfated enzyme intermediate. The other hydroxyl is required for the subsequent elimination of the sulfate and regeneration of the aldehyde group. In some prokaryotic members of the sulfatase gene family, the DNA sequence predicts a serine residue, and not a cysteine. Analysis of one of these prokaryotic sulfatases, however, revealed the presence of the C alpha-formylglycine indicating that the aldehyde group is essential for all members of the sulfatase family and that it can be generated from either cysteine or serine.

Aldehydes↗
PubMed2004

Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility.

Sulfatases, which cleave sulfate esters in biological systems, play a key role in regulating the sulfation states that determine the function of many physiological molecules. Sulfatase substrates range from small cytosolic steroids, such as estrogen sulfate, to complex cell-surface carbohydrates, such as the glycosaminoglycans. The transformation of these molecules has been linked with important cellular functions, including hormone regulation, cellular degradation, and modulation of signaling pathways. Sulfatases have also been implicated in the onset of various pathophysiological conditions, including hormone-dependent cancers, lysosomal storage disorders, developmental abnormalities, and bacterial pathogenesis. These findings have increased interest in sulfatases and in targeting them for therapeutic endeavors. Although numerous sulfatases have been identified, the wide scope of their biological activity is only beginning to emerge. Herein, accounts of the diversity and growing biological relevance of sulfatases are provided along with an overview of the current understanding of sulfatase structure, mechanism, and inhibition.

Amino Acid Sequence↗
PubMed1995

Effect of Decapeptyl (a GnRH analogue) and of transforming growth factor-alpha (TGF-alpha), in the presence of heparin, on the sulfatase activity of human breast cancer cells.

The effects of the polypeptide Decapeptyl (a gonadotropin-releasing hormone (GnRH) agonist analogue) and of transforming growth factor-alpha (TGF-alpha), on estrone sulfate-sulfatase activities in the homogenates of various breast cancer cell lines were studied in the presence of heparin. In hormone-dependent MCF-7 breast cancer cells, Decapeptyl can inhibit sulfatase activity, and this effect is significantly augmented in the presence of heparin. In the other hormone-dependent T-47D breast cancer cell line, the decrease of sulfatase activity was only significant when Decapeptyl was associated with heparin. No significant effect on sulfatase activity elicited by heparin, Decapeptyl or a mixture of both was found in the hormone-independent MDA-MB-231 breast cancer cells. TGF-alpha stimulates sulfatase activity in the MDA-MB-231 cells but has no effect in the MCF-7 cells; in contrast, TGF-alpha combined with heparin provokes a decrease of the sulfatase activity in both cell lines. It is concluded that the sulfatase activity in some types of breast cancer cell can be inhibited by heparin combined with the polypeptides Decapeptyl or TGF-alpha.

Arylsulfatases↗
PubMed2004

Gonadotropin-releasing hormone agonist inhibits estrone sulfatase expression of cystic endometriosis in the ovary.

OBJECTIVE: To clarify the inhibitory effect of GnRH agonist on estrone (E(1)) sulfatase expression. DESIGN: Retrospective immunohistochemical study. SETTING: The Jikei University Hospital, Tokyo, Japan. PATIENT(S): Thirty-three women who had undergone cystectomy of the ovary or oophorectomy and were proved histopathologically to have cystic endometriosis in the ovary. INTERVENTION(S): Fifteen of the 33 patients were treated with GnRH agonists monthly for 2-6 months before surgery. The other 18 patients did not receive any hormonal therapy. Tissue sections were immunostained with an anti-E(1) sulfatase monoclonal antibody (KM1049) originating from human placenta. MAIN OUTCOME MEASURE(S): Microscopic evaluation to assess the presence and localization of E(1) sulfatase and to describe any variations in its expression with or without treatment with GnRH agonist. RESULT(S): Immunostaining showed that E(1) sulfatase was localized only on the glandular epithelial cells of cystic endometriosis in the ovary. The immunostaining with anti-E(1) sulfatase proved that GnRH agonist inhibited E(1) sulfatase expression in the cystic endometriosis in the ovary. CONCLUSION(S): Gonadotropin-releasing hormone agonist inhibits E(1) sulfatase expression in cystic endometriosis in the ovary.

Adult↗
PubMed2001

Immunohistologic localization of estrone sulfatase in uterine endometrium and adenomyosis.

OBJECTIVE: To clarify histologic localization of estrone sulfatase in normal uterine endometrium and adenomyotic tissue and to confirm that estrone sulfatase is one of the enzymes that supplies estrogen to adenomyotic tissue. METHODS: Specimens from 21 patients who had undergone hysterectomy were obtained from uteri with histopathologically proven adenomyosis. Specimens from 28 patients who had undergone hysterectomy for a disease of the uterine cervix were used as control specimens of normal uterine endometrium. Cases of hormone-dependent disease, such as leiomyoma, adenomyosis, and endometrial neoplasm, were excluded from cases of normal endometrium. The myometrium in patients with adenomyosis was examined. These tissues were examined by immunohistochemistry using anti-estrone sulfatase monoclonal antibodies. Power analysis was performed. With alpha = 0.05, 1 - beta = 0.8, P1= 25%, and P2 = 75%, 14 specimens from each group were sufficient to detect significant differences among them. The Fisher exact test, sign test, and McNemar test were used for statistical analysis. RESULTS: In normal endometrial tissue, immunostaining for estrone sulfatase was observed only on the glandular epithelial cells of the basilar layer of the endometrium. However, all functional layers of the endometria were negative for staining for estrone sulfatase. In adenomyotic tissue, glandular epithelial cells showed immunostaining for estrone sulfatase. Rates of immunostaining in adenomyotic tissue were higher than those in the basilar layer of normal uterine endometrium (76% and 43%, respectively, P =.02). The myometrium was not stained. CONCLUSION: Estrone sulfatase may be one of the enzymes supplying estrogen for growth of adenomyosis.

Adult↗
PubMed2001

Localization and expression of steroid sulfatase in human fallopian tubes.

Localization of steroid sulfatase, a membrane-bound microsomal enzyme, in human fallopian tubes was immunohistochemically investigated, and expression of RNA was confirmed by competitive RT-PCR. Human fallopian tubes were obtained from 10 patients in follicular and early luteal phases during gynecological laparotomy. An anti-human rabbit polyclonal antibody was prepared against sulfatase protein purified from human placenta. Total RNA was isolated from epithelium of fallopian tubes. A heterologous RNA competitor was designed, and competitive RT-PCR was carried out. Steroid sulfatase was localized to the cytoplasm of epithelial cells. With respect to the positive staining of cells, the number of positive secretory cells was higher than that of ciliated cells. A significantly higher number of positive cells was found in tissue obtained from the early luteal phase than that found in tissue from the follicular phase. An abundant expression of sulfatase mRNA in early luteal phase was also observed. This study demonstrates, for the first time, that steroid sulfatase is localized to human epithelial cells and that steroid sulfatase staining and mRNA expression changes with the menstrual cycle. These results suggest that sulfatase in the fallopian tube may be involved in controlling the local steroid environment, which appears to regulate aspects of the physiological reproductive function of the fallopian tube.

Adult↗