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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)
Arylsulfatases are a group of enzymes that remove sulfate moieties from a diverse set of substrates including glycoproteins, steroids, and cerebrosides. We have isolated recombinant cDNA clones corresponding to an
arylsulfatase
(SpARS) message that encodes an abundant protein of pluteus larvae of the sea urchin Strongylocentrotus purpuratus. Although vertebrate arylsulfatases have broad tissue distributions, in situ hybridization with a probe for SpARS shows that the sea urchin message accumulates in the embryo only in the single cell type of aboral ectoderm and its precursors. The message is first detectable by RNase protection assays around hatching blastula stage and accumulates through pluteus larva stage. The open reading frame of cDNA clones is 1701 nt long and encodes a deduced protein with a predicted molecular mass of 61 kDa. Analysis of corresponding genomic DNA clones reveals that the pre-mRNA contains six exons. Consistent with the fact that
arylsulfatase
enzyme activity is extracellular, this polypeptide has a hydrophobic leader sequence and three potential glycosylation sites. Furthermore, hybridization in situ shows that in blastulae
arylsulfatase
message is preferentially concentrated around nuclei at the basal sides of cells. The S. purpuratus sequence is very similar to that recently reported for the same enzyme from Hemicentrotus pulcherrimus and 30% of the amino acid residues are also identical to those of both human
arylsulfatase C
(
steroid sulfatase
) and
arylsulfatase A
. Sequence relationships among these four mRNAs suggest that, assuming equal rates of evolution, the duplication separating the human genes occurred at about the time of separation of the echinoderm and vertebrate lineages.
...
PMID:Structure and tissue-specific developmental expression of a sea urchin arylsulfatase gene. 276 35
Steroid sulfatase
activity was quantified in liver microsomes from hypophysectomized adult female rats treated with estradiol and continuous or intermittent human growth hormone (hGH). Hypophysectomy clearly enhanced
sulfatase
activity as compared to intact female rats. Normal female values were completely restored by continuous infusion of hGH (1.4 i.u./kg/day). Neither the same dose of hGH given as two daily injections nor estrogen replacement therapy had any effect. It is concluded that liver microsome
sulfatase
activity in the non-pregnant rat is regulated by the sexually dimorphic secretory pattern of GH.
...
PMID:Secretory pattern of growth hormone regulates steroid sulfatase activity in rat liver. 277 33
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.
...
PMID:Steroid sulfatase. Biosynthesis and processing in normal and mutant fibroblasts. 294
It is now well established that the activity of certain liver enzymes displays sex differences and that administration of human growth hormone to male rats alters the liver metabolism in a "female" direction. In this work we studied
steroid sulfatase
activity and binding of estradiol-17 beta in livers from intact rats and found a sex difference, with considerably higher enzyme activity in male as compared to female liver tissue. Continuous infusion of native and recombinant human growth hormone and estradiol-17 beta to male rats reduced
sulfatase
activity to "female" levels. A specific binding of estradiol-17 beta with receptor properties was found in the rat livers, but the concentration of binding sites did not change after administration of growth hormone or estradiol in this group of intact animals. Our data confirm previous reports that continuous administration of human growth hormone "feminize" liver metabolism, and since estradiol was found to have an identical effect on
sulfatase
activity it is suggested that the effect of estradiol-17 beta in this respect may be indirect, mediated via an altered secretory pattern of rat growth hormone.
...
PMID:Effects of estrogen and growth hormone on steroid sulfatase activity and estrogen binding in rat liver. 296 75
Collagenase-dispersed cells from human chorion laeve were examined on Percoll gradients. The 3 beta-hydroxysteroid dehydrogenase (a trophoblast marker) and
steroid sulfatase
activities of the cells were measured and a system was developed to isolate enriched preparations of the trophoblast cells. No cells were found to sediment at Percoll concentrations greater than 50%, and using continuous gradients of Percoll there appeared to be cells with different 3 beta-hydroxysteroid dehydrogenase (3 beta HSD):
steroid sulfatase
ratios sedimenting in different regions of the gradient. Cells with a high ratio were found in the denser region of the gradient. Continuous gradients provided inadequate separations of distinct populations of cells, thus to obtain a more reproducible system to isolate cells, discontinuous gradients of Percoll were studied. A discontinuous gradient composed of 5, 20, 40, and 60% Percoll was developed and three bands of cells were found sedimenting at the 20, 40 and 60% interfaces, respectively. The number and appearance of cells at the 20 and 60% interfaces varied from tissue to tissue. In contrast, the cells sedimenting at the 40% interface were less variable, a substantial number was found to be present in every tissue studied, they were similar in appearance to the trophoblast cells and had high 3 beta HSD:
sulfatase
ratios.
...
PMID:Steroid metabolism by cells from human chorion laeve isolated on Percoll gradients. 300 69
Steroid sulfatase
(
STS
) activity was studied in Long-Evans rat testis. The affinity of the enzyme was shown to increase during postnatal development and to be always higher in purified Leydig cells than in seminiferous tubules.
STS
activity appeared to be higher in the seminiferous tubules at the earlier stages. In vivo injection of 100 IU hCG resulted in a decrease in the affinity and an increase in the activity of the enzyme expressed in Leydig cells with no such modification in seminiferous tubules. This suggests that
STS
could play a regulatory role in testosterone production by Leydig cells.
...
PMID:Ontogenesis and regulation of steroid sulfatase activity in Leydig cells and seminiferous tubules in the Long-Evans rat. 316 33
Multiple sulfatase deficiency is a lysosomal storage disorder, which can be divided into group I with severe and group II with moderate deficiencies in sulfatases. Antibodies raised against
steroid sulfatase
purified from human placenta were used to follow the biosynthesis and stability of this enzyme in multiple
sulfatase
-deficiency fibroblasts. Fibroblasts from both groups synthesized
steroid sulfatase
of apparently normal size and stability, while the apparent rate of enzyme synthesis and catalytic properties of
steroid sulfatase
were affected to a variable extent. Cell lines were observed, that synthesized normal amounts of steroid-
sulfatase
polypeptides, which were catalytically inactive, as well as cell lines that synthesized diminished amounts of catalytically active
steroid sulfatase
.
...
PMID:Synthesis and stability of steroid sulfatase in fibroblasts from multiple sulfatase deficiency. 316 68
We isolated 12 strictly anaerobic steroid-3-sulfate-desulfating strains from the intestinal floras of rats and humans. Two strains (S1 and S2) of the same atypical Clostridium species and an atypical Lactobacillus strain (termed R9) were obtained from rats. The human isolates were identified as Eubacterium cylindroides (two strains, H1 and H2), Peptococcus niger (two strains, H4 and H89), and Clostridium clostridiiforme. We also isolated, from different human fecal samples, four strains of phenotypically similar asaccharolytic Bacteroides strains, H6.2a, H6.2b, H65, and H175. Aryl
steroid sulfatase
activity for estrogen sulfates was present in all isolates. Alkyl
steroid sulfatase
activity for both 3 alpha- and 3 beta-sulfates was found only in P. niger H4. The same P. niger strain and Clostridium strains S1 and S2 also possessed bile acid
sulfatase
activity.
...
PMID:Isolation and identification of intestinal steroid-desulfating bacteria from rats and humans. 317 14
Steroid sulfatase
(
STS
) and aryl
sulfatase
C (ASC) in leucocytes, as well as the electrophoretic mobility of the beta-lipoproteins, were analyzed in 34 patients with autosomal dominant ichthyosis (ADI), 18 patients with X-linked recessive ichthyosis (XRI), 7 patients with congenital nonbullous ichthyosis (CNBI), and 48 controls. The geometric means of both
STS
and ASC were significantly lower in the group of XRI by a factor of approximately 10. Analysis of ASC showed a clear separation of the whole group of XRI patients opposed to patients with ADI and CNBI and the controls, whereas an overlapping was observed for
STS
. With one exception, the clinical and biochemical diagnosis (
sulfatase
) was confirmed by the results of the lipoprotein electrophoresis (LPE). This case, clinically and biochemically diagnosed as XRI, exhibited normal electrophoretic mobility of beta-lipoproteins. We conclude: if the electrophoretic mobility of beta-lipoproteins is enhanced, XRI can be diagnosed; if the LPE is normal, XRI cannot be excluded; in this case, the diagnosis of XRI can be confirmed or rejected by analysis of the microsomal sulfatases.
...
PMID:[Biochemical diagnosis of X chromosomal ichthyosis]. 345 82
The purpose of this study was to develop primary cultures of human chorion laeve cells and examine certain aspects of steroid metabolism during culture. Tissues obtained by elective cesarean section at term (38-40 weeks) were dispersed with collagenase. Cells were isolated on Percoll gradients at the interface between 20% and 40% Percoll and examined in primary culture for up to 1 week. Cultures were carried out in chemically defined media supplemented with 10% or 0.1% fetal calf serum (FCS). The morphological and biochemical properties of the cells were different in the two systems. In 0.1% FCS, cells formed clumps of tissue within 16 h of plating, and there was no cell replication. In contrast, in 10% FCS, the cells formed a carpet of tissue and reached confluence after 5 days in culture, resulting in increased DNA and protein content and thymidine incorporation in the dishes. Three steroidogenic enzymes were studied during culture: alkyl
steroid sulfatase
,
estrogen sulfatase
and 3 beta-hydroxysteroid dehydrogenase. The sulfatases had higher activities in 0.1% than in 10% FCS, and their activities decreased markedly during the culture period. In contrast, 3 beta-hydroxysteroid dehydrogenase activity was higher in 10% FCS than in 0.1% FCS. Activity remained constant during the culture period in 0.1% FCS and increased in 10% FCS. In the latter system this increase resulted in the enzyme maintaining a constant specific activity during culture. These studies describe two viable systems of chorion laeve cells in primary culture, which may be valuable for studying long term and/or subtle effects on various metabolic aspects of this tissue.
...
PMID:Primary culture of cells from human chorion laeve: steroid metabolism and properties of cells grown in defined media supplemented with 0.1% or 10% fetal calf serum. 345 98
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