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PubMed1994

[Uterine estrogen sulfotransferase and estrogen sulfatase in embryo implantation].

The relation conjugated/unconjugated estrogens associated with reproductive processes has brought about the interest to study the biological role and regulation of the estrogen sulfotransferase and estrogen sulfatase which participate in the formation and hydrolysis of estrogen 3-sulfates, respectively. In this paper, both activities were measured through the reciprocal conversion of 3H-estrone sulfate and 3H-unconjugated estrogen during in vitro incubation with implantation sites (SI) and non-implanted sites (SNI) from the rat uterus, during the process of embryo implantation. Contrasting enzyme activities were found in these tissues. While sulfotransferase activity was higher in SI than in SNI (0.205 vs 0.144 pmol of E1S formed/mg protein/h, the inverse was found for the sulfatase (1.470 vs 1.977 pmol of E1 formed/mg protein/h). These results indicate the presence of both enzymes in the rat uterus and suggest the existence of a mechanism in SI that locally regulate the concentration of free and sulfoconjugated estrogens in which these enzymes participate.

Animals↗
PubMed2002

Molecular analysis of Turkish mucopolysaccharidosis IVA (Morquio A) patients: identification of novel mutations in the N-acetylgalactosamine-6-sulfate sulfatase (GALNS) gene.

Mucopolysaccharidosis IVA (MPS IVA) is a lysosomal storage disorder caused by the deficiency of N-acetylgalactosamine-6-sulfate sulfatase (GALNS; EC 3.1.6.4). The deficiency of N-acetylgalactosamine-6-sulfate sulfatase leads to lysosomal accumulation of undegraded glycosaminoglycans, keratan sulfate and chondroitin-6-sulfate. Mutation screening of the GALNS gene was performed by SSCP and direct sequence analyses using genomic DNA samples from 10 Morquio A patients. By nonradioactive SSCP screening, 6 different gene mutations and 2 polymorphisms were identified in 10 severely affected MPS IVA patients. Five of the mutations and one of the polymorphisms are novel. The vast majority of the gene alterations were found to be single nucleotide deletions (389delG, 929delG, and 763delT) or insertions (1232-1233insT). The other two mutations were one previously identified missense mutation (Q473X) and one novel nonsense (P179S) mutation. Together they account for 95% of the disease alleles of the patients investigated. Beside mutations, one previously identified E477 polymorphism and one novel W520 polymorphism were found among Turkish MPS IVA patients.

Adolescent↗
PubMed1980

Morquio's disease type A: absence of material cross reacting with antibodies against N-acetylgalactosamine-6-sulfate sulfatase.

An antiserum was raised in guinea pigs against purified normal human N-acetylgalactosamine-6-sulfate sulfatase, the enzyme affecting in Morquio's disease type A. The antiserum precipitated most of N-acetylgalactosamine-6-sulfate sulfatase from a concentrate of normal human urine. The antigen-antibody complex was enzymatically active. Urine concentrates from five patients with Morquio's disease type A did not contain material competing with the normal enzyme for binding to soluble or Sepharose-bound antibodies. No precipitin arc was obtained on immunodiffusion of antiserum and urine from the single patient investigated by this method. From the sensitivity of the indirect immunoassay it was concluded that the urine of the five patients contained less than 5% of the normal amount of cross-reacting material.

Antibodies↗
PubMed1976

Mosaicism for sulfoiduronate sulfatase deficiency in carriers of Hunter's syndrome.

Using an assay for sulfoiduronate sulfatase based on the degradation of 35S mucopolysaccharides in a cell-free system, two clonal populations have been demonstrated in fibroblasts of heterozygotes for Hunter's syndrome. The locus responsible for sulfoiduronate sulfatase deficiency in this X-linked mucopolysaccharidosis is therefore subjected to dosage compensation in females.

Clone Cells↗
PubMed2005

Evidence for the Cd(2+) activation of the aryl sulfatase from helix pomatia.

Often used to remove sulfate groups from carbohydrates, the regulatory properties of the aryl sulfatase from Helix pomatia remain little characterized. As many hydrolytic enzymes utilize exogenous metal ions in catalysis, the effect of various divalent metal ions on the sulfatase was investigated. Evidence for metal ion activation was collected, with Cd(2+) being notable for effective activation. The enzyme was inhibited by Cu(2+). The response of other common hydrolases to divalent metal ions was characterized. Activation by Cd(2+) was not observed for chymotrypsin, rabbit liver esterase, or beta-galactosidase. Instead, Cd was found to inhibit both the esterase and the galactosidase. Inhibition by Cu(2+) and Zn(2+) was also observed for some of these hydrolases.

Animals↗
PubMed1995

A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy.

X-linked recessive chondrodysplasia punctata (CDPX) is a congenital defect of bone and cartilage development characterized by aberrant bone mineralization, severe underdevelopment of nasal cartilage, and distal phalangeal hypoplasia. A virtually identical phenotype is observed in the warfarin embryopathy, which is due to the teratogenic effects of coumarin derivatives during pregnancy. We have cloned the genomic region within Xp22.3 where the CDPX gene has been assigned and isolated three adjacent genes showing highly significant homology to the sulfatase gene family. Point mutations in one of these genes were identified in five patients with CDPX. Expression of this gene in COS cells resulted in a heat-labile arylsulfatase activity that is inhibited by warfarin. A deficiency of a heat-labile arylsulfatase activity was demonstrated in patients with deletions spanning the CDPX region. These data indicate that CDPX is caused by an inherited deficiency of a novel sulfatase and suggest that warfarin embryopathy might involve drug-induced inhibition of the same enzyme.

Abnormalities, Drug-Induced↗
PubMed2004

Identification and biochemical characterization of an avian sulfatase homologous to the human ARSE, the gene for X-linked chondrodysplasia punctata.

Despite many efforts, the mouse homolog of ARSE, the gene implicated in X-linked recessive chondrodysplasia punctata, has not yet been identified. This absence has so far impaired a deep study of the role of this gene. For this reason, we searched the avian homolog and here report the identification of a chicken sulfatase, cARS, that shares high degree of homology with the cluster of sulfatases located on the short arm of the human X chromosome. cARS activity against a sulfated artificial substrate is heat labile and inhibited by warfarin, features that are characteristic of ARSE. The expression in pharyngeal arches, somites, and leg buds during chick development is consistent with cARS being the functional ortholog of ARSE, matching the tissues affected in this genetic disorder. The identification of the ARSE chicken gene is an important step for the study of its natural substrate and its role during development.

Amino Acid Sequence↗
PubMedDate not supplied

Unusual clinical presentation in two cases of multiple sulfatase deficiency.

Multiple sulfatase deficiency (MSD) is an inborn error of metabolism that combines the clinical features of late infantile metachromatic leukodystrophy and mucopolysaccharidosis. The characteristic biochemical abnormality is a reduction in the activities of several sulfatases, with consequent tissue accumulation of sulfatides, sulfated glycosaminoglycans, sphingolipids, and steroid sulfates. In this study we present two unusual cases of MSD with variable enzymatic deficiency of arylsulfatases A, B, and C. Both patients had ichthyosis, broad thumbs and index fingers, an unusually slow progression of the neurologic symptoms, and lacked the hepatosplenomegaly that is typical of MSD. Olivopontocerebellar atrophy was present and one patient had a large retrocerebellar cyst. Mucopolysaccharides were not detected in the urine from either subject. Leukocyte arylsulfatase A activity in patient 1 was 0.46 nmol/mg protein/hr and in patient 2 was 0.0 nmol/mg protein/hr (normal 0.7-5.0 nmol/mg protein/hr). Leukocyte arylsulfatase B activity in patient 1 was 24 nmol/mg protein/hr and in patient 2 was 22 nmol/mg protein/hr (normal 115-226 nmol/mg protein/hr). Leukocyte arylsulfatase C in patient 1 was 0.30 pmol/mg protein/hr and in patient 2 was 0.28 pmol/mg protein/hr (normal 0.84 pmol/mg protein/hr). In conclusion, these two patients with MSD had mild clinical presentations not previously reported and variable enzymatic deficiency of arylsulfatases A, B, and C.

Adolescent↗
PubMed1990

Distribution of the lysosomal enzyme aryl sulfatase in murine mammary tissue through pregnancy, lactation, and involution.

Mammary tissue from 44 primiparous mice at various stages of pregnancy, lactation, and involution were stained for aryl sulfatase (lysosomal marker enzyme) activity and prepared for electron microscopy. Stereological techniques were used to determine the distribution of lysosomes per unit of cytoplasmic area in mammary epithelial cells. The number of primary lysosomes (containing only enzyme) was stable throughout the study, except for a temporary increase following parturition. Secondary lysosomes (containing substrate undergoing active digestion) designated as either telolysosomes or dense bodies were more frequent in mammary epithelial cells from animals in the late involution and early pregnancy stages than in lactating animals. However, telolysosomes did increase temporarily at the onset of lactation and casein micelles were identified within secondary lysosomes throughout the lactation stage. The frequencies for endoplasmic reticulum and Golgi apparatus containing aryl sulfatase reaction product were highest in secretory cells, when these structures were predominant. Shifts in lysosomal populations throughout the study suggests that lysosomes may have an active role within the mammary epithelial cells during differentiation and secretion as well as during involution.

Animals↗
PubMedDate not supplied

[Aryl sulfatase of unusual specificity from the liver of marine mollusk Littorina kurila].

An aryl sulfatase of unusual specificity has been isolated from the liver of marine mollusk Littorina kurila. It hydrolyzes p-nitrophenyl sulfate, does not affect the natural fucoidan, and catalyzes splitting off of the sulfate group in position C4 of xylose residues within the carbohydrate chains of holostane triterpene glycosides from sea cucumbers. The properties of the enzyme were studied at pH 5.4. The protein is homogeneous according to electrophoresis and has M 45 +/- 1 kDa. The semiinactivation time of the enzyme at 60 degrees C is 20 min, and its Km value for the hydrolysis of p-nitrophenyl sulfate is 8.7 +/- 1 mM. It was shown that natural sulfated polyhydroxysteroids inhibit activity of the sulfatase; their I50 values depend on their structures and are within the range from 10(-3) to 10(-5) M.

Animals↗
PubMed1985

Activator protein required for the enzymatic hydrolysis of cerebroside sulfate. Deficiency in urine of patients affected with cerebroside sulfatase activator deficiency and identity with activators for the enzymatic hydrolysis of GM1 ganglioside and globotriaosylceramide.

Urine specimens from two sibs affected with cerebroside sulfatase activator deficiency were examined to ascertain whether the deficiency of the supplementary activator protein required for the enzymatic hydrolysis of cerebroside sulfate was also evident in urine. Material from chromatographic fractionations was examined for the activator activity to avoid ambiguities resulting from protein inhibition. There were substantial deficits in all chromatographic fractions corresponding to activator-containing fractions of control urines. Since patient urines contained elevated amounts of lactosylceramide, digalactosylceramide, and globotriaosylceramide and since similarities between activators for cerebroside sulfate and GM1 ganglioside hydrolyses had been noted previously, the chromatographic fractions were also examined for activators in other glycosphingolipid hydrolase systems. There was coincidence of activators for the GM1 ganglioside/beta-galactosidase and the globotriaosylceramide/alpha-galactosidase A reactions with the cerebroside sulfatase activator in control urine fractions, and the patients' urines were deficient in activator activities for the three reactions. Identity of the three activators was suggested and antiserum to purified GM1 ganglioside activator was used to test this possibility. There were depressed levels of cross-reacting material in fractions of patient urines by Ouchterlony double diffusion and in unfractionated urine by enzyme-linked immunosorbent assay. Purified activators for the cerebroside sulfate and GM1 ganglioside systems showed lines of identity with no spurring on Ouchterlony double diffusion, identical mobility on immunoelectrophoresis, and similar stimulatory activities toward hydrolysis of the three glycosphingolipid species by their respective enzymes. Finally, the three activator activities were retained by anti-GM1-activator IgG coupled to Sepharose 4B. The results suggest strongly that the same protein entity serves as activator for the enzymatic hydrolysis of cerebroside sulfate, GM1 ganglioside, and globotriaosylceramide.

Animals↗
PubMed1984

Early manifestations of multiple sulfatase deficiency.

We describe two boys, presenting by 1 year of age, with developmental delay from birth, mildly coarse facial features, and hepatomegaly. These clinical features were most suggestive of a mucopolysaccharidosis, particularly MPS II. Biochemical studies, including sulfate incorporation in fibroblasts and lysosomal enzyme analyses in fibroblasts, leukocytes, and serum, showed abnormalities in both sulfatide and mucopolysaccharide metabolism and led to the diagnosis of multiple sulfatase deficiency. With time, both patients developed an ichthyotic rash and profound intellectual deterioration. We conclude that findings in the first year of life in some patients with MSD may closely resemble those in patients with a MPS disorder rather than the late infantile form of metachromatic leukodystrophy, as is classically described. Thus, MSD should be considered in the young patient suspected of having a MPS disorder.

Cerebroside-Sulfatase↗
PubMed1982

Aryl sulfatase A in acute nonlymphocytic leukemia.

To ascertain whether estimation of urinary aryl sulfatase A (ASA) is a reliable noninvasive technique for monitoring disease activity in adult acute nonlymphocytic leukemia, we studied the excretion pattern of this enzyme during active disease, partial remission, and complete remission in ten patients and compared the results with those of ten healthy volunteers. There was no significant difference in enzyme excretion between complete remission cases and the control group. Patients with partial remission and active disease had significantly different urinary enzyme levels from each other and from the control and complete remission groups. Estimation of urinary ASA is a useful noninvasive method of monitoring disease activity in adult acute nonlymphocytic leukemia.

Acute Disease↗
PubMed1986

A new syndrome of anosmia, ichthyosis, hypogonadism, and various neurological manifestations with deficiency of steroid sulfatase and arylsulfatase C.

We describe a family consisting of 3 affected men with congenital ichthyosis, anosmia, hypogonadism, nystagmus with decreased visual acuity, strabismus, hypopigmentation of the iris, and mirror movements of the hands and feet. Two of them had limitation of ocular movement and unilateral renal agenesis or hypoplasia. The condition appears to be inherited as an X-linked recessive trait. Clinical, pathological, and biochemical evaluations were compatible with a diagnosis of X-linked ichthyosis. Steroid sulfatase and arylsulfatase C activities in leukocytes and fibroblasts were markedly diminished in the affected patients. Their hypogonadism was due to decreased luteinizing hormone-releasing hormone secretion (hypogonadotropic). Hyposecretion of antidiuretic hormone was also recognized. Chromosome analysis of leukocytes and skin fibroblasts revealed a normal 46,XY male karyotype in all of the patients.

Adolescent↗
PubMed1990

Screening for steroid sulfatase (STS) gene deletions by multiplex DNA amplification.

Deletions are the most common molecular defect in steroid sulfatase (STS) deficiency. We describe the application of multiplex DNA amplification, by polymerase chain reaction, for deletion screening in patients with STS deficiency (STS-PCR). Genomic DNA from 38 unrelated patients was amplified using two sets of primers, corresponding to the 5' and the 3' ends of the STS gene. The analysis of the amplified products was always consistent with the results obtained by Southern analysis. This method represents a sensitive fast non-radioactive test for detecting STS gene deletions.

Arylsulfatases↗
PubMed1981

Activity of steroid sulfatase in fibroblasts with numerical and structural X chromosome aberrations.

In cultured fibroblasts of patients with numerical and structural X chromosome aberrations the activity of steroid sulfatase (STS) is correlated with the number of functional STS gene copies. While normally, this X-linked gene is not inactivated, our data suggest that it may be subject to inactivation when carried on a structurally altered X-chromosome. Similar inactivation patterns have been reported earlier for the Xg locus which, like STS, is located on the distal portion of Xp.

Cells, Cultured↗
PubMed1984

A sensitive and dependable assay for distinguishing hamster and human X-linked steroid sulfatase activity in somatic cell hybrids.

A radioisotopic assay is described to distinguish between Chinese hamster and human steroid sulfatase activity in extracts prepared from hamster X human somatic cell hybrids. This assay is based on different pH optima and provides a sensitive and unambiguous biochemical marker for the short arm of the human X chromosome and as well as for otherwise genetically inactivated X chromosomes in rodent X human hybrids.

Animals↗