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

---

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

Two methods for the extraction of acrosomal membranes and enzymes from both human and rabbit spermatozoa were compared. Treatment of spermatozoa with hypotonic MgCl2 (0.05 M) solution causes removal of the plasma membrane, vesiculation, disruption and removal of the outer acrosomal membrane posterior to the equatorial segment with accompanying loss of soluble acrosomal material. Subsequent exposure to Hyamine 2389 and Triton X-100 removes acrosomal material bound to the inner acrosomal membrane with concomitant solubilization of this membrane. The MgCl2 extract from rabbit spermatozoa contained a higher yield of hyaluronidase, acrosin, and total proteinase activities, whereas the subsequent detergent extracts contained higher yields of both arylsulfatase A and B activities. By comparison, after 4 minutes of sonication to separate heads and tails, both rabbit and human spermatozoa when viewed by transmission electron microscopy showed alterations of plasma and outer acrosomal membranes with considerable loss of the acrosomal contents. Analysis of acrosomal enzymes indicates the greatest percentage of all the enzymes assayed was located in the extract obtained by sonication in contrast to either the separated head or tail fractions used for further subcellular extraction. Subsequent treatment with Hyamine and Triton yields only minimal amounts of enzyme activity.
...
PMID:Extraction of human and rabbit acrosomes: a comparison of sequential and sonication methods. 51 71

The ultrastructural changes of a sural nerve biopsy, liver biopsy and the autopsy of a case (I) of fucosidosis are described. Light microscopy revealed the presence of foam cells in various organs. The contents of the vacuoles stained positive with P.A.S. and Sudan. Electron microscopical examination showed inclusions in hepatocytes, Schwann cells and neurons. These inclusions had a single limiting membrane and contained heterogeneous structures, vesicular, multivesicular and membrane like structures, forming concentric lamellae. In another patient (case III) with a different clinical presentation and a different enzyme pattern (a reduced alpha-L-fucosidase activity, in combination with a reduced arylsulfatase A activity) similar abnormalities as in case I were found in a sural nerve and liver biopsy. It is suggested that the combined reduction of enzyme activity is responsible for the disease.
...
PMID:Fucosidosis. II. Ultrastructure. 57 98

The effects of age-specific peculiarities and the duration of maintaining rats on a ration with 4 per cent of protein (the initial mass of rats in the 1st group 100 g each; duration of the experiment--30 days. Initial mass rats in the 2d group--200 g each; duration of experiment--90 days on the activity of the lysosomal hydrolase was studied. The latter included beta-glucosidase, beta-galactosidase, beta-glucoronidase, beta-N-acetylglucosaminidase, arylsulfatase A and B, acid phosphatase, phospholipase A1 and A2, cholinesterase, the total proteolytic activity and that of catepsines A, B, C and D. An ambiguity of changes in the enzymes activity in the animals of the 1st and 2d groups was revealed. Placing the growing animals on a ration containing 4 per cent of protein produces an activation of the most of the lysosomal enzymes, whereas in animals of the 2d test group the nature of changes in the activity of individual enzymes proved to differ quite appreciably. Thus, the summary activity of catepsines, beta-glucoronidase and cholinesterase was below the control level, while the activity of beta-galactosidase, beta-N-acetyl-glucoseaminidase and phospholipase A1 and A2 went up. A prolonged maintenance of rats on a protein-poor ration led to upsetting the stability of the lysosomal membranes, which manifested itself in a higher solubilization of lysosomal enzymes in vitro.
...
PMID:[Characteristics of the enzymatic adaptation of rat liver lysosomes to protein deficiency]. 68 19

The distribution of soluble arylsulfatase (aryl-sulfate sulfohydrolases, EC 3.1.6.1) in human tissues was investigated by DEAE-cellulose chromatography, All tissues examined contained arylsulfatase A and arylsulfatase B. In addition, brain singularly contained significant quantities (15-25% of total arylsulfatase) of a minor anionic arylsulfatase from designated arylsulfatase Bm, whereas only trace amounts of arylsulfatase Bm were found in liver, kidney, testis and placenta. Arylsulfatase B and arylsulfatase Bm had equal activity toward methyl-umbelliferyl sulfate, nitrocatechol sulfate and a physiological substrate UDP-N-acetylgalactosamine 4-sulfate, but both forms were inactive toward the arylsulfatase A substrates cerebroside sulfate and ascorbic acid 2-sulfate. Purified preparations of placental arylsulfatase B, brain arylsulfatase Bm, and urinary arylsulfatase A did not hydrolyze estrone sulfate, dehydroepiandrosterone sulfate or pregnenolone sulfate. The physico-chemical properties of arylsulfatase Band arylsulfatase Bm differed with respect to thermal lability, DEAE-cellulose chromatography, polyacrylamide gel electrophoresis and isoelectric focussing. In the latter technique, utilizing thin polyacrylamide slab gels, the isoelectric point for placental arylsulfatase B was 8.2, while brain arylsulfatase Bm resolved into 3 activity bands with pI values 6.8, 7.0 and 7.2. Although the physico-chemical properties differed, arylsulfatase B and arylsulfatase Bm appear to be functionally equivalent as well as generically related.
...
PMID:Arylsulfatase of human tissue. Studies on a form of arylsulfatase B found predominantly in brain. 87 49

In an effort to improve the precision in prenatal monitoring for metachromatic leukodystrophy, levels of cerebroside sulfatase were determined in fibroblasts and amniotic fluid cells. Cells from MLD patients demonstrated no significant sulfatide hydrolysis, whereas cultures from heterozygous subjects hydrolyzed diminished but definite amounts of sulfatide. Cells from a fetus with low arylsulfatase A activity were able to cleave considerable amounts of sulfatide; enzyme assays performed postnatally suggest that the infant is heterozygous for MLD. This report documents the value of cerebroside sulfatase assays in the in utero monitoring for MLD.
...
PMID:Cerebroside sulfatase activity in cultivated human skin fibroblasts and amniotic fluid cells;. 112 3

In a family with juvenile metachromatic leukodystrophy (sulfatide lipidosis) 2 patients showed residual arysulfatase A activities of 5--6%. The patients' healthy father was characterized biochemically by a 39% normal activity of leukocyte plus plasma arylsulfatase A. The father was further characterized by a high sulfatide excretion (0.2--0.5 mg/I urine) and, paradoxically, by a normal sulfatide degrading enzyme activity in vitro. This special carrier is suspected to be heterozygous for a) arylsulfatase A deficiency and b) arylsulfatase A (sulfatidase) lability. This presumed additional genetic defect could be the cause of the sulfatide excretion which, in turn, would be a sign of the preclinical stage of an exceptional form of adult metachromatic leukodystrophy. The normal sulfatidase activity seems to be due to an in vitro effect.
...
PMID:Sulfatide excreting heterozygous carrier of juvenile metachromatic leukodystrophy or asymptomatic patient of adult metachromatic leukodystrophy. 117 45

The human colon adenocarcinoma cell lines SW 948, SW 1116, and SW 1222 were tested for their ability to sort and internalize lysosomal enzymes. The biosynthesis of the lysosomal enzymes cathepsin B, arylsulfatase A, and beta-hexosaminidase in these cell lines exhibits no significant differences to that in human fibroblasts. The intracellular targeting of newly synthesized hydrolases to the lysosomes relies in colon carcinoma cells on the mannose 6-phosphate receptor system. Both the cation-independent mannose 6-phosphate receptor (CI-MPR) and the cation-dependent mannose 6-phosphate receptor are expressed in all colon carcinoma cell lines investigated. Endocytosis of lysosomal enzymes via mannose 6-phosphate receptors is reduced in colon carcinoma cells as compared with human fibroblasts. SW 1116 cells were shown to be deficient in receptor-mediated endocytosis of mannose 6-phosphate containing ligands. Ligands of other endocytic receptors as well as the fluid-phase marker horseradish peroxidase were internalized at normal rates. While antibodies against CI-MPR bind to the surface of SW 1116 cells, these antibodies cannot be internalized. These data suggest that the cycling of CI-MPR is specifically impaired in SW 1116 cells.
...
PMID:Biosynthesis and endocytosis of lysosomal enzymes in human colon carcinoma SW 1116 cells: impaired internalization of plasma membrane-associated cation-independent mannose 6-phosphate receptor. 132 52

A previously suggested model for the correlation between residual activity of a lysosomal enzyme and the turnover rate of its substrate(s) has been extended to a discussion of substrate accumulation rates in individual cells and whole organs. With these considerations, much of the observed variability in age of onset and clinical phenotype, as well as the phenomenon of pseudo-deficiency, can be understood as the consequences of small differences in the residual activity of the affected enzyme. In order to experimentally verify the basic assumptions on which this model rests, studies were performed in cell culture. The radiolabeled substrates ganglioside GM2 and sulfatide were added to cultures of skin fibroblasts with different activities of beta-hexosaminidase A or arylsulfatase A, respectively, and their uptake and turnover measured. In both series of experiments, the correlation between residual enzyme activity and the turnover rate of the substrate was essentially as predicted: degradation increased steeply with residual activity, to reach the control level at a residual activity of approximately 10-15% of normal. All cells with an activity above this critical threshold had a normal turnover. Comparison of the results of these feeding studies with the clinical status of the donor of each cell line basically confirmed our notions but also revealed the limitations of the cell culture approach.
...
PMID:Quantitative correlation between the residual activity of beta-hexosaminidase A and arylsulfatase A and the severity of the resulting lysosomal storage disease. 134 43

Multiple sulfatase deficiency (MSD) is an inherited lysosomal storage disease characterized by the deficiency of at least seven sulfatases. The basic defect in MSD is thought to be in a post-translational modification common to all sulfatases. In accordance with this concept, RNAs of normal size and amount were detected in MSD fibroblasts for three sulfatases tested. cDNAs encoding arylsulfatase A, arylsulfatase B, or steroid sulfatase were introduced into MSD fibroblasts and fibroblasts with a single sulfatase deficiency by retroviral gene transfer. Infected fibroblasts overexpressed the respective sulfatase polypeptides. While in single-sulfatase-deficiency fibroblasts a concomitant increase of sulfatase activities was observed, MSD fibroblasts expressed sulfatase polypeptides with a severely diminished catalytic activity. From these results we conclude that the mutation in MSD severely decreases the capacity of a co- or post-translational process that renders sulfatases enzymatically active or prevents their premature inactivation.
...
PMID:Multiple sulfatase deficiency: catalytically inactive sulfatases are expressed from retrovirally introduced sulfatase cDNAs. 134 58

Highly purified cerebroside sulfate activator from pig kidneys was characterized by a number of chemical and biological procedures. Methods for chemical modifications were evaluated in an attempt to obtain biologically active derivatives. Iodination, dabsylation, and to a lesser degree reductive methylation provided useful products with good retention of cerebroside sulfate activator activity. Other procedures resulted in largely inactive derivatives or losses in both protein and biological activities. Attempts at renaturation of cerebroside sulfate activator subjected to various denaturing conditions appeared to be successful in many instances, but it was uncertain if the protein structure had actually been disrupted. The binding of cerebroside sulfate by activator was estimated by gel filtration under conditions similar to those of its assay. The formation of a relatively stable 1:1 complex was observed, collaborating results with the human protein. The complex was stable enough to be isolated and shown to be an efficient substrate for arylsulfatase A. The effectiveness of the pig kidney cerebroside sulfate activator for correcting the metabolic defect in activator-deficient human fibroblasts was compared with human materials. The pig kidney protein was taken up more efficiently by the cells and resulted in a better metabolic correction than material from human liver, but was somewhat less effective than a preparation from human urine.
...
PMID:The cerebroside sulfate activator from pig kidney: derivitization, cerebroside sulfate binding, and metabolic correction. 134 22


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---