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)

During their differentiation in the bone marrow, eosinophilic leukocytes synthesize a number of enzymes and package them into secretory granules. The pathway by which three enzymes (peroxidase, acid phosphatase, and arylsulfatase) are segregated and packaged into specific granules of eosinophils was investigated by cytochemistry and electron microscopy. During the myelocyte stage, peroxidase is present within (a) all rough ER cisternae, including transitional elements and the perinuclear cisterna; (b) clusters of smooth vesicles at the periphery of the Golgi complex; (c) all Golgi cisternae; and (d) all immature and mature specific granules. At later stages, after granule formation has ceased, peroxidase is not seen in ER or Golgi elements and is demonstrable only in granules. The distribution of acid phosphatase and arylsulfatase was similar, except that the reaction was more variable and fully condensed (mature) granules were not reactive. These results are in accord with the general pathway for intracellular transport of secretory proteins demonstrated in the pancreas exocrine cell by Palade and coworkers. The findings also demonstrate (a) that in the eosinophil the stacked Golgi cisternae participate in the segregation of secretory proteins and (b) that the entire rough ER and all the Golgi cisternae are involved in the simultaneous segregation and packaging of several proteins.
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PMID:Segregation and packaging of granule enzymes in eosinophilic leukocytes. 545

In the previous paper we presented findings which indicated that enzyme heterogeneity exists among PMN leukocyte granules. From histochemical staining of bone marrow smears, we obtained evidence that azurophil and specific granules differ in their enzyme content. Moreover, a given enzyme appeared to be restricted to one of the two types. Clear results were obtained with alkaline phosphatase, but those with a number of other enzymes were suggestive rather than conclusive. Since the approach used previously was indirect, it was of interest to localize the enzymes directly in the granules. Toward this end, we carried out cytochemical procedures for five enzymes on normal rabbit bone marrow cells which had been fixed and incubated in suspension. The localization of reaction product in the granules was determined by electron microscopy. In accordance with the results obtained on smears, azurophil granules were found to contain peroxidase and three lysosomal enzymes: acid phosphatase, arylsulfatase, and 5'-nucleotidase; specific granules were found to contain alkaline phosphate. Specific granules also contained small amounts of phosphatasic activity at acid pH. Another finding was that enzyme activity could not be demonstrated in mature granules with metal salt methods (all except peroxidase); reaction product was seen only in immature granules. The findings confirm and extend those obtained previously, indicating that azurophil granules correspond to lysosomes whereas specific granules represent a different secretory product.
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PMID:Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. II. Cytochemistry and electron microscopy of bone marrow cells. 569 83

HL-60 promyelocytic leukemia cells differentiated to eosinophils and eosinophilic precursors when cultured under mildly alkaline conditions (pH 7.6-7.8) for 7 d without refeeding. New cytoplasmic granules appeared blue in the least mature cells and red in the most mature cells when stained with Wright-Giemsa. The granules also stained with Luxol-fast-blue, a characteristic of eosinophil granules. Furthermore, most cells contained the eosinophil major basic protein (MBP); the Charcot-Leyden Crystal (CLC) protein (lysophospholipase), eosinophil peroxidase, acid phosphatase, and arylsulfatase were also detected in a portion of these cells. The eosinophil major basic protein was found in a high proportion of undifferentiated cells, and thus may be constituitively produced. By examining finely banded chromosomes, translocation break points were demonstrated at q22 on one chromosome 16 and at q23 on the other homologue; abnormalities in this region of the long arm of 16 are a characteristic finding in the recently described syndrome of acute myelomonocytic leukemia (AMMoL) with abnormal bone marrow eosinophils. In common with the bone marrow eosinophils in these patients, the HL-60 eosinophil granules contained chloroacetate esterase and periodic-acid Schiff (PAS) reactive material; crystalloid inclusions were rare. Therefore, the HL-60 cell line appears to be an in vitro model for eosinophilopoiesis and may be specially suited for the study of the abnormal eosinophils seen in certain malignant conditions.
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PMID:Eosinophilic differentiation of the human promyelocytic leukemia cell line, HL-60. 658 34

This study has examined the fine structure and some cytochemical characteristics of the endodermal and mesothelial cells of the rhesus monkey yolk sac between 25 and 66 days of gestation. The endodermal cells were characterized by abundant granular endoplasmic reticulum, some agranular endoplasmic reticulum, a well-developed Golgi apparatus, and numerous large mitochondria. During the earlier part of the period studied, endodermal cells had a few acid phosphatase and arylsulfatase-positive lysosomes and moderate numbers of catalase-positive microperoxisomes. During the later stages of development, large granules (believed to be lysosomes) with a heterogeneous content were numerous in the cytoplasm. Mesothelial cells showed fewer development changes. Throughout this period they were usually flattened cells with long microvilli, small mitochondria, and limited amounts of granular endoplasmic reticulum. The mesothelial cells had acid phosphatase reaction product in the Golgi region and occasional large vesicles, but were negative for arylsulfatase and catalase. One specimen was incubated at 37 degrees C in the presence of horseradish peroxidase in order to examine endocytosis. Both the mesothelial cells and endodermal cells internalized the peroxidase into a variety of cytoplasmic vesicles. Based on their cytology, the endodermal cells may function in the synthesis of serum proteins during this period, as has been suggested in other species. They may also be involved in lipid metabolism. The mesothelial cells appeared less synthetically active, but evidence suggested that they may be involved in collagen and extracellular matrix production. The endocytic activity displayed by both cell types may indicate a role in fluid and metabolite transfer across the epithelia. The cytology of both cell types was very similar to that described for human yolk sacs, suggesting that the rhesus monkey may be a useful species in which to study the maturation of yolk sac function.
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PMID:A fine structural and cytochemical study of the rhesus monkey yolk sac: endoderm and mesothelium. 684 66

Fc receptors on the luminal membranes of intestinal epithelial cells in the neonatal rat mediate the vesicular transfer of functionally intact IgG from the intestinal lumen to the circulation. In addition, there is a low level of nonselective protein uptake, but in this case transfer does not occur. To determine whether a specialized class of endocytic vesicles could account for the selective transfer of IgG, mixtures of IgG conjugated to ferritin (IgG-Ft) and unconjugated horseradish peroxidase (HRP) were injected together into the proximal intestine of 10-d-old rats, and the cellular distribution of these two different tracers was determined by electron microscopy. Virtually all apical endocytic vesicles contained both tracers, indicating simultaneous uptake of both proteins within the same vesicle. However, only IgG-Ft bound to the apical plasma membrane, appeared within coated vesicles at the lateral cell surface, and was released from cells. HRP did not bind to the luminal membrane and was not transferred across cells but was confined to apical lysosomes as identified by acid phosphatase and aryl sulfatase activities. To test the possibility that the binding of IgG to its receptor stimulated endocytosis, HRP was used as a fluid volume tracer, and the amount of HRP taken up by cells in the presence and absence of IgG was measured morphologically and biochemically. The results demonstrate that endocytosis in these cells is constitutive and occurs at the same level in the absence of IgG. The evidence presented indicates that the principal selective mechanism for IgG transfer is the binding of IgG to its receptor during endocytosis. Continued binding to vesicle membranes appears to be required for successful transfer because unbound proteins are removed from the transport pathway before exocytosis. These results favor the proposal that IgG is transferred across cells as an IgG-receptor complex.
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PMID:Evidence for the sorting of endocytic vesicle contents during the receptor-mediated transport of IgG across the newborn rat intestine. 729 22

We have used two electron microscopic tracers, asialoorosomucoid covalently coupled to horseradish peroxidase (ASOR-HRP) and lactosaminated ferritin (Lac-Fer), to investigate the internalization of proteins bound by the asialoprotein receptor of rat hepatocytes. Both ligands are cleared rapidly from the circulation of rats, are retarded in their clearance by an excess of ASOR and accumulate principally in the liver. Morphological examination of the livers of rats after injection of the probes confirmed that the hepatocyte is the principal liver cell involved in the clearance of galactose-terminating proteins. Internalization occurred via coated pits and coated vesicles of 1000 A diameter. At 30 sec to 2 min the tracers began to accumulate in a complex arrangement of larger smooth-surfaced vesicles and tubular structures at the sinusoidal periphery of the cell. Fluid phase pinocytosis did not appear to account for any of the uptake into larger vesicles. The particulate tracer, Lac-Fer, was closely apposed to the membrane of coated pits and vesicles, but was found scattered throughout the lumen of the larger vesicles, possibly indicating dissociation of the ligand from its receptor. Although occasional lysosomes were detected cytochemically in the cell periphery, vesicles containing Lac-Fer showed no demonstrable aryl sulfatase activity. At 5 min, the tracers began to appear in Golgi-lysosome regions of the hepatocyte and were present in small vesicles of <2000 A in diameter, larger irregular vesicles and tubules. Serial sectioning indicated that tubular structures in Golgi-lysosome regions were often interconnected to the larger vesicles, but that tubules in the peripheral cytoplasm were only occasionally connected to larger structures. Some of the Lar-Fer-containing vesicles in Golgi-lysosome areas at 15 min after injection were found to contain aryl sulfatase reaction product, indicating fusion with lysosomes.
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PMID:The galactose-specific recognition system of mammalian liver: the route of ligand internalization in rat hepatocytes. 740 14

The murine steroid sulfatase (mSTS) is a microsomal enzyme, important in steroid metabolism. In the mouse, the gene encoding mSTS is pseudoautosomal and thus escapes X-inactivation. We have purified steroid sulfatase approximately 30-fold from mouse liver microsomes and its properties have been investigated. The major steps in the purification procedure included solubilization with Triton X-100, gel filtration chromatography, DEAE-Sephadex chromatography and HPLC gel filtration chromatography. The purified sulfatase showed a relative molecular weight of 128 kDa on HPLC gel filtration, whereas the enzyme migrated as two bands of 60 and 68 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point of steroid sulfatase was estimated to be 6.2 by column chromatofocusing. Polyclonal antibodies to the purified protein were prepared. An Enzyme Linked Immunosorbent Assay (ELISA) was developed using purified monospecific anti-mSTS antibodies labelled with peroxidase. The standard criteria of precision and reproducibility were satisfied. The assay was applicable to routine determination of mSTS samples in research laboratories. Differences in mSTS liver concentrations were used to identify putative alleles for the mSTS gene (Sts). Results in ELISA confirmed the polymorphism previously demonstrated for an enzymatic mSTS activity assay in two inbred mouse strains.
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PMID:Murine steroid sulfatase (mSTS): purification, characterization and measurement by ELISA. 785 78

Steroid sulfatase (STS) desulfates a number of 3 beta-hydroxysteroid sulfates, converting inactive steroid hormone to the active form. We have established an enzyme-linked immunosorbent assay (ELISA) of STS by using polyclonal antibody against STS purified from human placenta to measure the amount of the enzyme protein in sera. ELISA was performed by a 'Sandwich' method using a peroxidase conjugated anti-STS IgG Fab' fragment. A range of STS of 10-1,500 ng/ml in serum was assayed by this method. When the serum STS from the patients with gynecologic carcinomas was assayed by the ELISA, the level was significantly elevated in endometrial carcinoma (P < 0.05) and ovarian carcinoma (P < 0.01), respectively, as compared with that of normal healthy women.
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PMID:Serum levels of steroid sulfatase protein in gynecologic carcinomas. 807 Jan 31

Renal damage caused by polycationic peptides is well documented, but renal damage caused by polyanionic peptides is not. During our attempts to inhibit the nephrotoxicity of aminoglycoside antibiotics by polyanionic peptides, we discovered that poly-D-glutamic acid (molecular weight, 20 kd; 250 mg/kg/day subcutaneously for 1 to 4 days) produces an acute thesaurismosis in the proximal tubular cells associated with a marked proliferation of peritubular interstitial cells in rat kidney. Thesaurismotic bodies were easily visualized by light microscopy at the basal pole of proximal tubular cells with the cationic stain Giemsa. By electron microscopy, these bodies appeared membrane-limited, frequently distorted, filled with heterogeneous granular material, accessible to injected peroxidase (a tracer of the endocytic pathway), and generally stainable for the lysosomal enzyme arylsulfatase. Specimens obtained 3 hours after injection of poly-D-glutamic acid and horseradish peroxidase suggested an impairment of endosome and/or lysosome fission, but not fusion. By histoautoradiographic examination after 3H-thymidine incorporation, global labeling indices of cortical cells were increased 11- to 18-fold in poly-D-glutamic acid-treated rats as compared with controls, with > 80% of labeled cells localized in the interstitium. Distal tubular and glomerular cells also showed a moderate proliferation, but proximal tubular cells showed no significant necrosis or proliferation. Although tubular thesaurismosis persisted, interstitial cell proliferation resolved within 7 days after cessation of treatment. We suggest that poly-D-glutamic acid is a convenient tool to induce a rapid and sustained lysosomal storage disorder. It could also help clarify the relationship between insults to tubular cells and proliferation of peritubular cells, two features frequently associated in tubulointerstitial disorders. The mechanism of the thesaurismosis and of the interference with the dynamics of fusion-fission of the endocytic apparatus are addressed in the companion paper.
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PMID:Poly-D-glutamic acid induces an acute lysosomal thesaurismosis of proximal tubules and a marked proliferation of interstitium in rat kidney. 866 6

Eosinophils have a characteristic content of cationic proteins, stored in core-containing specific granules and released at sites of inflammation; coreless granules (sometimes called primary) are present in eosinophil promyelocytes. In order to determine a possible relationship between the two granule subsets, immunoelectron-microscopic techniques were used to determine the presence and precise intragranular distribution of major basic protein (MBP), eosinophil cationic protein (ECP), eosinophil peroxidase (EPO), and arylsulfatase B of eosinophil granules, as well as the Charcot-Leyden crystal (CLC) protein, in eosinophil progenitors of the bone marrow. MBP, ECP, EPO, and arylsulfatase B were observed in both coreless and core-containing (specific) granules. The difference in the distribution of MBP, having a uniform distribution in coreless granules and a crystalloid distribution in core-containing (specific) granules, could indicate a maturational process of a common organelle. CLC protein was distributed in the cytosol, in the euchromatin of the nuclei, but was also present in a rare granular compartment of both immature and mature eosinophils. The present findings suggest that coreless granules develop into core-containing specific granules.
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PMID:Localization of granule proteins in human eosinophil bone marrow progenitors. 933 6


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