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:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ultrastructural study of the midgut of Calanoid Copepods revealed the presence of several cell types in all species. In a previous report we described and assigned a function to each of these cell types. In order to affirm the validity of those assignments we undertook an investigation of enzymatic activity especially of phosphatase and arylsulphatase. By cytochemical methods, alkaline phosphatase activity was detected in R-, R'-D- and B-cells, with labelling being observed on the apical plasmic membrane level in all four, and in B-cells on the pinocytotic vesicle membranes. Acid phosphatase and aryl-sulphatase activities were only detectable in B-cells; the most frequently labelled structures were located in the vacuolar system, dictyosomes and Golgi vesicles, although Golgi structures occasionally reacted to acid phosphatase. Nome of the dense bodies observed in B-cells reacted to arylsulphatase. Similarly they were unevenly labelled during acid phosphatase tests. Hence it may be assumed that dense bodies are not involved in hydrolases. It is possible that these enzymes originated from vesicles generated by the Golgi saccules surrounding and joined to the vacuoles, thus bypassing the lysosome I stage.
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PMID:Cytochemical detection of phosphatase and arylsulphatase activities in the midgut of Centropages typicus (Copepod, Calanoid). 609 19

Kupffer cells are the sinusoidal macrophages of the liver. Using ultrastructural phosphatase cytochemical methods, we examined the relationship between the Golgi apparatus, GERL, and lysosomes of Kupffer cells in fetal rat livers identified, in part, by their ability to phagocytize intravenously injected latex spheres. Thiamine pyrophosphatase (TPPase) activity was localized to the inner Golgi saccules and some vesicles in the Golgi region but not to GERL. A TPPase-like activity, demonstrable in lysosomes, was abolished by sodium fluoride but not suppressed by the alkaline phosphatase inhibitors L-cysteine and L-p-bromotetramisole. Acid phosphatase (AcPase) was localized by GERL, some coated vesicles, and in lysosomes, but not to the Golgi stacks. Continuities between GERL and lysosomes were observed. Phagosomes containing internalized latex spheres received TPPase and AcPase sequentially. TPPase was localized in phagosomes immediately after latex administration. AcPase activity was not found here until at least 10 minutes following the injection of the particulates. Our findings indicate that Kupffer cell lysosomes are derived from GERL, but also suggest that phagosomes may receive material packaged by the Golgi apparatus as well as GERL.
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PMID:The relationships between the Golgi apparatus, GERL, and lysosomes of fetal rat liver Kupffer cells examined by ultrastructural phosphatase cytochemistry. 611 32

Rat kidney cortex slices were homogenized with a polytron in a isoosmotic medium containing 5 mmol/l EGTA. By two precipitations with MgCl2 (12 mmol/l) and differential centrifugation, brush border membranes were purified. The brush border marker enzymes alkaline phosphatase and aminopeptidase M were found to be enriched 17.0 +/- 5.3-fold and 16.7 +/- 3.7-fold, respectively. By this method, a high yield of brush border membranes was obtained (48.3 +/- 7.9% for alkaline phosphatase; 47.0 +/- 9.5% for aminopeptidase M). The acid phosphatase was enriched 5-fold, whereas other lysosomal enzymes (glucosaminidase, glucuronidase, cathepsin D) were enriched only 0.2-fold. Acid phosphatase activity could not be washed out, but could be separated from alkaline phosphatase and leucine aminopeptidase by means of free flow electrophoresis and sucrose density gradient centrifugation. Vesicles prepared by the presently described Mg/EGTA-method show better transport properties, compared to vesicles prepared by the calcium method of Evers et al. (Evers, C., Haase, W., Murer, H. and Kinne, R. (1978) Membrane Biochem. 1, 203-219), whereas by SDS-polyacrylamide gel electrophoresis, no differences in the protein patterns were observed.
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PMID:A high yield preparation for rat kidney brush border membranes. Different behaviour of lysosomal markers. 611 19

Human lymphocytes were isolated from defibrinated blood by Ficoll-Hypaque centrifugation with erythrocyte hypotonic lysis. Homogenates of mixed lymphocytes were subjected to analytical subcellular fractionation by sucrose gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their marker enzymes: cytosol (lactate dehydrogenase), plasma membrane (5'-nucleotidase), endoplasmic reticulum (neutral alpha-glucosidase), mitochondria (malate dehydrogenase), lysosomes (N-acetyl-beta-glucosaminidase), peroxisomes (catalase). gamma-Glutamyl transferase was exclusively localized to the plasma membrane. Leucine amino-peptidase, especially when assayed in the presence of Co2+, was also partially localized to the plasma membrane. Experiments with diazotized sulphanilic acid, a non-permeant enzyme inhibitor, showed that these plasma membrane enzymes are present on the cell surface. No detectable alkaline phosphatase was found in the lymphocytes. Acid phosphatase and beta-glucuronidase were localized to lysosomes and there was some evidence for lysosomal heterogeneity. Leucine amino peptidase, optimal at pH 8.0, showed a partial localization to intracellular vesicles, possibly lysosomes, especially when assayed in the presence of EDTA. These studies provide a technique for determining the intracellular distribution of hitherto unassigned lymphocyte constituents and serve as a basis for investigating the cell pathology of lymphocytic disorders.
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PMID:Enzyme analysis and subcellular fractionation of human peripheral blood lymphocytes with special reference to the localization of putative plasma membrane enzymes. 614 55

Forty-seven human leukaemia/lymphoma cell lines belonging to myelocytic, monocytic, non-T/non-B, T-, and B-lineage and representing different levels of maturation as well as fresh cells from normal and leukaemic subjects were examined for immunological markers and cytochemically for acid phosphatase, alkaline phosphatase, alpha-naphthyl acetate esterase (pH 5.8 and 8.0), alpha-naphthyl butyrate esterase (pH 5.8 and 8.0), non-specific esterase, chloroacetate esterase, chymotrypsin-like protease, deoxyribonuclease II, beta-glucuronidase, sudan black, and periodic acid Schiff's staining. Strong sudan black, nonspecific esterase, and chloroacetate esterase reaction was obtained only for myelocytic and monocytic cell lines with the reaction intensity increasing progressively in more mature cells. Focal acid phosphatase reaction like T-ALL was found in all T-ALL cell lines, whereas myeloid/monocytoid lines had semicircular distribution and B-cell lines cytoplasmic distribution of activity. Acid phosphatase activity appeared to decline with maturation along both myeloid and T-cell lineage. High activity of alpha-naphthyl acetate esterase and alpha-naphthyl butyrate esterase both at pH 5.8 and 8.0 and of beta-glucuronidase was found in myeloid/monocytoid lines although both B- and T-cell lines in contrast to peripheral blood B-cells also had significant esterase activity. alpha-Naphthyl butyrate esterase activity declined with increasing cell maturation along myeloid lineage. Except for weak activity in two B-cell lines alkaline phosphatase was not detected in any cell lines. Monocyte esterase activity was inhibited by sodium fluoride whereas acid phosphatase, only from hairy cell leukaemia line, was resistant to L-tartarate. Although periodic acid Schiff's staining could not distinguish myeloid, T-, B-, or non-T/non-B cell lines it gave characteristic reaction (large number of coarse granules against a clear background forming a ring around the nucleus) with erythroblastic leukaemia cell line and along myeloid series its intensity increased in more mature cells. Deoxyribonuclease II and chymotrypsin-like protease staining were not discriminatory. The results of this study show that cytochemical staining characteristics of various leukaemia/lymphoma cell lines are comparable to those of corresponding cells from patients and that the intensity and pattern of expression of these activities are related to cell type and degree of cell maturation. These studies give further credence to the use of these cell lines in cell differentiation, differential drug cytotoxicity, and many other studies.
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PMID:Cytochemical comparison of immunologically characterized human leukaemia/lymphoma cell lines representing different levels of maturation. 619 Apr 91

The enzymatic changes in tertiary nasal syphilis were studied in 5 patients. The cholinesterase was increased in the subepithelium, around the glands and blood vessels, denoting parasympathetic hyperactivity. Acid phosphatase was increased in the epithelium, stromal histiocytes, around the glands and ducts, indicating increased phagocytotic activity. Alkaline phosphatase was increased in the capillary endothelium and periglandular stroma, denoting marked vascular changes. Succinic dehydrogenase, alkaline phosphatase, alpha esterase and PAS-alcian blue were diminished in the epithelium and glands, denoting diminished secretory activity, hence a diminished natural defence mechanism of the nasal mucosa. When serological tests are inconclusive, these findings become an important adjuvant to a final diagnosis.
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PMID:The human respiratory nasal mucosa in nasal syphilis. A histochemical study. 623 4

The distribution and activities of phosphatases and oxidative enzymes have been determined with the help of histochemical methods in the kidney of the Prussian Carp, a stenohaline freshwater-fish. In addition to fish maintained in freshwater aquaria, a group of the animals used has been adapted to seawater of moderate salinity. The following pattern of enzyme reaction intensities has been observed in the various kidney structures: Strong reactions of alkaline phosphatase in the nephron are confined to the glomerular capillary convolute and the brush border of proximal segments. Equally enzyme activities are observed in the connective tissue sheath of the collecting duct -- archinephric duct system. Acid phosphatase can be detected in all segments of the nephronic tubule, strong activities are found in the proximal segment (P I), in the epithelium of the archinephric duct, and, especially, in the interstitial tissue. ATPase reacts strongly positive in epithelial cells of the distal tubule and the collecting duct -- archinephric duct system. ATPase reactions are inhibited by Ouabain, and therefore can be regarded as reactions of Na--K-ATPase. Mitochondrially bound oxidative enzymes, connected with the citric acid cycle and the respiratory chain, show very strong reaction intensities in the distal tubule and the collecting duct- archinephric duct system, while the glomeruli generally exhibit negative reactions. Lactate -- and malate dehydrogenases are found to react weakly to negatively throughout the whole kidney. Maintenance in seawater does not deeply affect the enzyme pattern of the kidney of the Prussian carp, with exception of some oxidative enzymes, reacting weaker in the distal tubule and the collecting duct-archinephric duct system. In addition, the epithelial cells of the archinephric duct of seawater adapted fish show a marked apical localization of reaction products for these enzymes. Possible relations between enzyme histochemistry and fish kidney physiology are discussed, in connection with comparative aspects of the enzyme histochemistry of the vertebrate kidney. A short review of normal histology and function of the kidney of the Prussian carp is added.
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PMID:[Phosphatases and oxidative enzymes in the kidney of the Prussian carp (Carassius auratus gibelio Bloch) adapted to salt water]. 625 47

Localization of phosphatases in the parathyroid of laying hens was examined by electron microscopy. Activities of both alkaline phosphatase and adenosine triphosphatase were intensive on the apposed plasma membranes between contiguous chief cells, but weak or almost lacking on those facing the interstitial connective tissue, and this finding differed from previous data in mammals. This difference seemed to be associated with the fact that in the parenchymal cells of the hens there was found a narrow, delicate filament-rich zone in the peripheral cytoplasm along the basal lamina. Activities of both thiamine pyrophosphatase and inosine diphosphatase were seen in most of the Golgi cisternae having serpentine tubular profiles, and this indicated that the latter cisterna belong to the Golgi apparatus. Acid phosphatase activities were mainly demonstrated in lysosomal dense bodies, including autophagic vacuoles, as well as in most of the lipofuscin granules, and only occasionally encountered in the Golgi apparatus, including the thick membranous cisternae, in contrast with findings in mammals. The reason for this weak activity in this organelle was discussed in relation to calcium metabolism, secretory products, and lysosomes in the laying hen.
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PMID:Electron microscopic studies on localization of phosphatases in the laying hen parathyroid. 626 87

The effect of X-ray irradiation on the process of primary mineralization in bone was studied by biochemical and ultrastructural methods. A single dose of 1500R was administered to the head region of rats. The animals were examined immediately after irradiation and 1, 2 and 3 weeks later. Fractions of isolated cells and extracellular matrix vesicles were prepared from the maxillary alveolar bone of irradiated and untreated rats by collagenase digestion and differential centrifugation. The protein content and activities of vesicular phosphatases were determined in both fractions. A continuous decrease in the activity of alkaline phosphatase could be observed in both cell and matrix vesicle fractions during a three-week follow up after irradiation. Acid phosphatase activity decreased only in the vesicle fraction. Transmission electron microscopy of irradiated bone tissue revealed that many matrix vesicles were devoid of intact membranes and apatite crystals. Calcifying nodules were abundant in the matrix without their apparent fusion into larger mineralized structures. It is suggested that irradiation interferes with enzymatic processes associated with primary mineralization.
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PMID:Effect of X-ray irradiation on primary mineralization in rat alveolar bone. 629 95

The cytochemical localisation of five hydrolytic enzymes has been studied in the brain capillaries of laboratory animals. Acid phosphatase is present in primary lysosomes of endothelial cells; alkaline phosphatase activity is seen mainly on the plasma membrane of the luminal side but also in the basal lamina. The latter is also active concerning 5'nucleotidase. Butyrylcholinesterase is an enzyme synthesized by most brain capillary endothelial cells, as can be seen by intensive staining of endoplasmic reticulum cisternae. In contrast acetylcholinesterase activity at the capillaries presumably is of neuronal origin. Local neurons appear to secrete this enzyme, which then reaches the endothelial basal lamina via the extracellular spaces. From these cytochemical observations it is concluded that pinocytotic traffic in brain endothelial cells is predominantly from the brain tissue side to the luminal side.
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PMID:Enzyme cytochemistry of the cerebral microvessel wall. 630 81


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