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cystic fibrosis/phosphatase
Veza se sprema u međuspremnik
Page 1 od 274 rezultati
Protocol for prenatal diagnosis of cystic fibrosis based on studies of alkaline phosphatase isoenzymes.
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Amniotic fluid analysis of microvillar enzymes, including alkaline phosphatase (ALP) total activity and ALP isoenzymes, has been widely experimented with and used for the prenatal diagnosis of cystic fibrosis in the second trimester of gestation. Since the development of cystic fibrosis molecular
Prenatal diagnosis of cystic fibrosis using a monoclonal antibody specific for intestinal alkaline phosphatase.
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A monoclonal antibody (AAP-1), specific for the intestinal isoenzyme of alkaline phosphatase (ALP), has been used to develop an immunoassay for amniotic fluid samples. Values in the immunoassay correlated closely with those obtained by direct determination of phenylalanine-inhibitable ALP. A panel
Amniotic fluid alkaline phosphatase isoenzymes in early prenatal diagnosis of cystic fibrosis.
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Second-trimester amniotic fluid contains two major alkaline phosphatase (ALP) isoenzymes, one susceptible to inhibition by phenylalanine and the other to inhibition by homoarginine. The proportions of these isoenzymes are constant between 15 and 21 weeks of gestation. In pregnancies where the fetus
Isoenzymes of alkaline phosphatase in amniotic fluid: implications in prenatal screening for cystic fibrosis.
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Utilizing their differential susceptibilities to inhibitors and heat, we determined the amounts of the placental, liver, and fetal-intestinal isoenzyme forms of alkaline phosphatase in 143 samples of normal amniotic fluid obtained at 14 to 18 weeks' gestation (1). For reliable results, it was
Induction of alkaline phosphatase in cultured human fibroblasts. Comparison of normal cells and those from patients with cystic fibrosis.
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The membrane glycoprotein enzyme, alkaline phosphatase was induced in cultured human fibroblasts by dibutyryl cyclic AMP, sodium butyrate, the serum glycoprotein fetuin, the Tamm-Horsfall urinary glycoprotein, and by a number of inhibitors of DNA synthesis. The uninduced basal enzyme activity
Effect of IBMX and alkaline phosphatase inhibitors on Cl- secretion in G551D cystic fibrosis mutant mice.
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Some cystic fibrosis transmembrane conductance regulator (CFTR) mutations, such as G551D, result in a correctly localized Cl- channel at the cell apical membrane, albeit with markedly reduced function. Patch-clamp studies have indicated that both phosphatase inhibitors and
Protein phosphatase 2C dephosphorylates and inactivates cystic fibrosis transmembrane conductance regulator.
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cAMP-dependent phosphorylation activates the cystic fibrosis transmembrane conductance regulator (CFTR) in epithelia. However, the protein phosphatase (PP) that dephosphorylates and inactivates CFTR in airway and intestinal epithelia, two major sites of disease, is not certain. We found that in
Studies in meconium in cystic fibrosis: the activities of alpha-D-mannosidase, beta-glucuronidase, beta-D-fucosidase, acid and alkaline phosphatase.
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The specific activities of alpha-D-mannosidase, beta-glucuronidase, beta-D-fucosidase, acid and alkaline phosphatase were studied in meconium from infants with cystic fibrosis (CF) and control subjects. The study revealed significant variations in the specific activity of the enzymes except for acid
Association of cystic fibrosis transmembrane conductance regulator and protein phosphatase 2C.
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Cystic fibrosis transmembrane conductance regulator (CFTR) chloride channels are rapidly deactivated by a membrane-bound phosphatase activity. The efficiency of this regulation suggests CFTR and protein phosphatases may be associated within a regulatory complex. In this paper we test that
Alkaline phosphatase activity of normal and cystic fibrosis fibroblasts.
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Alkaline phosphatase (ALP) activities were compared in fibroblasts from three cystic fibrosis patients and two normal controls after culturing the cells in normal growth medium and in medium containing Tamm-Horsfall glycoprotein, isoproterenol, and theophylline. No consistent alterations in ALP
Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by specific protein kinases and protein phosphatases.
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Cystic fibrosis transmembrane conductance regulator (CFTR) is a regulated Cl- channel; in secretory epithelia, it is located in the apical membrane where it regulates transepithelial Cl- secretion. Previous studies have shown that cAMP-dependent protein kinase (PKA) can phosphorylate and activate
High-molecular-mass ("biliary") isoenzyme of alkaline phosphatase and the diagnosis of liver dysfunction in cystic fibrosis.
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The high-Mr isoenzyme of alkaline phosphatase (AP, EC 3.1.3.1), a highly sensitive index to cholestasis, was measured by liquid chromatography in 45 patients with cystic fibrosis. Results of serum tests for liver dysfunction--including gamma-glutamyltransferase, aspartate aminotransferase, alanine
Interaction of the protein phosphatase 2A with the regulatory domain of the cystic fibrosis transmembrane conductance regulator channel.
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A direct interaction of the regulatory domain (R domain) of the cystic fibrosis transmembrane conductance regulator protein (CFTR) with PR65, a regulatory subunit of the protein phosphatase 2A (PP2A), was shown in yeast two hybrid, pull-down and co-immunoprecipitation experiments. The R domain could
Prenatal detection of intestinal obstructions, aneuploidy syndromes, and cystic fibrosis by microvillar enzyme assays (disaccharidases, alkaline phosphatase, and glutamyltransferase) in amniotic fluid.
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Microvillar enzymes (disaccharidases, alkaline phosphatase, and gamma-glutamyltransferase) were assayed in amniotic fluid from pregnancies with normal and abnormal fetuses to determine their specificity and reliability for the prenatal detection of intestinal obstructions and cystic fibrosis. All
Inhibition of Tamm-Horsfall glycoprotein induction of alkaline phosphatase in cystic fibrosis fibroblasts by medium conditioned by normal cells.
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It is confirmed that the level of alkaline phosphatase in fibroblasts derived from cystic fibrosis patients can be induced many-fold by growing the cells in the presence of Tamm-Horsfall glycoprotein. It is further shown that normal fibroblasts produce a "CF corrective factor" which markedly
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