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)

The early effects of lithium on the kidney were studied in rats receiving a moderate daily dose (serum-Li: 0.5 to 0.8 mM per liter) for 3, 7, and 21 days. Enzyme histochemical reactions for acid and alkaline phosphatase, glucose 6-phosphatase, succinate and alpha-glycerophosphate dehydrogenase, and NADH tetrazolium reductase revealed changes confined to distal convoluted tubules and collecting ducts. The distal convoluted were unchanged at 3 days of treatment. At 7 days, a decrease in succinate dehydrogenase and NADH tetrazolium reductase and an increase in alpha-glycerophosphate dehydrogenase were noted. These changes were more conspicuous at 21 days and accompanied by tubular dilation and changes in light microscopic cellular morphology. In the collecting ducts, a cell enlargement and an increase in mitochondrial oxidative enzyme activities began to appear at 3 days, becoming more pronounced at 7 and particularly at 21 days. At 7 and even more at 21 days, a cellular hyperplasia was evident in the collecting ducts, and autoradiography after 3H-thymidine incorporation showed a marked increase in DNA synthesis in the collecting duct cells. The changes observed in the collecting ducts were most pronounced near the limit between the outer and the inner zone of the medulla. In conclusion, the rats developed morphologic changes at 3 to 7 days of treatment. The changes include (1) signs of cellular damage in the distal convoluted tubules and (2) hyperplasia and signs of increased functional activity in the collecting ducts.
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PMID:Early changes in renal distal convoluted tubules and collecting ducts of lithium-treated rats: light microscopy, enzyme histochemistry, and 3H-thymidine autoradiography. 706 26

Preparations enriched with plasmalemmal, outer mitochondrial, or Golgi complex membranes from rat liver were subfractionated by isopycnic centrifugation, without or after treatment with digitonin, to establish the subcellular distribution of a variety of enzymes. The typical plasmalemmal enzymes 5'-nucleotidase, alkaline phosphodiesterase I, and alkaline phosphatase were markedly shifted by digitonin toward higher densities in all three preparations. Three glycosyltransferases, highly purified in the Golgi fraction, were moderately shifted by digitonin in both this Golgi complex preparation and the microsomal fraction. The outer mitochondrial membrane marker, monoamine oxidase, was not affected by digitonin in the outer mitochondrial membrane marker, monoamine oxidase, was not affected by digitonin in the out mitochondrial membrane preparation, in agreement wit its behavior in microsomes. With the exception of NADH cytochrome c reductase (which was concentrated in the outer mitochondrial membrane preparation), typical microsomal enzymes (glucose-6-phosphatase, esterase, and NADPH cytochrome c reductase) displayed low specific activities in the three preparations; except for part of the glucose-6-phosphatase activity in the plasma membrane preparation, their density distributions were insensitive to digitonin, as they were in microsomes. The influence of digitonin on equilibrium densities was correlated with its morphological effects. Digitonin induced pseudofenestrations in plasma membranes. In Golgi and outer mitochondrial membrane preparations, a few similarly altered membranes were detected in subfractions enriched with 5'-nucleotidase and alkaline phosphodiesterase I. The alterations of Golgi membranes were less obvious and seemingly restricted to some elements in the Golgi preparation. No morphological modification was detected in digitonin-treated outer mitochondrial membranes. These results indicate that each enzyme is associated with the same membrane entity in all membrane preparations and support the view that there is little overlap in the enzymatic equipment of the various types of cytomembranes.
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PMID:Analytical study of microsomes and isolated subcellular membranes from rat liver VIII. Subfractionation of preparations enriched with plasma membranes, outer mitochondrial membranes, or Golgi complex membranes. 725 62

The distribution and intensity of alkaline phosphatase deposition in 54 patients with dermatomyositis-polymyositis (PM-DM) was analyzed by the enzyme histochemical method. Increased enzyme reactivity of endomysial capillaries was found in 28% of patients, equally distributed between adult onset PM (Group I) and PM-DM with overlap in other connective tissue diseases (Group V). Patients with high endomysial capillary reactivity (R1 larger than or equal to 60) responded poorly to steroids, had an increased incidence of rheumatoid factor, and had less fiber degeneration/necrosis in their biopsies. Twenty-two percent of patients demonstrated prominent perimysial phosphatase reactivity localized in newly formed collagen and fibroblasts. Thirty patients (55%) demonstrated significant numbers of alkaline-phosphatase-positive fibers positively correlated with increased fiber degeneration/necrosis, endomysial fibrosis, increased numbers of triglyceride-containing muscle fibers, and NADH tetrazolium reductase hyperreactivity. Minimal overlap between the three enzyme distribution patterns was found. Endomysial capillary activity probably represents endothelial alkaline phosphatase induction analogous to the pattern seen normally in lower mammals (rat, rabbit, guinea pig). Alkaline phosphatase fiber reactivity probably represents a particular phase in fiber regeneration/maturation especially after denervation and is positively correlated with an increased incidence of spontaneous fibrillation potentials in PM-DM.
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PMID:Polymyositis-dermatomyositis: diagnostic and prognostic significance of muscle alkaline phosphatase. 744 98

The NADPH-diaphorase (NADPH-d) reaction is frequently used to visualize the diaphorase activity of nitric oxide synthase (NOS). However, this tetrazolium salt procedure can be of limited specificity at sites where non-specific alkaline phosphatase (alP) and NADHd activity co-exist. This is shown in the present paper using methods of catalytic histochemistry for these three enzymes and levamisole as alP inhibitor for certain mouse tissues. In the urothelium, portio, vaginal and endometrial epithelium as well as in some smooth muscle cells alP hydrolyzes NADPH to NADH which in turn serves as substrate for NADHd leading to false-positive formazan production. To exclude this possibility, it is recommended always to include levamisole in the incubation medium if the NADPHd activity of NOS has to be investigated.
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PMID:Nonspecific alkaline phosphatase activity can be responsible for staining of NADPH-diaphorase activity in certain non-neural cells. 755 70

The L/B/K type of mammalian alkaline phosphatase (ALP) is inhibited uncompetitively by nucleotides. A combination of adenosine and nicotinamide is more effective than either adenosine or nicotinamide alone, probably because a dinucleotide structure is necessary to trigger a conformational change accompanying binding of structures such as NADH. It has been suggested that a loop region containing residue 429 in the ALP polypeptide is important in the interaction of uncompetitive inhibitors with the enzyme. In the L/B/K isoenzyme, residue 429 is a histidine and is a potential target for modification. In an attempt to learn more about the molecular events accompanying inhibition of ALP by uncompetitive inhibitors, bovine kidney ALP was reacted with oxidized adenosine in the presence of nicotinamide to see if site-directed modification occurs. Kidney ALP was irreversibly inactivated by oxidized adenosine but the reaction was slow. The site modified is likely to be close to the region of binding. Sequence data for the kidney enzyme shows that in the region of residue 429 there are no residues except His429 itself that is likely to react with oxidized adenosine.
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PMID:Time-dependent irreversible inhibition of bovine kidney alkaline phosphatase by oxidized adenosine. Use of this compound as a site-directed inhibitor for studying uncompetitive inhibition. 783 15

Inhibitors of mammalian cytochrome P450 and P450 reductase were used to investigate the enzymes in flounder (Platichthys flesus) hepatic microsomes involved in the stimulation of NAD(P)H-dependent iron/EDTA-mediated 2-keto-4-methiolbutyric acid (KMBA) oxidation (hydroxyl radical production) by the redox cycling compounds menadione and nitrofurantoin. Inhibitors were first tested for their effects on flounder microsomal P450 and flavoprotein reductase activities. Ellipticine gave type II difference binding spectra (app. Ks 5.36 microM; delta A max 0.16 nmol-1 P450) and markedly inhibited NADPH-cytochrome c reductase, NADPH-cytochrome P450 reductase, and monooxygenase (benzo[a]pyrene metabolism) activities. 3-aminopyridine adenine dinucleotide phosphate (AADP; competitive inhibitor of P450 reductase) inhibited NADPH-cytochrome c but not NADH-cytochrome c or NADH-ferricyanide reductase activities. Alkaline phosphatase (inhibitor of rabbit P450 reductase) stimulated NADPH-cytochrome c reductase activity seven fold but had less effect on NADH-reductase activities. AADP inhibited nitrofurantoin- and menadione-stimulated KMBA oxidation by 45 and 17%, respectively, indicating the involvement of P450 reductase at least in the former. In contrast, ellipticine had relatively little effect, possibly because, unlike cytochrome c, the smaller xenobiotic molecules can access the hydrophilic binding site of P450 reductase. Alkaline phosphatase stimulated NAD(P)H-dependent basal and xenobiotic-stimulated KMBA oxidation, showing general consistency with the results for reductase activities. Overall, the studies indicate both similarities (ellipticine, AADP) and differences (alkaline phosphatase) between the flounder and rat hepatic microsomal enzyme systems.
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PMID:Inhibition studies on the involvement of flavoprotein reductases in menadione- and nitrofurantoin-stimulated oxyradical production by hepatic microsomes of flounder (Platichthys flesus). 807 49

We describe a continuous coupled spectrophotometric assay for alkaline phosphatase which uses alpha- or beta-glycerophosphate as substrate, and glycerol dehydrogenase as ancillary enzyme. The glycerol liberated by alkaline phosphatase is determined by measuring the increase in absorbance at 340 nm caused by NADH formation that is combined with glycerol oxidation by the ancillary enzyme. The assay procedure was optimized using a bovine bone extract as alkaline phosphatase source.
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PMID:A continuous spectrophotometric assay for alkaline phosphatase with glycerophosphate as substrate. 815 Oct 68

A new micromethod for the determination of sphingomyelin in samples suspended in aqueous solutions, and modified micromethods for determining phosphatidylcholine and phosphatidylglycerol were used to determine phosphatidylcholine and sphingomyelin (detection limits of 1.8 mumol/l), and phosphatidylglycerol (detection limit of 2.3 mumol/l) in lipid dispersions, membranes from sheep erythrocytes and platelets, and pulmonary surfactants from rats of different ages and rats maintained under normobaric hyperoxia for 2 days prior to their sacrifice. The procedures are easy to perform, accurate, require less sample than conventional methods and can also be applied directly to aqueous samples. Phospholipase C and sphingomyelinase were used to release phosphorylcholine from phosphatidylglycerol and sphingomyelin, respectively. The choline released from phosphorylcholine by alkaline phosphatase is reconverted to phosphorylcholine by ATP and choline kinase. In the phophatidylglycerol determination, phospholipase D was used to release glycerol and phosphatidate. The glycerol formed was converted to glycerolphosphate using ATP and glycerol kinase. In all cases, the ADP thus formed was determined by following the enzymatic conversion of NADH to NAD at 340 nm in an coupled pyruvate kinase/lactate dehydrogenase system. Significant variations in the phospholipid composition of rat pulmonary surfactant were found during development; in particular there was an increase in the phosphatidylglycerol content of adult rats as compared with younger rats. Hyperoxia produced changes in the phosphatidylglycerol content of surfactant from adult rats, but not from 2-day old rats.
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PMID:Enzymatic determination of phosphatidylcholine, sphingomyelin and phosphatidylglycerol in lipid dispersions, blood cell membranes and rat pulmonary surfactant. 870 43

The rnf genes in Rhodobacter capsulatus are unique nitrogen fixation genes that encode potential membrane proteins (RnfA, RnfD, and RnfE) and potential iron-sulfur proteins (RnfB and RnfC). In this study, we first analyzed the localization and topology of the RnfA, RnfB, and RnfC proteins. By activity and immunoblot analysis of expression of translational fusions to Escherichia coli alkaline phosphatase, RnfA protein was shown to span the chromatophore membrane with its odd-numbered hydrophilic regions exposed to periplasm. By alkaline treatment of membrane fractions and following immunoblot analysis using antibodies against recombinant proteins expressed in E. coli, both RnfB and RnfC proteins were revealed to situate at the periphery of the chromatophore membranes. Second, mutual interaction of the Rnf proteins was analyzed by immunochemical determinations of RnfB and RnfC proteins in rnf mutants and their complemented derivatives. The contents in cellular fractions indicated that RnfB and RnfC stabilize each other and that the presence of RnfA is necessary for stable existence of both proteins. These results support a hypothesis that the Rnf products are subunits of a membrane complex. Finally, we detected homologs of rnf genes in Haemophilus influenzae and Vibrio alginolyticus by data base searches and in E. coli by cloning of a fragment of an rnfA homolog followed by a data base search. Close comparisons revealed that RnfC has potential binding sites for NADH and FMN which are similar to those found in proton-translocating NADH:quinone oxidoreductases and that RnfA, RnfD, and RnfE show similarity to subunits of sodium-translocating NADH:quinone oxidoreductases. We predict that the putative Rnf complex represents a novel family of energy-coupling NADH oxidoreductases.
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PMID:Membrane localization, topology, and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energy-coupling NADH oxidoreductases. 915 34

Previous work has shown that reduction-of-function mutations in the genes daf-2 and age-1 can increase adult life (Age phenotype) of Caenorhabditis elegans and that certain daf-12 alleles considerably amplify this effect in daf-2; daf-12 doubles. We have measured the light production potential (LPP) and alkaline phosphatase (ALP) and protein tyrosine kinase (PTK) activity levels as suitable biochemical markers to further investigate genetic interactions between these genes. The light production assay measures superoxide anion production by freeze-thawed worms in assay medium containing sufficient amounts of nicotineamide adenine dinucleotide, reduced form (NADH) and nicotineamide adenine dinucleotide phosphate, reduced form (NADPH) to drive the chemiluminescent reaction at maximal speed, and 5 mM cyanide to fully repress cytosolic superoxide dismutase (SOD). This assay thus provides an estimate of the maximum output of the metabolic pathways involved at the instant of freeze-fixation, and under the condition of the assay. LPP and PTK activities decreased similarly in daf-12(m20), and a control strain that had wild-type alleles of daf-12, age-1, and daf-2. The age-dependent decrease of LPP and PTK was reduced in age-1(hx542) and age-1(hx542); daf-2(e1370), and virtually absent in daf-2(e1370) and daf-2(e1370); daf-12(m20) mutant worms. ALP activity increased with age in non-Age genotypes and showed little, if any, age-dependent alteration in daf-2(e1370) and daf-2(e1370); daf-12(m20) mutant worms. Mutation in both age-1 and daf-2 caused no stronger phenotype than a single mutation as estimated by LPP, PTK, and ALP. We propose that (a) daf-2 is the major effector of metabolic activity during adult life, (b) daf-2 downregulates metabolic activity with increasing age, and (c) daf-12 stimulates oxygen consumption independently of daf-2.
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PMID:Age-specific modulation of light production potential, and alkaline phosphatase and protein tyrosine kinase activities in various age mutants of Caenorhabditis elegans. 975 36


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