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)

Parallel stereo- and cytospectrophotometric examinations of human myocardial capillaries, 20-60 min after biological death were carried out. The activity of alkaline phosphatase, adenosine triphosphatase, lactate dehydrogenase and NAD-diaphorase in the capillary wall in relation to the sex and age in cardiovascular pathology, renal diseases and leukemias were studied. The permeability and level of energy supply of transendothelial transport were found to depend on the kind of the main pathological process and type of death. According to the parameters under study, the functional state of the capillary network of the myocardium in atherosclerosis with or without its combination with hypertension and also in secondary renal hypertension is described.
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PMID:[Stereological characteristics and enzymatic activity of myocardial capillaries in different variants of pathology and death (data from immediate autopsies)]. 686 Jan 68

The observation that NAD inhibits sodium-dependent phosphate (P) uptake by the luminal brush border membrane (BBM) of the proximal tubule prompted us to examine the specificity and mechanism of this process. Addition of 10(-5) M NAD to the perfusate of isolated perfused rabbit proximal straight tubules inhibited lumen-to-bath P flux by approximately 50%. ADP-ribose had an identical effect, whereas nicotinamide had no effect. ADP and 5'-AMP (10(-5) M) also inhibited P flux. Na-dependent uptake of 32P by rabbit BBM vesicles was inhibited by 0.1-0.3 mM NAD, ADP-ribose, ADP, ATP, 5'-AMP, and GDP, which were preincubated with the vesicles for 30 min. The kinetics of inhibition showed an apparent increase in the Km for P but no change in Vmax. These findings are consistent with "competitive inhibition." The nucleotides inhibited P uptake even when BBM alkaline phosphatase was inhibited by 96% with 10 mM theophylline. Evidence of nonspecific phosphatase activity was present, since incubation of BBM with 0.1 mM solution of nucleotides for 30 min resulted in an elevation of free P in the medium of approximately 0.15-0.22 mM. Correction of 32P specific activity for this change resulted in values for Km and Vmax that were not significantly different from control. The "competitive inhibition" could thus be ascribed to an isotope-dilution effect. There was no evidence to suggest that NAD caused ADP-ribosylation of the luminal membrane. These studies indicate that adenine and guanine nucleotides do not inhibit P transport by a direct action on the luminal membrane of the proximal tubule but do inhibit lumen-to-bath P flux in isolated perfused proximal tubules at concentrations of 10(-5) M. Since there is no direct inhibitory effect of these compounds at the level of the BBM, it is possible that they inhibit P transport by altering some event subsequent to the transfer of P across the luminal membrane.
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PMID:Nucleotide inhibition of phosphate transport in the renal proximal tubule. 688 41

The article deals with the results of histochemical study of some redox and proteolytic enzymes (SDH, MDH, NAD-diaphorase, LDH, and acid and alkaline phosphatase) in experiments on animals in various periods after infliction of a craniocerebral injury and on autopsy material, i.e. the brain of patients who had died from severe craniocerebral injury incompatible with life. It is shown that the activity of all enzymes decreases (SDH, MDH, NAD-diaphorase, and alkaline phosphatase) or increases (LDH, acid phosphatase) in various periods after the injury. The results were compared with the findings of morphological examination of the same brain areas performed by means of neurohistological methods.
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PMID:[Redox and proteolytic enzymes in brain tissue after a concussion]. 689 60

Glycogen in the epithelium is interpreted as a sign of cell activity; its accumulation seems to take place gradually during cell migration. The oxido-reductase and hydrolytic enzyme-groups represent a sensitive indicator of changes in cell metabolism. The occurrence and intensity of glycogen, lactic and succinic dehydrogenases, NAD-cytochrome-c-reductase, alkaline and acid phosphatases were studied in 20 biopsy materials obtained from patients with keratotic buccal lesions. The results were compared with 20 biopsies from healthy oral mucosa. Variations were found in the localization and amount of glycogen, but no significant difference could be observed in the intensity of the oxido-reductase enzymes and alkaline phosphatase reactions. Acid phosphatase showed increased reactivity in most superficial layers of the keratinized epithelium.
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PMID:Keratotic lesions of the oral epithelium. 730 73

Examination of macrophages, polymorphonuclear leukocytes (PMNL) and lymphocytes of the trachea, PMNL and blood lymphocytes, of the condition of pulmonary tissue in the time course of the process (1st day--l months) revealed an association between the developing cellular and tissue changes. The development of alterations in the lungs with predominant anabolic changes and moderate exudation are characterized by a decrease in the content of nucleoproteins (deoxyribonucleoproteins, ribonucleoproteins), and activity of NAD-diaphorase and alkaline phosphatase, an increase in the activity of acid phosphatase in the above-mentioned cells of the trachea and blood as well as by increased permeability of lysosomal membranes and degeneration of macrophages, PMNL and lymphocytes of the trachea. The above cellular changes in combination with increased permeability of PMNL and blood lymphocyte lysosomal membranes correspond to the development in the lungs of catabolic alterative lesions, marked exudation, and suppurative-necrotic processes. The increase in the content of nucleoproteins and NAD-diaphorase and alkaline phosphatase activity and the decrease in the acid phosphatase activity are accompanied by activation of proliferation in the lungs.
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PMID:[Cyto-histochemical study of morphogenesis of experimental nonspecific pneumonia]. 741 96

Although used for analytical purposes for more than 40 years it is only recently that biochemiluminescence (BCL) has found widespread acceptance. Methods employing BCL reactions now play an important role in biomedical research and laboratory medicine. The main attractions for the assay technology include exquisite sensitivity (attomole-zeptomole), high selectivity, speed and simplicity. In biomedical research, the most important applications of BCL are: (1) to estimate microbial numbers and to assess cellular states (e.g., after exposure to antibiotic or cytotoxic agents) and in reporter gene studies (firefly luciferase gene); (2) NAD(P)H involved in redox/dehydrogenase studies using Vibrio luciferase complex; (3) BCL labels and CL detection of enzyme labels in immunoassays are the most widespread routine application for this technology. BCL enzyme immunoassays represent the most active area of development, e.g., enhanced BCL method for peroxidase and BCL assays for alkaline phosphatase labels using adamantyl 1,2-dioxetane.
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PMID:Biochemiluminescence and biomedical applications. 769 95

IgG antibodies against the 2,3-di-o-acyltrehalose glycolipid of Mycobacterium tuberculosis were determined in a set of 49 sera from patients with pulmonary tuberculosis and 65 negative control subjects. We compared a conventional ELISA method using a beta-galactosidase anti-human IgG conjugate developed with ONPG, with an amplification ELISA system constituted of an anti-human IgG biotinylated conjugate, a streptavidin-alkaline phosphatase complex, and NADP as a substrate. The resulting NAD was measured by using a redox enzymatic recycling system of alcohol dehydrogenase, diaphorase and iodonitrotetrazolium as chromogen. With specificity set at 92.31% in both methods, we obtained a sensitivity of 42.86% in the conventional method and a sensitivity of 61.22% in the amplified method. We conclude that by using a more sensitive method we can detect cases that otherwise could be identified as false negatives.
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PMID:Development of an enzyme-linked immunosorbent assay (ELISA) combined with a streptavidin-biotin and enzyme amplification method to detect anti-2,3-di-o-acyltrehalose (DAT) antibodies in patients with tuberculosis. 782 39

Benzamide riboside exhibits significant cytotoxicity against a variety of human tumor cells in culture. On the basis of metabolic studies, the primary target of this drug's action appears to be IMP dehydrogenase (IMPDH). Incubation of human myelogenous leukemia K562 cells with an IC50 concentration of benzamide riboside resulted in an expansion of IMP pools (5.9-fold), with a parallel reduction in the concentration of GMP (90%), GDP (63%), GTP (55%) and dGTP (40%). On kinetic grounds, it was deduced that benzamide riboside (whose Ki versus IMPDH is 6.4 mM, while that of its 5'-monophosphate is 3.9 mM) or its 5'-monophosphate were unlikely to be responsible for inhibition of this target enzyme, IMPDH, since only micromolar concentrations of benzamide riboside were needed to exert potent inhibition of tumor-cell growth. Studies on the metabolism of this C-nucleoside have revealed the presence of a new peak eluting in the nucleoside diphosphate area on HPLC. Treatment of this peak with venom phosphodiesterase degraded it and concurrently nullified its inhibitory activity versus IMPDH; alkaline phosphatase, on the other hand, totally failed to digest the anabolite. These results suggest that the metabolite in question is the phosphodiester, benzamide adenine dinucleotide (BAD). Evidence that the inhibitor was an analog of NAD, wherein the nicotinamide moiety has been replaced by benzamide, was provided by both NMR and mass spectrometric analysis and confirmed by enzymatic synthesis. Further insight into the nature of the active principle was obtained from kinetic studies, which established that BAD competitively inhibited NAD utilization by partially purified IMPDH from K562 cells with a Ki of 0.118 microM. In concert, these studies establish that benzamide riboside exhibits potent antiproliferative activity by inhibiting IMPDH through BAD.
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PMID:Cytotoxicity and characterization of an active metabolite of benzamide riboside, a novel inhibitor of IMP dehydrogenase. 790 81

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

Recently, oxidation products of linoleic acid such as 13-hydroxyoctadecadienoic acid (HODE) have been implicated in the regulation of cellular physiology including the proliferative response to growth factor treatment. In addition, an NAD(+)-dependent 13-HODE dehydrogenase was recently described. To evaluate the contribution of this enzyme to cellular processes we have examined the behavior of the enzyme under different conditions. In the present report, changes in the activity of 13-hydroxyoctadecadienoic acid dehydrogenase during in vitro differentiation of two different cell lines were examined. The cell line HT-29 undergoes induced differentiation via manipulation of the medium while the Caco-2 line undergoes spontaneous differentiation upon attainment of confluence. In both cell lines, longer culture times were accompanied by increases in 13-HODE dehydrogenase activity. The increase in enzyme activity continued even after cell proliferation had ceased. Cellular differentiation was verified by the observation of increases in sucrase and alkaline phosphatase activities. In addition, the activity of 13-HODE dehydrogenase was measured in growing, early confluent and late confluent cultures of undifferentiating Swiss mouse 3T3 fibroblasts. In the fibroblast line, no significant changes in 13-HODE dehydrogenase activity were observed during the course of the experiment. The specific activity of 13-HODE dehydrogenase was also significantly different between the three cell lines, consistent with the extent of differentiation. Highest levels of activity were found in Caco-2 cells (200-400 pmol/min/mg) and barely detectable levels in the fibroblasts (0.6-2 pmol/min/mg). The correlation between 13-HODE dehydrogenase and cell differentiation suggests the enzyme may have a role to play in the partitioning of cells between proliferation and differentiation pathways.
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PMID:Increases in 13-hydroxyoctadecadienoic acid dehydrogenase activity during differentiation of cultured cells. 824 49


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