Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Suckling rats were exposed for 15 and 30 days to manganese through the milk of nursing dams receiving 15 mg MnCl2--4H2O/kg/day orally and after which the neurological manifestations of metal poisoning were studied. No significant differences in the growth rate, developmental landmarks and walking movements were observed between the control and manganese-exposed pups. The metal concentration was significantly increased in the brain of manganese-fed pups at 15 days and exhibited a further three-fold increase over the control, at 30 days. The accumulation of the metal in the brain of manganese-exposed nursing dams was comparatively much less. A significant decrease in succinic dehydrogenase, adenosine triphosphatase, adenosine triphosphatase, adenosine deaminase, acetylcholine esterase and an increase in monoamine oxidase activity was observed in the brain of experimental pups and dams. The results suggest that the developing brain may also be susceptible to manganese.
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PMID:Effect of manganese on neonatal rat: manganese concentration and enzymatic alterations in brain. 14 Nov 94

Activity of specific mitochondrial enzymes was studied in rat liver during 2-acetylamine fluorene or diethylnitrosamine-induced hepatocancerogenesis. The results of enzymatic activities studied correlated with morphological changes in cancerogenesis. Alterations in activity of monoamine oxidase, adenylate cyclase and adenosine triphosphatase depended on the step of cancerogenesis. Activity of adenylate cyclase in cell membranes decreased gradually during the impairment. Change in activity of the enzymes, observed at the step of enhanced liver cell proliferation, proceeded at further steps of cancerogenesis. The data obtained suggest that alterations in activity of mitochondrial enzymes are related to modified metabolism observed in the impaired cells.
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PMID:[Changes in the activity of monoamine oxidase, adenylate cyclase and adenosine triphosphatase in liver cells during the process of hepatocarcinogenesis]. 15 Jul

In this study, enzyme activities of the pancreatic appendages of the ductus hepatoPancreas (the so-called "pancreas") in Sepia officinalis L. have been demonstrated by light and electron micicroscopical methods: Malate dehydrogenase, monoamine oxidase, acid phosphatase, beta-glucuronidase, adenosine triphosphatase and carbonic anhydrase were shown by the former, and monoamine oxidase, catalase, glutamic oxalacetic transaminase, choline esterase (non-specific), alkaline phosphatase, acid phosphatase and carbonic anhydrase by the latter technique. The correlation between enzyme activity and distribution, and the presumed function of the two pancreatic epithelia is discussed.
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PMID:The localization of enzyme activities in the pancreatic appendages of Sepia officinalis L. (Cephalopoda). 15 95

The dermal cells in grey, xanthic, and white goldfish integuments were cytochemically characterized for the following enzymatic activities: tyrosinase, DOPA-oxidase, cytochrome oxidase, monoamine oxidase, peroxidase, non-specific esterase, cholinesterase, NAD-diaphorase, NADP-diaphorase, aryl sulfatase, nucleotide phosphodiesterase, beta-glucuronidase, acid phosphatase, alkaline phosphatase, adenosine triphosphatase, thiamine pyrophosphatase, glucose-6-phosphatase, aldolase, as well as succinate, malate, isocitrate, glutamate, glucose-6-phosphate, 6-phosphogluconate, alpha-glycerophosphate, alcohol, lactate, and beta-hydroxybutyrate dehydrogenases. It was found that the epidermis was a significant barrier to the access of cytochemical reaction substrates. Removal of the epidermal barrier provided dermal cell localizations of enzymatic activities which were reproducible. Further, alterations in reaction times and temperatures from the mammalian methodology provided conditions fe various integumental cells were compared for possible interrelationships. The basic foundations for future work with the dermis of poikilothermic vertebrates on an experimental basis were established. In addition, a previously undescribed non-pigmented dermal cell, the "x"-cell, was found to have enzymatic characteristics similar to both melanophores and lipophores. The "x"-cell may be the common precursor of both types of pigment cells.
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PMID:Cytochemical characterization of goldfish (Carassius auratus L.) dermis with special reference to the pigment cells. 82 86

In vitro alterations induced by a 10 micrograms/ml and 50 micrograms/ml dose each of thiophenate and fenbendazole on the absorptive surfaces of Haemonchus contortus (Nematoda: Trichostrongylidae) were studied. The most significant changes were induced in the gut epithelium. Alkaline phosphatase and adenosine triphosphatase activities were decreased, succinic dehydrogenase activity was increased, while acid phosphatase and glucose-6-phosphatase were completely lost from the intestinal epithelium after treatment with either of the drugs. A stimulatory effect of these two anthelmintics was observe on lactic dehydrogenase and reduced nicotinamide adenine dinucleotide diaphorase distribution. Thiophenate caused an increase in the activities of glutamate dehydrogenase (GDH), glucose-6-phosphate dehydrogenase (G-6-PD) and nonspecific esterases and a decrease in reduced nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-D) activity. Fenbendazole treatment led to the inhibition of GDH, while G-6-PD, NADPH-D, cytochrome oxidase, monoamine oxidase and nonspecific esterase activity remained unaltered in the epithelium.
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PMID:Histoenzymic effects of thiophenate and fenbendazole on the absorptive surfaces of Haemonchus contortus. 133 82

Histochemical activities of several enzymes were investigated in the olfactory epithelium (OE) and vomeronasal organ (VNO) of the golden hamster. Activities of adenosine triphosphatase, lactate dehydrogenase and succinate dehydrogenase were intense in the OE, and the sensory (VSE) and respiratory epithelium (VRE) of the VNO. The activity of acid phosphatase was intense in both the OE and the VSE, while that of non-specific esterase was intense in the VSE alone. The activity of alkaline phosphatase was detectable only in the VRE. Activities of monoamine oxidase and acetylcholine esterase were negative in all of the OE, VSE and VRE. These similarities and differences in the histochemical distribution of enzymes between OE and VSE may reflect the common olfactory function and/or functional specialization in these epithelia. On the other hand, the VRE was considerably different from the OE and VSE in the enzymatic distribution. This may reflect the non-olfactory function of this epithelium.
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PMID:Enzyme histochemistry of the olfactory and vomeronasal sensory epithelia in the golden hamster. 142 May 49

Haemonchus contortus, incubated in 10 micrograms/ml and 50 micrograms/ml concentrations of Nilzan and albendazole in Tyrode solution were stained for histoenzymatic demonstration of various phosphatases, oxido-reductases and esterases. The intestine showed major alterations after drug treatments. The alkaline phosphatases (AkPase), adenosine triphosphatase (ATPase), glucose-6-phosphatase, succinic dehydrogenase (SDH), glutamate dehydrogenase (GDH), reduced nicotinamide adenine dinucleotide phosphate diaphorase and reduced nicotinamide adenine dinucleotide diaphorase showed a decreased activity in intestine after Nilzan treatment, whereas lactic dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G-6-PD) and monoamine oxidase resisted increased reaction. The albendazole treatment resulted in altered distribution pattern of the AkPase, ATPase, SDH, and GDH; while LDH, G-6-PD, and non-specific esterases exhibited slightly enhanced activity in the epithelium. The functional significance of these changes has been fully discussed.
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PMID:Effect of Nilzan and albendazole on the absorptive surfaces of Haemonchus contortus (Nematoda)--a histoenzymic study. 196 79

The anticonvulsant drug, phenytoin, has been reported to inhibit both the transport of catecholamines into synaptosomes and monoamine oxidase. The objective of this research was to determine whether phenytoin inhibited the transport of catecholamines into storage granules. This was tested by examining the effects of phenytoin (0.05 to 0.4 mM) on the ability of (-)-[3H] norepinephrine to be transported into chromaffin granule "ghosts" isolated from bovine adrenal glands. Our results indicated that phenytoin, but not phenobarbital, inhibited catecholamine transport in a dose-dependent manner with 50% inhibition occurring at a phenytoin concentration of 0.2 mM. Kinetic analysis of the effects of phenytoin on this transport process indicated that phenytoin was a competitive inhibitor of catecholamine transport with an approximate Ki of 0.3 mM. Furthermore, phenytoin did not inhibit the Mg adenosine triphosphatase required for providing the energy source for the catecholamine transport process, nor did it dissipate the membrane potential generated by this enzyme. The competitive inhibition of catecholamine transport produced by phenytoin is probably not related to the anticonvulsant effects of the drug as it occurred at greater than therapeutic concentrations. However, this effect may be related to the toxic effect of the drug.
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PMID:Inhibition of catecholamine transport into chromaffin granule ghosts isolated from bovine adrenal glands by phenytoin. 614 5

Toxicological studies of a leachable stabilizer Di-n-butyltin dilaurate (DBTL) were undertaken. Effects of DBTL after 15 days oral exposure to rats were studied on brain and liver enzyme activities. A significant decrease in body weight gain of DBTL exposed rats were observed. No effect was observed in the activities of brain enzymes, succinic dehydrogenase, adenosine triphosphatase, acetylcholine esterase and monoamine oxidase. In liver, DBTL treatment resulted in a significant decrease in the activities of microsomal enzymes glucose-6-phosphatase, aminopyrine-N-demethylase, benzphetamine-N-demethylase, aniline hydroxylase, benzo(a)pyrene hydroxylase and also on cytochrome P-450 content, whereas no difference in the activities of mitochondrial enzymes, succinic dehydrogenase, Mg2+-adenosine triphosphatase as well as in the activity of lysosomal enzyme acid phosphatase was observed. Duration of exposure dependent increase in pentabarbital induced sleeping time was also observed. DBTL treatment produced an induction in heme oxygenase activity whereas the activity of -aminolevulinic acid synthetase remained unaltered. The results demonstrate that DBTL significantly affects the biotransformation mechanism and heme metabolism of hepatocytes.
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PMID:Toxicological studies of a leachable stabilizer di-n-butyltin dilaurate(DBTL): effects on hepatic drug metabolizing enzyme activities. 726 48

Isatin (10 microM) strongly inhibited the activity of rat brain monoamine oxidase-B (MAO-B) in vitro. At millimolar concentrations (1-10 mM) it inhibited brain acetylcholinesterase (AChE) and sodium, potassium-adenosine triphosphatase (Na+, K(+)-ATPase) activity also. However, isatin did not affect these enzymes after both acute and chronic treatments in vivo. Administration of isatin to rats at 300 mg/kg body weight for 2 and 6 h significantly raised brain serotonin levels. Chronic treatment for 20 days resulted in enhanced brain glycolipids and plasmalogen levels. There was no change in the levels of 5-hydroxy indole acetic acid (5 HIAA), phospholipids, cholesterol and gangliosides under these conditions.
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PMID:In vivo effects of isatin on certain enzymes, lipids & serotonergic system of rat brain. 782 61


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