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)

When Cladosporium resinae is provided with n-hexadecane and glucose, n-hexadecane is used preferentially. Studies using [14C]glucose indicated that n-hexadecane did not inhibit glucose uptake but did retard oxidation of glucose to CO2 and assimilation of glucose carbon into trichloroacetic acid-insoluble material. Glucose could be recovered quantitatively from hydrocarbon-grown cells that had been transferred to glucose. Four enzymes that may be involved in glucose metabolism, hexokinase, glucose-6-phosphate dehydrogenase, glucose-phosphate isomerase, and succinate dehydrogenase, were not detected in cells grown on hexadecane but were present in cells grown on glucose. Addition of hexadecane to extracts of glucose-grown cells resulted in immediate loss of activity for each of the four enzymes, but two other enzymes did not directly involved in glucose metabolism, adenosine triphosphatase and alanine-ketoacid aminotransferase, were not inhibited by hexadecane in vitro. Cells grown on hexadecane and transferred to glucose metabolize intracellular hexadecane; after 1 day, activity of hexokinase, glucose-6-phosphate dehydrogenase, glucosephosphate isomerase, and succinate dehydrogenase could be detected and 22% of the intracellular hydrocarbon had been metabolized. Hexadecane-grown cells transferred to glucose plus cycloheximide showed the same level of activity of all the four enzymes as cells transferred to glucose alone. Thus, intracellular n-hexadecane or a metabolite of hexadecane can inthesis of those enzymes is not inhibited.
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PMID:Inhibition of glucose metabolism by n-hexadecane in Cladosporium (Amorphotheca) resinae. 13 54

Ribonucleic acid was isolated from the fundic gastric mucosae of rats and rabbits by cesium chloride centrifugation of guanidine isothiocyanate-denatured mucosal homogenates, and poly A+ RNA was recovered from the pellets by oligodeoxythymidine column selection. When added to rabbit reticulocyte lysates, this poly A+ RNA stimulated [35S]methionine incorporation into trichloroacetic acid-precipitable material. Fluorographic analysis of the lysates showed protein synthesis to be dominated by polypeptides with molecular weights from 40,000 to 50,000, presumably prepepsinogen isoforms. Immune precipitation of the lysates with monoclonal antibodies directed against the gastric H+,K+-adenosine triphosphatase yielded bands at 94 kilodaltons and more diffuse banding at 180 kilodaltons. Further purification of the poly A+ RNA on sucrose gradients eliminated prepepsinogen messenger RNA; nascent H+,K+-adenosine triphosphatase synthesized by purified messenger RNA consisted of polypeptides with molecular weights between 88,000 and 94,000. The study indicates that cell-free translation of gastric mucosal messenger RNA may provide a useful model for analysis of gastric H+,K+-adenosine triphosphatase biosynthesis and processing.
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PMID:Cell-free synthesis of rat and rabbit gastric proton pump. 255 Mar 9

The activity levels of aspartate aminotransferase (AAT), alanine aminotransferase (AlAT) and total adenosine triphosphatase (ATPase) were studied in muscle, gill, liver and brain tissues of control and methyl parathion exposed (MPE) fish. Both aminotransferases were elevated in all the tissues inferring the diversion of alpha-amino acids into the TCA cycle as keto acids to augment energy production during methyl parathion (MP) stress. In gill, liver and brain tissues, there seemed to be a shift in the aminotransferase reactions under MP impact. The total ATPase activity was decreased in all tissues, suggesting inhibition of active transport and oxidative phosphorylation.
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PMID:Tissue specific alteration of aminotransferases and total ATPases in the fish (Tilapia mossambica) under methyl parathion impact. 622 5

Insulin influences certain metabolic and transport renal functions and is avidly degraded by the kidney, but the relative contribution of the luminal and basolateral tubular membranes to these events remains controversial. We studied (125)I-insulin degradation [TCA and immunoprecipitation (IP) methods] and the specific binding of the hormone by purified luminal (L) and basolateral (BL) tubular membranes. These were prepared from rabbit kidney cortical homogenates by differential and gradient centrifugation and ionic precipitation steps in sequence, which resulted in enrichment vs. homogenate of marker enzymes' activities (sodium-potassium-activated adenosine triphosphatase for BL and maltase for L) of 8- and 12-fold, respectively. Both fractions degraded insulin avidly and bound the hormone specifically without saturation even at pharmacologic concentrations (10 muM). At physiologic insulin concentrations (0.157 nM) BL membranes degraded substantial amounts of insulin (44.2+/-2.6 and 40.7+/-2.2 pg/mg protein per min by the TCA and IP methods, respectively), even though at lesser rates (P < 0.001) than the luminal fraction (67.2+/-2.3 and 75+/-6.2 pg/mg protein per min, respectively); the rate of insulin catabolism by BL membranes was significantly higher (P < 0.001) than that which could be attributed to their contamination by luminal components [12.2+/-1.9 pg/mg per min (TCA method), or 13.7+/-1.9 pg/mg per min (IP method)]. Competition experiments suggested that insulin-degrading activity in both fractions includes both specific and nonspecific components. In contrast to degradation, insulin binding by both membranes was highly specific for native insulin and was severalfold higher in BL than L membranes [17.5+/-1.3 vs. 4.5+/-0.4 fmol/mg protein (P < 0.001) at physiologic insulin concentrations]. Despite the marked difference in the binding capacity for insulin by the two membranes, the patterns of labeled insulin displacement by increasing amounts of unlabeled hormone were superimposable (50% displacement required approximately 3 nM), suggesting that their receptors' affinity for insulin was similar. These observations provide direct evidence that interaction of insulin with the kidney involves binding and degradation of the hormone at the peritubular cell membrane.
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PMID:Insulin binding and degradation by luminal and basolateral tubular membranes from rabbit kidney. 704 Apr 74

Endosulfan is one of the most hazardous organochlorines pesticides responsible for environmental pollution, as it is very persistent and shows bio-magnification. This study evaluated the impact of acute endosulfan toxicity on metabolic enzymes, lysozyme activities, heat shock protein (Hsp) 70 expression, and histopathology in Tilapia (Oreochromis mossambicus). Among the indicators that were induced in dose dependent manner were the enzymes of amino acid metabolism (serum alanine aminotransferase and aspartate aminotransferase), carbohydrate metabolism (serum lactate dehydrogenase), pentose phosphate pathway (Glucose-6-phosphate dehydrogenase) as well as lysozyme and Hsp70 in liver and gill, while liver and gill Isocitrate dehydrogenase (TCA cycle enzyme) and marker of general energetics (Total adenosine triphosphatase) were inhibited. Histopathological alterations in gill were clubbing of secondary gill lamellae, marked hyperplasia, complete loss of secondary lamellae and atrophy of primary gill filaments. Whereas in liver, swollen hepatocyte, and degeneration with loss of cellular boundaries were distinctly noticed. Overall results clearly demonstrated the unbalanced metabolism and damage of the vital organs like liver and gill in Tilapia due to acute endosulfan exposure.
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PMID:Cellular metabolic, stress, and histological response on exposure to acute toxicity of endosulfan in tilapia (Oreochromis mossambicus). 2506 Sep 92