Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: HUMANGGP:021133 (ATP)
 132,114 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The characterization and localization of a Ca(2+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) in the tooth germ of the porcine fetus are reported. This enzyme, a microsome fraction, is preferentially activated by Ca(2+). In the presence of 0.5 mM ATP, maximal enzyme activity is obtained at 0.5--1.0 mM CaCl2. The maximal rate of ATP hydrolysis is approx. 20 mumol per h per mg of protein as the enzyme preparation is used here. At optimal Ca(2+) concentration, the Mg(2+) has an inhibitory effect. The enzyme does not require Na+ or/and K+ for activation by Ca(2+). Other nucleotide triphosphates may serve as the substrate, but V for ATP is the highest. The Km for ATP is 8.85 - 10(-5) M. The optimal pH for Ca(2+) activation of the enzyme lies around 9.2. Well known inhibitors of (Na+ + K+)-ATPase, mitochondria ATPase and Ca(2+)-ATPase in the erthrocyte do not inhibit the enzyme. In the subcellular order the enzyme may be assumed to be localized in the smooth endoplasmic reticulum fraction containing cell and Golgi body membrane fragments and in the tissue order in the enamel organ containing an ameloblast layer, stratum intermedium and stellate reticulum.
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PMID:Calcium-stimulated adenosine triphosphatase in the microsomal fraction of tooth germ from porcine fetus. 0 71

Both UDP-glucuronyltransferase (GT) and beta-glucuronidase (betaG) were assayed in untreated liver microsomes. Optimum assay conditions were established with rat liver microsomes using p-nitrophenol (pNP) and its glucuronide (pNPGA) at the pH optima of GT (7.5) and betaG (4.5). The activities of the two enzymes were compared using microsomes from rats, mice, pigs, cattle and horses, with pNP, pNPGA, and phenolphthalein as substrate, in the presence of various cofactors and inhibitors at pH 7.5 and 4.5. These data disclose pronounced differences with respect to species, substrate and other experimental conditions, thereby precluding the establishment of general optimum conditions. The two enzymes were also assayed under strictly identical conditions using pNP and pNPGA and rat liver microsomes at pH 7.5 in the presence and absence of UDP-glucuronate disodium (UDPGA), activators (ATP;UDP-N-acetylglucosamine) and inhibitors. When provided with a functional level of UDPGA, both enzymes proved active under those conditions, and a conjugation-deconjugation interplay was indicated. The two processes could be selectively and totally inhibited by Zn2+ and saccharolactone. The results suggest that conjugation-deconjugation-reconjugation cycles may be operative in the metabolism of drugs in vivo, taking place already at the level of the liver endoplasmic reticulum.
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PMID:Liver microsomal beta-glucuronidase and UDP-glucuronyltransferase. 0 Feb 30

Tests were carried out on the influence of alloxan-induced diabetes mellitus on the metabolism and the ultrastructure of ovaries of juvenile rats. The diabetes mellitus caused the following changes in the metabolism: reduction in the concentration of ATP and NADPH, increase in the lactate/pyruvate quotient to above 40, reduction in the ATP/ADP quotient to below 1, reduction in the level of activity of the hydrogen-conveying enzymes G-6-P-dehydrogenase, isocitrate dehydrogenase and malate dehydrogenase, increase in the level of activity of the alkaline phosphatase, reduction of the protein content. Ultrastructure: almost complete disappearance of the rough endoplasmic reticulum, shrinkage of the mitochondria, reduction of the cristae and condensation of the matrix. The smooth endoplasmic reticulum remains unchanged, the extent of the Golgi-complex is reduced. Easy removal of the lipid deposits.
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PMID:Metabolism and ultrastructure in ovaries of alloxan-diabetic juvenile rats. 0 67

Endogenous phosphorylation was studied with highly purified fractions of the plasma membrane and the endoplasmic reticulum of SV40-transformed mouse fibroblasts using [gamma-32P]ATP and [gamma-32P]GTP as precursors. With ATP maximum overall incorporation of 32P into both membrane fractions occurred at pH 7.8 in the presence of 10 mM MgCl2 after incubation for 1 min. GTP could be utilized only by the plasma membrane fraction showing maximum incorporation of 32P at pH 7.8 and 10 mM MgCl2 after incubation for 3 min. The pattern of phosphoproteins of the plasma membrane is represented by more than 15 proteins whereas the endoplasmic reticulum essentially contained only one phosphorylated component of 35 000 molecular weight. The comparison of ATP- and GTP-specific phosphorylation of the plasma membrane revealed GTP to be a less efficient precursor yielding a similar phosphoprotein pattern with one significant difference: the GTP-specific main component exhibited a molecular weight of about 100 000 and the ATP-specific main component a molecular weight of 110 000. The relative distribution of individual phosphoproteins in the pattern of the plasma membrane was dependent on pH but not on MgCl2 concentration or time of incubation. Increasing concentrations of plasma membrane protein altered the patterns of phosphoproteins dramatically: At high protein concentrations the ATP-specific main component (Mr = 110 000) was no more phosphorylated whereas with GTP the main component Mr = 100 000 was essentially the sole phosphorylated protein.
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PMID:Characterization of specific differences in protein phosphorylation of the plasma membrane and the endoplasmic reticulum of mouse fibroblasts. 3 72

2-Deoxy-D-galactose, in a dose of 3 mmol/kg, was administered intraperitoneally twice daily to young rats for periods up to 12 weeks. This dosage schedule resulted in recurrent phosphate trapping predominantly in liver. UTP deficiency was excluded by simultaneous uridine injections. Phosphate trapping was caused by the rapid accumulation of 2-deoxy-D-galactose 1-phosphate and was most pronounced in liver but also demonstrated in small intestine, brain, spleen, and thymus. The marked, although transient, drop in the hepatic content of inorganic phosphate triggered the catabolism of adenine nucleotides and a loss of ATP. Other metabolic pathways affected by phosphate deficiency include glycogenolysis and glycolysis. Increasing with time, repeated doses of the galactose analog led to retardation and arrest of growth, hepatomegaly, and splenomegaly. The average relative liver and spleen weights were elevated 2.5- and 4.5-fold, respectively, after 12 weeks of treatment. Liver damage was indicated by hyperbilirubinaemia and a progressive rise in the activity in plasma of sorbitol dehydrogenase, alkaline phosphatase, and gamma-glutamyltransferase. Examination by light and electron microscopy showed increasing numbers of vacuoles, surrounded by a single membrane, in hepatocytes, sinusoidal endothelial cells, and Kupffer cells. Focal cytoplasmic degeneration in hepatocytes was occasionally indicated by formation of autophagic vacuoles and finger print lysosomes. Hepatocytes of 2-deoxy-D-galactose-treated rats showed a dissociation and fragmentation of the rough endoplasmic reticulum. Sinusoidal endothelial cells and Kupffer cells were markedly enlarged, the latter contained a PAS-positive but amylase resistant substance. Extrahepatic changes included an increased occurrence of vacuolated cells in thymus. Phosphate trapping and its metabolic consequences are common phenomena in the experimental injury induced b 2-deoxy-D-galactose and in some hereditary diseases such as uridylyltransferase deficiency galactosaemia, fructose intolerance and glucose-6-phosphatase deficiency.
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PMID:Consequences of recurrent phosphate trapping induced by repeated injections of 2-deoxy-D-galactose. Biochemical and morphological studies in rats. 4 10

The reversibility of changes in ultrastructure, K+, and ATP content was studied in experimental injury of Ehrlich ascites tumor cells. Different grades of injury resulted from incubations in N2 atmosphere and omitting substrate after which air and glucose were reinstated. The changes observed in cells after 1 hour of anoxia such as dilations of endoplasmic reticulum, complex invaginations of plasma membrane, and slight condensation of mitochondria, as well as a drop of K+ and ATP content to a level approximating 40 per cent of the paired controls, were entirely reversible. After 2 hours of anoxia approximately 50 per cent of the cells recovered, but after 3 and 4 hour of anoxia most of the cells were irreversibly damaged showing markedly swollen mitochondria with flocculent densities.
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PMID:Studies of cellular recovery from injury. I. Recovery from anoxia in Ehrlich ascites tumor cells. 5 20

Continuous sucrose density gradient subfractions from bovine adrenal medullary microsomes were found to accumulate 45-Ca-2+ in the presence of ATP and ammonium oxalate mainly in subfractions of intermediate density. (Na-++K-+)-ATPase (plasma membrane marker) and Ca-2+-ATPase activities were also concentrated in these intermediate subfractions but thiamine pyrophosphatase (Golgi apparatus marker) was not. NADH oxidase (endoplasmic reticulum marker) activity was distributed throughout all subfractions. 45-Ca-2+ accumulation in adrenal cortical microsomes was found to rise and fall in parallel with thiamine pyrophosphatase but not with (Na-++K-+)-ATPase or NADH oxidase activities. Accumulation of 45-Ca-2+ in membrane vesicles in these experiments suggests the existence of a calcium transfer mechanism in plasma membranes of the adrenal medulla but not adrenal cortex.
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PMID:Evidence for a plasma membrane calcium pump in bovine adrenal medulla but not adrenal cortex. 12 98

The activity of adenosine triphosphatase and alkaline phosphatase was investigated at the fine structural level in the cyst stages of Sarcocystis tenella parasitic in the esophagus of sheep. Alkaline phosphatase reaction was observed along the outer membrane of the parasite's pellicle. The enzymatic activity was much higher on the surface of metrocytes than that of zoites, which proved to be infectious. No reaction was noted in the interior of the parasites. However, a significant amount of alkaline phosphatase activity occurred along the inner surface of the 25 nm thick primary layer of the cyst wall. No evidence of the reaction of this enzyme was seen in the secondary cyst wall, which consisted of degenerated host cells. ATP-ase activity was found in a considerable degree along the primary cyst wall (=directly limiting the cyst's interior), whereas the ground-substance of the cyst, surrounding the parasites, is free of deposits. In the parasites ATP-ase was localized in the endoplasmic reticulum, in the perinuclear space, and between the two inner membranes of the three-layered pellicle. Only rarely a slight reaction was seen in the mitochondria of the metrocytes, which are the reproductive cells. The other organelles typical for S. tenella were free of ATP-ase. The results indicate that the enzymes studied participate in the growing process of the cysts, in which finally the infectious zoites remain in a more or less inactive state. The localizations of the enzymes corresponded with the results known from metazoa.
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PMID:[Ultrastructural localization of alkaline phosphatase and ATP-ase in cyst stages of Sarcocystis tenella (Sporozoa, Coccidia) parasitic in the esophagus of sheep (author's transl)]. 12

Spontaneously hypertensive rats (SHR) and two strains of normotensive rats were compared with respect to enzymatic activities and calcium accumulation of plasma membrane and endoplasmic reticulum enriched fractions from their mesenteric arteries. Increased specific activities of alkaline phosphatase, 5'-nucleotidase and Mg2+-ATPase, and increased ATP-dependent calcium accumulation were found in 5- to 6-month-old SHR as compared to both strains fo age-matched normotensive rats. Alkaline phosphatase was increased in 33-day-old "early hypertensive" and 3- to 4-month-old SHR, but 5'-nucleotidase, Mg2+-ATPase, and calcium accumulation were not. Hydralazine treatment of young SHR partially prevented the increase of both alkaline phosphatase activity and blood pressure that develops with age. The relationship between alkaline phosphatase activity and the alterations in vascular reactivity associated with hypertension remains to be determined.
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PMID:Relationship between blood pressure of spontaneously hypertensive rats and alterations in membrane properties of mesenteric arteries. 13 88

In Hirudo medicinalis an extensive and highly elaborate three dimensional network of smooth endoplasmic reticulum cisternae is found in very close structural relationship to the receptive (microvillar) membrane, as reported for many other invertebrates. A variant of the potassium pyroantimonate technique showed that these submicrovillar endoplasmic reticulum cisternae (SMC) and mitochondria are major intracellular calcium stores. Furthermore, using saponine-skinned photoreceptors for an in situ accumulation experiment, calcium oxalate precipitates in SMC demonstrate that this organelle is able to accumulate Ca2+ from a concentration of 2 x 10(-5) M, when ATP, Mg2+, and oxalate ions are present in the accumulation medium. This result provides direct evidence for the hypothesis that SMC may play a particularly important role in the regulation of intracellular ionized calcium in invertebrate photoreceptor cells. Morphological evidence supports this view.
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PMID:Subcellular calcium localization and AT0-dependent Ca2+-uptake by smooth endoplasmic reticulum in an invertebrate photoreceptor cell. An ultrastrucutral, cytochemical and X-ray microanalytical study. 16 Mar 17


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