Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Basolateral membrane vesicles were isolated from the rat kidney cortex by a modified method of cation precipitation. Different steps of preparation were analysed using the marker enzymes: Na+,K+-ATPase (for basolateral membrane), alkaline phosphatase (for apical membrane), glucose-6-phosphatase (for membranes of endoplasmic reticulum) and succinate dehydrogenase (for mitochondria). The basolateral membrane was purified by a 8-9-fold treatment with Na+,K+-ATPase, while other membrane contaminations were as low as 2% (as compared to homogenate). The transport of 3H-p-aminohippurate (3H-PAH) by basolateral membrane vesicles was measured under different experimental conditions. The 3H-PAH uptake was found to be Na-gradient dependent. The initial rate of 3H-PAH uptake in the presence of NaCl gradient (500 pM/mg X min) was higher than without the gradient (88 pM/mg X min). It is concluded that the PAH transfer across the basolateral membrane may be energized by the Na+ chemical gradient.
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PMID:[Effect of a NaCl gradient on the transport of para-aminohippuric acid into the vesicles of the basolateral membrane of the kidney cortex]. 359 Mar 16

It was established in an experiment with 13 sheep of the local improved breed that the single s/c injection of levamisole at the rate of 7.5 mg per kg of body mass led to a rise of the phagocytic activity of neutrophil leukocytes. These cells also had higher cytochemical activity of the alkaline phosphatase, glucose-6-phosphatase, and lipids (sudanophilia). No changes in the total count of leukocytes were found. The cytochemical activity of lactate-dehydrogenase, succinate-dehydrogenase, and alpha-glycerophosphate-dehydrogenase was also found to rise. On the base of the marker capacity of the acid naphthylacetate esterase with regard to the T-lymphocyte system there set in on the 3rd day following levamisole injection a 4 to 5 rise in the T-lymphocyte count, particularly in the mature T mu-lymphocytes, to the detriment of the B-cells which dropped in number. On the 7th day all these changes receded, however, the percent of lymphocytes with azure granules in the cytoplasm and the average number of these granules per lymphocyte cell rose. In the entire 7-day period of investigation a lowering trend was shown by the amount of serum lysozyme which dropped several times as against the initial level.
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PMID:[Effect of levamisole on the cytochemical function of leukocytes and on blood lysozyme in sheep]. 361 82

Compound LY171883 caused dose-related and reversible hepatomegaly in male Fischer 344 rats. Histological examination revealed hepatocellular hypertrophy with no other evidence of liver disease. There were only minor changes in serum glucose, total bilirubin, alkaline phosphatase, and alanine transaminase which were generally unrelated to dose and dissociable from the hepatomegaly. Total liver DNA increased but the DNA concentration decreased, indicating that liver growth involved a combination of hypertrophy and hyperplasia. Total liver protein and RNA increased. Hepatic mitochondrial protein content increased but cytochrome oxidase activity was not changed. There were minor changes in mitochondrial respiratory parameters; however, all the values were in the normal range and there was no indication of mitochondrial toxicity. Microsomal protein, drug-metabolizing activity, and cytochrome P-450 increased, but glucose-6-phosphatase activity was not changed. The induction of drug-metabolizing enzymes and absence of toxicity were evidence that the hepatomegaly was an adaptation to an increased functional load in the liver. An increase in catalase activity suggested that the response may have also involved peroxisomes. In addition to rats, LY171883 administration caused hepatomegaly in mice and hamsters at daily exposures exceeding 100 mg/kg. The response was not observed in guinea pigs, beagle dogs, or rhesus monkeys given maximum tolerated doses, indicating LY171883-induced hepatomegaly is not a response common to all species. The doses required to elicit hepatomegaly greatly exceeded doses that produce pharmacological efficacy in animals and those that are expected to be used clinically. Since humans will not receive doses comparable to those given rodents, and considering that the primate species tested did not experience hepatomegaly, it is unlikely that the effect observed in rodents can be extrapolated to humans.
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PMID:Characterization of liver enlargement induced by compound LY171883 in rats. 384 Jan 8

Hematological, biochemical, histoenzymological, and histopathological changes in serum and tissues were studied in chickens during outbreaks of nephritis. Hematological studies revealed normocytic-normochromic anemia characterized by increased total erythrocyte counts, hemoglobin, packed cell volume, and erythrocyte sedimentation rate. Albumin-to-globulin ratio and sodium levels in serum, glucose in blood, and alkaline phosphatase and glucose-6-phosphatase in liver and kidneys were decreased. Glutamate pyruvate transaminase, uric acid, non-protein-nitrogen, and potassium levels in serum were increased. No significant change in the calcium, phosphorus, and total protein levels in serum was observed. These changes were directly related to the severity of the nephritis.
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PMID:Clinicopathological, hematological, and biochemical studies in some outbreaks of nephritis in poultry. 407 33

Particulates containing a large part of the alkaline phosphatase activity of renal tissue were separated from homogenates and from ribosomal preparations by zonal centrifugation. The particles had a high content of phospholipid and cholesterol that was not removed by treatment with I percent deoxycholate. Enzymatic activities concentrated with the particles were the alkaline phosphatase, a peptidase resistant to proteolysis, glucose-6-phosphatase, inorganic pyrophos-phatase, and adenosine triphosphatase. The particles accumulated leucine with no stimulation from soluble factors and with inhibition by other amino acids; the accumulation was stimulated by adenosine triphosphate and was not inhibited by puromycin. The particles appear to be derived from the membranes of the brush borders of tubular cells.
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PMID:Brush border particulates of renal tissue. 430 46

A method is described for the rapid isolation of a plasma membrane fraction containing a high concentration of intact bile canaliculi from the rat liver. Isolated bile canaliculi retain most of the ultrastructural features exhibited in the intact liver cell. The final fraction contains 5'-nucleotidase activity at approximately the same concentration as that in previous preparations of plasma membranes. In the presence of 0.01 M Mg(++), 5'-nucleotidase exhibits a double pH optimum at pH values of 7.5 and 9.5. The activities of glucose-6-phosphatase and alkaline phosphatase are present in low amounts. Cytochrome P-450 is not detectable. Na(+)-K(+)-activation of ATPase is observed to the extent of 20-36% in about half of the assays. The availability of a method for preparation of intact bile canaliculi should prove useful for studying the biochemical events associated with the transport of bile constituents into canaliculi.
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PMID:Plasma membranes of the rat liver. Isolation and enzymatic characterization of a fraction rich in bile canaliculi. 430 40

1. The distribution of enzymatic activities was determined in subcellular fractions of rat kidney cortex homogenates after various homogenization procedures. The specific activities of kininogenase (KGA), BAEE esterase (pH 8.5), alkaline phosphatase and glucose-6-phosphatase were, on average, 3.4 times higher in the microsomal fraction than in the whole homogenate. The total amount of these activities in the microsomal fraction after gentle, ordinary and forced homogenization were about 15, 40 and 65% of total recovered activities, respectively. These results confirmed the localization of KGA in the microsomal fraction.2. Renin activity was primarily recovered in the heavy mitochondrial fraction. When the force of the homogenization was increased some renin activity was shifted to the soluble fraction.3. When a mixture of renin and purified urinary KGA was given intravenously to an anaesthetized rat, a hypotensive response due to the KGA was followed by a hypertensive renin response. Over a certain range of concentrations KGA and renin could be measured simultaneously. In fractions of kidney homogenates, however, KGA activity was too low to be measured by this method.
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PMID:Subcellular localization of renin and kininogenase in the rat kidney. 432 58

Brush borders and plasma membranes have been purified from mucosal epithelial cells of rabbit ileum under control conditions and after treatment for 3 hr with cholera toxin in vivo. The activity of several enzymes in these preparations was measured. It was concluded that adenyl cyclase, like NaK-ATPase, seems not to be a normal constituent of brush borders. Both these enzymes are present in plasma membrane preparations derived largely from the basal and lateral margins of the epithelial cells, both may be phospholipid dependent enzymes and both are affected by cholera toxin. Adenyl cyclase activity is increased while NaK-ATPase is decreased. The activities of alkaline phosphatase, leucineaminopeptidase, 5'-nucleotidase, glucose-6-phosphatase, and Mg-ATPase were not found to be affected by the toxin. Cholera toxin, which makes contact with the luminal side of the epithelial cells, in the natural disease and in the experimental model, would appear to exert its pathologic effect on adenyl cyclase at the opposite (basal and lateral) side of the cells.
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PMID:Localization of the action of cholera toxin on adenyl cyclase in mucosal epithelial cells of rabbit intestine. 434 29

Non-specific and specific phosphatases have been histochemically localized in the tissues of Avitellina lahorea, an intestinal parasite of sheep and goats. Large quantities of acid phosphatase, alkaline phosphatase and adenosine triphosphatase were observed in almost all organs except the parenchyma where there were moderate amounts of acid phosphatase and no alkaline phosphatase; the reproductive ducts contained moderate amounts of alkaline phosphatase. 5-nucleotidase was observed only in the uterus, egg pouches and eggs and glucose-6-phosphatase activity was restricted to the tegument. The probable functions of these moieties at different sites are discussed.
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PMID:Histochemical localization of phosphomonoesterases in Avitellina lahorea Woodland, 1927 (Cestoda: Anoplocephalida). 608 41

The uteri of 8 goats (2 each at pregnancy, estrus, diestrus, and prepubertal periods) were used for histoenzymic localization of alkaline phosphatase (AKP), acid phosphatase (ACP), glucose-6-phosphatase (G6P), and adenosine triphosphatase (ATPase). In the surface and glandular epithelia of endometrium, all the enzymic reactions showed no appreciable change during pregnancy as compared with diestrus, except that the G6P activity was reduced. At estrus, the AKP reaction in the surface as well as glandular epithelia and ATPase in the glandular epithelium did not change, the ACP decreased and G6P increased in both epithelia but ATPase decreased in surface epithelium. Caruncular tissue showed increased AKP and decreased ACP and ATPase reactions at estrus, all being maximum during pregnancy. No specimen showed G6P reaction in the caruncular tissue. In prepubertal uteri, all the enzymes studied were localized in the same locations as in diestrus uteri except that ACP and G6P were not localized in the caruncular tissue. The myometrium of all the samples demonstrated only ATPase.
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PMID:Histoenzymic studies on phosphatases in the uterine wall of the goat (Capra hircus). 609 1


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