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:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mg2+-dependent and HCO-3-stimulated ATPase activity was highest in the brush border (microvilli) of rat duodenal mucosa compared with that of the other gastrointestinal mucosa. This ATPase may be useful to neutralize the gastric acid in the duodenal lumen. Carbonic anhydrase seems to accomplish a subsidiary role in the above reaction.
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PMID:Mg2+-HCO-3-ATPase and carbonic anhydrase in rat intestinal mucosa. 613 24

Rat and hamster pancreatic ducts were isolated by digestion with collagenase plus chymotrypsin and were cultured for eight weeks in an agarose matrix. Freshly isolated and cultured ducts were characterized morphologically and biochemically. The in vivo morphology of the ducts was maintained in vitro, although certain differences were noted. Both interlobular and intralobular ducts could be identified. gamma-Glutamyltranspeptidase and Mg-ATPase were stable enzymatic activities of the ducts of both species; alkaline phosphatase persisted only in the hamster ducts. Carbonic anhydrase and (Na + K)ATPase were minor activities of the rat ducts. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the rat ducts suggested that actin was the major duct peptide and that the major zymogens were greatly diminished. These results demonstrate that pancreatic ducts can be maintained in vitro and can be used for biochemical studies of this minor pancreatic tissue type.
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PMID:Morphologic and biochemical characteristics of isolated and cultured pancreatic ducts. 616 52

Carbonic anhydrase (CA) activity was histochemically localized in the elasmobranch rectal gland at the light and electron microscopic levels. Reaction product in the secretory tubules was localized coincident with that reported for sodium-potassium activated adenosine triphosphatase (Na-K-ATPase): along the highly amplified basolateral plasma membranes of the epithelial cells. Reaction product was also localized along the plasma membrane of adjacent central canal epithelial cells. The results suggest that CA plays a role in modulating the environment of the intercellular space which in the secretory tubule is believed to be the paracellular pathway for sodium. The results also draw attention to the possible role of the central canal epithelium in modification of the secreted fluid.
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PMID:Carbonic anhydrase localization in the elasmobranch rectal gland. 640 44

We studied the influence of normal aging on 13 glycolytic enzymes, ATPase, carbonic anhydrase, and protein kinase in the human brain cortex and putamen, where there is a significant increase in soluble HK activity with age. This phenomenon is considered to be the result of an increased release of HK from mitochondrial membranes. A significant negative correlation of the activity of F6PK with age is observed in brain cortex and putamen. While the regulation of glycolysis imposes a limit on the formation of ATP with increasing age, no change appears to occur in the enzymatic capacity to break down ATP. Na+/K+-ATPase and Mg++-ATPase do not change with age. Carbonic anhydrase, important in the regulation of the pO2/pCO2 ratio in the brain tissue, demonstrates a significant decline with increasing age. Thus pCO2-dependent regulation of tissue pH, ionic transport processes, and cerebral blood flow regulation have the tendency to become more and more unstable. Protein kinase demonstrates a progressive age-dependent decline in cAMP-dependent activity, which is most significant in brain cortex and thalamus, followed by hippocampus, amygdala, and globus pallidus. The enzyme is of importance for the phosphorylation of the cell membrane and is thus of functional relevance for the nerve cell.
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PMID:Neurochemical findings in the aging brain. 644 47

Carbonic anhydrase (CA) activity was localized in the salivery glands of the cockroach, Periplaneta americana, by (1) Hansson's histochemical technique, and (2) the use of the fluorescent sulphonamide, 5-dimethyl-amino-naphthalene-1-sulphonamide (DNSA). Both techniques reveal the same distribution pattern of CA in the four morphologically different cell types of the glands: peripheral cells, central cells, inner acinar duct cells, and distal duct cells. Positive reactions with Hansson's cobalt/phosphate technique were found in the apical regions of the peripheral cells and the distal duct cells, and were inhibited by 10(-5) M acetazolamide in control experiments. No staining could be detected in the central cells and the inner acinar duct cells. The fluorescent CA inhibitor DNSA (10(-4)M) specifically stained the peripheral cells and the distal duct cells in methanol-fixed cryostat sections, whereas the central cells and the inner acinar duct cells remained unstained. The role of CA in the peripheral cells is not clear. CA activity in the distal duct cells may provide the protons needed to run the vacuolar-type H(+)-ATPase on the apical infoldings of the cells. This ATPase may be involved in modification of the primary saliva.
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PMID:Localization of carbonic anhydrase in the salivary glands of the cockroach, Periplaneta americana. 784 90

The epithelium covering the large intestinal lymphoid follicles in fetal and postnatal lambs was examined for potassium-dependent p-nitrophenyl-phosphatase (K(+)-NPPase), carbonic anhydrase, magnesium-dependent adenosine triphosphatase (Mg(2+)-ATPase) and acid phosphatase. Reactivities for these enzymes indicated a homogenous population of cells in the follicle-associated epithelium (FAE), distinct from the absorptive epithelium. There were essentially no differences in the enzyme reactivities of the large intestinal FAE between fetuses in late gestation and postnatal lambs. The FAE showed a weak reaction for K(+)-NPPase and a variable staining for Mg(2+)-ATPase and acid phosphatase. In contrast, the adjacent absorptive epithelium demonstrated strong reactions for these enzymes. Carbonic anhydrase gave a strong reaction at the luminal and apparent basolateral cell borders of the large intestinal FAE. This distribution of reactivity for carbonic anhydrase resembled that found in the ileal FAE. In absorptive epithelial cells, only the luminal cell border reacted strongly for carbonic anhydrase. Serial sections of large intestinal tissue showed a variation in the basolateral staining of FAE from one section to the next, a finding which suggested that the reaction may be associated with transcytosis. The lymphoid follicles and domes of the large intestine showed a variable granular pattern of carbonic anhydrase staining, which also suggested a dependence on epithelial transcytosis.
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PMID:Potassium-dependent p-nitrophenyl phosphatase and carbonic anhydrase reactivities suggest that lymphoid follicles in the large intestine of lambs are lined with a uniform type of epithelial cell distinct from the absorptive epithelium. 840 61

The aim of the present work was to study the in vitro effect of cadmium on enzymes, such as intestinal and branchial carbonic anhydrase (CA) and Na(+)-K(+)-ATPase which play a key role in salt- and osmoregulation and acid-base balance in the teleost fish, Anguilla anguilla. Carbonic anhydrase activities in gill and intestinal homogenates were significantly inhibited by CdCl(2), the gill CA being more sensitive to the heavy metal (IC(50) for the branchial CA=9.97+/-1.03x10(-6) M, IC(50) for the intestinal CA=3.64+/-1.03x10(-5) M, P<0.01). With regards to the intestinal CA activity, it has been shown in a previous study (Maffia et al., 1996) that two isoforms exist, a cytosolic and a brush-border membrane bound. These two isoforms show a different sensitivity to cadmium, with the membrane-bound enzyme less sensitive with respect to the cytosolic one, since it showed still an incomplete inhibition at the highest cadmium concentration tested. The inhibition of all the CA activity tested revealed a time-dependence since it required at least 10 min (1 h for the membrane-bound isoform) preincubation with the heavy metal to appear. Na(+)-K(+)-ATPase enzymatic activities, measured in intestinal and branchial homogenates, were inhibited by cadmium in a dose-dependent manner, with the branchial activity being more sensitive to the action of the heavy metal than the intestinal one (IC(50) for the branchial enzyme=1.38+/-0.09x10(-7) M, IC(50) for the intestinal enzyme=2.86+/-0.02x10(-7) M, P<0.01). The most of inhibition of the enzyme appeared without any preincubation with the heavy metal. Mg(2+)-ATPase activity was not significantly altered by the in vitro cadmium exposure either in the gills or in the intestine. These findings observed in vitro could be useful in the understanding of the toxic effects that cadmium elicits on aquatic organisms in vivo. In fact, the impairment of the activity of enzymes which carry out key physiological roles could cause alterations of the physiology of the whole organism.
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PMID:Inhibition of eel enzymatic activities by cadmium. 1079 37

The transepithelial transport of inorganic carbon to endolymph and its subsequent deposition on otoliths were pharmacologically examined by incubating the sacculus containing an otolith with NaH(14)CO(3). Calcium incorporation was also studied. Carbon incorporation into endolymph and otoliths was saturated with increased concentrations of bicarbonate ions in the incubation medium and was followed by the Michaelis-Menten equation with a K(m) of 26.3 mM and 0.4 mM, respectively. Carbon incorporation decreased with an increase in chloride concentrations in the medium. Calcium incorporation was not affected by chloride and bicarbonate ions up to 10 mM. Higher concentrations of bicarbonate ions reduced calcium incorporation into both fractions. Carbon incorporation into endolymph and otoliths was inhibited by acetazolamide, disulfonate stilbenes (DIDS and SITS), thiocyanate, and ouabain. Calcium incorporation was not affected by these inhibitors. Amiloride inhibited carbon incorporation into otoliths alone. These results suggest that HCO(3)(-)-ATPase and Cl(-)/HCO(3)(-)-exchangers are involved in the transepithelial transport of bicarbonate ions to the endolymph. Carbonic anhydrase was also suggested to play a role in carbonate production for otolith calcification.
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PMID:Effects of enzyme and anion transport inhibitors on in vitro incorporation of inorganic carbon and calcium into endolymph and otoliths in salmon Oncorhynchus masou. 1113 50

Carbonic anhydrase and proton ATPase are co-distributed, being restricted to the apical regions of the gill epithelium of freshwater teleosts. Carbonic anhydrase supplies protons to the apical proton ATPase. Carbonic anhydrase is absent from the basal regions of the gill epithelium. Plasma flowing through the gills has no available carbonic anhydrase activity and plasma CO2/bicarbonate reactions are uncatalyzed. Thus, bicarbonate dehydration in plasma is negligible, and catalyzed bicarbonate dehydration occurs in erythrocytes in blood flowing through the gills. This results in tight coupling of carbon dioxide excretion to oxygen uptake and the evolution of hemoglobins with large Haldane effects but low buffering capacities, typical of many freshwater teleosts. Tight coupling of carbon dioxide and oxygen transfer in these fish also ensures that the Root shift does not impair oxygen uptake at the gills. Under these conditions, there is a selective advantage for hemoglobins with a Root shift. The presence of a Root shift augments oxygen transfer to the tissues in general and the eye and swimbladder in particular.
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PMID:Interactions between ion and gas transfer in freshwater teleost fish. 1125 98

A time course analysis using (110m)Ag, (24)Na(+), and (36)Cl(-) examined gill silver accumulation and the mechanism by which waterborne silver (4.0 x 10(-8) M; 4.3 microg/l) inhibits Na(+) and Cl(-) uptake in gills of freshwater rainbow trout. Analyses of gill and body fluxes allowed calculation of apical uptake and basolateral export rates for silver, Na(+), and Cl(-). To avoid changes in silver bioavailability, flow-through conditions were used to limit the buildup of organic matter in the exposure water. For both Na(+) and Cl(-) uptake, apical entry, rather than basolateral export, was the rate-limiting step; Na(+) and Cl(-) uptake declined simultaneously and equally initially, with both uptakes reduced by approximately 500 nmol.g(-1).h(-1) over the 1st h of silver exposure. There was a further progressive decline in Na(+) uptake until 24 h. Carbonic anhydrase activity was inhibited by 1 h, whereas Na(+)-K(+)-ATPase activity was not significantly inhibited until 24 h of exposure. These results indicate that carbonic anhydrase inhibition can explain the early decline in Na(+) and Cl(-) uptake, whereas the later decline is probably related to Na(+)-K(+)-ATPase blockade. Contrary to previous reports, gill silver accumulation increased steadily to a plateau. Despite the rapid inhibition of apical Na(+) and Cl(-) uptake, apical silver uptake (and basolateral export) increased until 10 h, before decreasing thereafter. Thus silver did not inhibit its own apical uptake in the short term. These results suggest that reduced silver bioavailability is the mechanism behind the pattern of peak and decline in gill silver accumulation previously reported for static exposures to silver.
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PMID:Time course analysis of the mechanism by which silver inhibits active Na+ and Cl- uptake in gills of rainbow trout. 1501 22


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