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)

1. While much is now known about the Na-K-ATPase and the posttetanic hyperpolarization of nervous tissue, they have yet to be studied together in the same preparation. 2. The post-tetanic hyperpolarization was studied in desheathed garfish olfactory nerve. The rate constant of decay of the post-tetanic hyperpolarization was determined by monitoring difference potentials after stimulation at 1/sec for 2-3 min. 3. In membrane fractions prepared from these nerves, the ouabain-sensitive ATPase activity (Na-K-ATPase) was determined by spectrophotometric measurements. 4. Both the post-tetanic hyperpolarization and the Na-K-ATPase showed a similar sigmoidal dependence on K+ concentration. The sequence of cation specificities measured at the K-site of the enzyme was the same as that determined by post-tetanic hyperpolarization measurements in whole nerve. 5. The rate constants of the enzyme showed a dependence on Na+ concentration that paralleled the way in which the post-tetanic hyperpolarization rate constants varied as a function of the number of impulses. When Na+ was completely replaced by Li+, neither enzyme activity nor post-tetanic hyperpolarization could be measured. 6. The pH optimum for enzyme activity was between pH 7-0 and 7-8, while the optimal pH for post-tetanic hyperpolarization was above pH 8-0. 7. Metabolite levels in preparations of this nerve studied in vitro correspond to levels found in vivo. 8. High energy phosphate levels were measured fluorometrically in extracts of nerve samples that had been stimulated in air at 1/sec for various intervals. 9. During the first 2 min of stimulation, there was a significant accumulation of inorganic phosphate, and the ATP/ADP.Pi ratio dropped appreciably. 10. The accumulation of ATPase products was commensurate with the approach of post-tetanic hyperpolarization rate constants to their maximum level. This provides direct evidence for an ATPase functioning in active Na+ transport in nerve. 11. The garfish Na-K-ATPase is sensitive to the ATP/ADP ratio of the incubating medium, but is relatively insensitive to orthophosphate, Pi. The fall in post-tetanic hyperpolarization rate constants observed with continued nerve stimulation may have been partially due to the falling ATP/ADP ratio measured in nerve under similar conditions.
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PMID:Post-tetanic hyperpolarization, sodium-potassium-activated adenosine triphosphatase and high energy phosphate levels in garfish olfactory nerve. 13 26

Phenylketonuric squirrels have shown marked inhibition of alkaline phosphatase in the olfactory lobes and cerebral hemispheres, whereas the Na+-K+-ATPase remained less altered. In the pathogenesis of phenylketonuria inhibition of alkaline phosphatase at the level of "Blood-Brain Barrier" (BBB), leads transport system to impaired functioning.
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PMID:Imbalance in the activities of alkaline phosphatase and Na+-K+-ATPase in the brain of experimentally induced phenylketonuric squirrels (Funambulus palmarum). 21 45

1. The subcellular distribution of binding sites for 125I-labeled alpha-bungarotoxin was studied in rat cerebral cortex. Primary fractions showing higher specific activity than homogenate were P2 (crude mitochondria and nerve endings) and P3-P2 was subfractionated on a Ficoll gradient with the P2B (nerve ending) subfraction exhibiting the greatest recovery (65%) and enrichment of toxin binding. Toxin binding showed a distribution similar to that of acetylcholinesterase, choline acetyltransferase, and sodium and potassium ion-activated ATPase. 2. P2B and P3 were subfractionated on five-step discontinuous sucrose gradients. The highest specific activity of toxin binding and acetylcholinesterase was associated with fractions of relatively low buoyant density, while choline acetyltransferase activity was associated with fractions of higher density. 3. Toxin binding, acetylcholinesterase, and choline acetyltransferase activities were relatively high in olfactory lobes, cerebral cortex, thalamic region, caudate nucleus, and brain stem; intermediate in hippocampus; low in cerebellum. 4. The relationship of toxin binding to the putative acetylcholine receptor in brain is discussed.
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PMID:Subcellular and regional distribution of 125I-labeled alpha-bungarotoxin binding in rat brain and its relationship to acetylcholinesterase and choline acetyltransferase. 115 70

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

1. Membrane fractions were obtained from homogenates of olfactory rosettes from Atlantic salmon (Salmo salar) or from isolated olfactory cilia and homogenates of deciliated olfactory rosettes. 2. Specific binding of L-[3H]alanine was saturable, high-affinity, and effectively inhibited by L-threonine, L-serine and L-alanine but not by L-lysine or L-glutamic acid. Comparable results were obtained with L-[3H]serine except for the presence of a second, lower affinity, binding site for L-alanine but not L-serine. 3. Specific binding of L-[3H]alanine was inhibited by low concentrations of mercury ion, acidic pH, and high concentrations of cadmium, copper or zinc ions. Aluminum had no effect. 4. Specific binding sites for L-alanine were present in membranes from isolated cilia at a level 2-fold that of membranes prepared from the deciliated rosette. 5. Ouabain sensitive Na+, K(+)-ATPase activity was also determined in cilia preparations. This enzyme was present in cilia at a level approximately 3-fold that of membranes prepared from the deciliated rosette. 6. The results are consistent with the presence of an olfactory alanine receptor in S. salar with binding characteristics similar to those of a variety of other fish species and with a localization on olfactory cilia as well as non-ciliated receptor cell membranes.
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PMID:L-alanine binding sites and Na+, K(+)-ATPase in cilia and other membrane fractions from olfactory rosettes of Atlantic salmon. 164 34

The NaK-adenosine triphosphatase (ATPase)-rich nerve-ending particle preparations (B fractions) of the epithelial tissue of chicken olfactory tubercle and the olfactory main concha were isolated by differential centrifugation. These tissues were exposed to the following odorants: 2-nonanone, 1-nonanol, 1-octanol, (+)2-octanol, and (-)2-octanol. There was a significant stimulation of NaK-ATPase by 2-nonanone (1 x 10(-3) M) in the B fraction of the olfactory tubercle and olfactory main concha. The NaK-ATPase increased significantly in the B fraction response of the olfactory main concha with 1 x 10(-3) M of 1-octanol but NaK-ATPase declined significantly in the presence of 1 x 10(-3) M of 1-nonanol. Both optical and structural isomers of odorants were shown to elicit different responses in NaK-ATPase activity. It is proposed that interactions between the odorant molecules and the membrane bound NaK-ATPase complex lead to recognition of odor by chickens.
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PMID:Effects of several selected odorants on the sodium- and potassium-dependent adenosine triphosphatase activities of two different chicken olfactory tuberinals. 164 65

The olfactory epithelium is comprised of bipolar sensory neurons, sustentacular cells, and basal cells. The sensory neurons have apical knobs and cilia, which project into the olfactory mucus toward the nasal lumen, and represent presumptive sites of odorant binding. Ionic currents, measured across this epithelium in both the resting and odorant-stimulated states, are known to be sustained, at least in part, by active transport of sodium. Information identifying the cellular sites of ion transport in olfactory sensory epithelium will therefore aid in elucidating the ionic mechanisms associated with olfactory transduction. The membrane-bound enzyme Na+/K(+)-ATPase mediates active ion transport in many other cells and tissues. We have consequently employed the cytochemical technique reported by Ernst (J. Histochem. Cytochem., 20 (1972) 23-38, 1322) to identify possible sites of elevated Na+/K(+)-ATPase activity in olfactory epithelium. This procedure detects inorganic phosphate (Pi) released from an artificial substrate (nitrophenyl phosphate) by enzyme catalytic activity. In the presence of strontium ion. Pi is precipitated near regions of high enzymatic activity, then converted to a product visible in the electron microscope. Parallel control preparations were incubated in media (1) supplemented with the specific Na+/K(+)-ATPase inhibitor ouabain (to abolish formation of specific reaction product); (2) with substrate deleted (to demonstrate possible non-specific binding of Sr2+ and/or Pb2+); or (3) with the necessary cofactor K+ deleted. In tissues incubated for demonstration of Na+/K(+)-ATPase activity, reaction product was associated with apical knobs, cilia and dendrites of olfactory receptor neurons at the apical surface. In the more proximal region of the epithelium, reaction product was associated with cell bodies and axons of the sensory neurons, and with the lateral membranes of sustentacular cells. Reaction product was deposited intracellularly, compatible with the known mechanism of the Na+/K(+)-ATPase enzymatic reaction. In control specimens incubated with ouabain, with substrate deleted, or with K+ deleted, only a small quantity of non-specific precipitate was observed. These results are discussed with reference to the various sodium currents implicated in olfactory transduction and transepithelial transport.
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PMID:Ultrastructural localization of Na+/K(+)-ATPase in rodent olfactory epithelium. 164 70

SERCA-2 is an endoplasmic reticulum Ca2+ ATPase present in brain [Gunteski-Hamblin A.-M. et al. (1988) J. biol. Chem. 263, 15032-15040]. We sought to map the distribution of this pump in the rat brain and investigate its relationship to Ca2+ uptake by brain endoplasmic reticulum. Using in situ hybridization and Northern blots with antisense oligonucleotide probes, we found that SERCA-2 is concentrated most densely in the cerebellum, especially in Purkinje cells, and in the hippocampus, with heavy labeling also in cortex, thalamus, pontine nuclei and the mitral cell layer of the olfactory bulb. 45Ca2+ uptake displayed a similar pattern with heaviest accumulation in cerebellum, hippocampus, cortex, thalamus and olfactory bulb. In corpus striatum and substantia nigra, relative 45Ca2+ accumulation was greater than SERCA-2 mRNA. Thus, SERCA-2 appears to be involved in Ca2+ uptake into endoplasmic reticulum in brain for release by inositol 1,4,5-trisphosphate and other agents.
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PMID:Localization of an endoplasmic reticulum calcium ATPase mRNA in rat brain by in situ hybridization. 183 65

Protein content and ATPase activities have been determined in the superficial and deep layers of the rat olfactory bulb. Protein levels, Mg2(+)-ATPase and Na+,K(+)-ATPase activities were significantly higher in the whole homogenate for the superficial layers. These differences were amplified when activity was expressed on a wet weight basis in a crude microsomal preparation isolated by differential centrifugation. Specific activities, however, showed similar values in the microsomal fractions from superficial and deep layers. The results are discussed in terms of differences in the density of neuronal processes and efficiency of K+ reuptake mechanisms.
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PMID:Na+,K(+)-ATPase in the rat olfactory bulb: evidence for a higher enzymatic activity in the glomerular layer. 215 23

To determine the effect of starvation on brain insulin receptors, rats were fed 4 g of chow/day for 14 days and then P2 fraction membranes were prepared from different brain regions. Compared to the fed state, there was an 18% reduction of insulin binding in olfactory bulbs from starved animals, but no change in the cerebellum, frontal cortex, amygdala, medial hypothalamus or lateral hypothalamus. A 15% reduction of olfactory bulb insulin binding was obtained by totally starving animals for four days. When membrane content was measured using the plasma membrane marker Na/K ATPase, insulin binding decreased by 26% and 14% in olfactory bulb membranes from starved and totally starved animals, respectively. The starvation-induced change in olfactory bulb binding was due to a loss of binding sites and not a decrease in binding affinity. Non-specific catabolism of protein and a change in the composition of membranes following starvation were excluded as causes for this effect. As streptozotocin induced diabetes had no effect on brain insulin binding, it was concluded that hypoinsulinaemia associated with starvation had not caused the reduction in olfactory bulb binding. Under similar conditions of starvation and diabetes, insulin binding in liver plasma membranes increased 26% and 38%, respectively. At 8 and 14 days of starvation, the reductions in olfactory bulb insulin binding and body weight were similar. On refeeding for three days, there was no increase in insulin binding, although body weight increased 7%. On refeeding for eight days, olfactory bulb insulin and body weight had returned to near normal.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of starvation on insulin receptors in rat brain. 274 26


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