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)

The sodium-potassium activated adenosine triphosphatase (NaKATPase) activity of the rat cornea was investigated histochemically using a Pb2+-precipitation technique in which adenosine triphosphate (ATP) is used as substrate and two methods for potassium-dependent para-nitrophenyl-phosphatase (K-NPPase) activity. With all the three techniques used it was demonstrated that the sodium-potassium-activated adenosine triphosphatase (NaK-ATPase) activity is localized in the cell membranes of the endothelium whereas a much weaker activity was observed in the epithelium. When the Pb2+-technique was used, the epithelial cell membranes showed a weaker reaction in the presence of ouabain. This activity was only Mg2+-dependent and was presumably due to an Mg2+-dependent ATPase. The validity of the histochemical techniques for NaK-ATPase activity is discussed. The results emphasize the importance of the endothelium as the main site of Na+ transport in the cornea. Small amounts of the enzyme are also present in the epithelium, which seems to be rich in Mg2+-ATPase. Provided that careful controls are performed, all the methods give consistent results in the cornea.
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PMID:Transport adenosine triphosphatase activity in the rat cornea. 6 3

1. Six rat liver plasma-membrane subfractions of different density and morphological, enzymic and chemical properties were prepared from homogenates by a combination of differential, rate-zonal and density-gradient centrifugation. They consisted of three vesicular 'light' subfractions of density 1.12-1.13 and three 'heavy' subfractions of density 1.16-1.18 containing membrane strips and intercellular junctions. 2. All six subfractions contained a basal adenylate cyclase activity. One of the 'light' subfractions that showed the highest glucagon-stimulated adenylate cyclase activity was identified as deriving form the blood-sinusoidal face of the hepatocyte. This subfraction, unlike the others, was contaminated by Golgi components, as indicated by its morphological properties and the presence of galactosyl- and sialyl-transferase activities. 3. All the six subfractions showed high activities of the following plasma-membrane marker enzymes: 5'-nucleotidase, alkaline phosphodiesterase (nucleotide pyrophosphatase), alkaline phosphatase, leucine naphthylamidase and Mg2+-activated adenosine triphosphatase. A 'light' subfraction that showed the highest specific activities of all the above marker enzymes, but lacked a glucagon-stimulated adenylate cyclase activity, was identified as deriving from the bile-canalicular face of the hepatocyte. 4. The 'heavy' subfractions, which showed generally the lowest activities of the above plasma-membrane enzyme markers, and were characterized by the presence of desmosomes and gap junctions, were taken to originate from the contiguous faces of the hepatocyte. 5. The protein composition of the six subfractions was generally similar, as shown by polyacrylamide-gel electrophoresis. Differences in the amounts of various protein and glycoprotein bands among the subfractions correlated with their morphology, enzymic composition and sialic acid content. 6. Hormonal and histochemical evidence supporting the identification of a bile-canalicular subfraction, a blood-sinusoidal subfraction and contiguous-face subfractions is discussed.
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PMID:Functional polarity of the rat hepatocyte surface membrane. Isolation and characterization of plasma-membrane subfractions from the blood-sinusoidal, bile-Canalicular and contiguous surfaces of the hepatocyte. 12 84

A cytochemical method for the light and electron microscope localization of the K- and Mg-dependent phosphatase component of the Na-K-ATPase complex was applied to rat kidney cortex, utilizing p-nitrophenylphosphate (NPP) as substrate. Localization of K-N-ATPase activity in kidneys fixed by perfusion with 1% paraformaldehyde -0.25% glutaraldehyde demonstrated that distal tubules are the major cortical site for this sodium transport enzyme. Cortical collecting tubules were moderately reactive, whereas activity in proximal tubules was resolved only after short fixation times and long incubations. In all cases, K-NPPase activity was restricted to the cytoplasmic side of the basolateral plasma membranes, which are characterized in these neplron segments by elaborate folding of the cell surface. Although the rat K-NPPase appeared almost completely insensitive to ouabain with this cytochemical medium, parallel studies with the more glycoside-sensitive rabbit kidney indicated that K-NPPase activity in these nephron segments is sensitive to this inhibitor. In addition to K-NPPase, nonspecific alkaline phosphatase also hydrolyzed NPP. The latter could be differentiated cytochemically from the specific phosphatase, since alkaline phosphatase was K-independent, insensitive to ouabain, and specifically inhibited by cysteine. Unlike K-NPPPase, alkaline phosphatase was localized primarily to the extracellular side of the microvillar border of proximal tubules. A small amount of cysteine-sensitive activity was resolved along peritubular surfaces of proximal tubules. Distal tubules were unreactive. In comparative studies, Mg-ATPase activity was localized along the extracellular side of the luminal and basolateral surfaces of proximal and distal tubules and the basolateral membranes of collecting tubules.
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PMID:Transport ATPase cytochemistry: ultrastructural localization of potassium-dependent and potassium-independent phosphatase activities in rat kidney cortex. 12 60

p-Nitrophenyl phosphatase (p-NPPase) activity of (Na+-K+)-activated adenosine triphosphatase ((Na+-K+)-ATPase) on the acinar cells of dog submandibular gland was demonstrated by using light microscopy. The reaction products of p-NPPase of fresh frozen sections were seen to be localized on the basal parts of acini, and disappeared when the sections were incubated in medium containing 10(-3) Mouabain or in a K-free medium. Under the electron microscope, the reaction products of ATPase were found to be localized on the basolateral plasma membrane of both serous and mucous cells. On the microvilli of the luminal plasma membrane of the acinar cell, a small quantity of the reaction products was also present. This localization of ATPase reaction products on the serous and mucous cells seemed to coincide well with that of p-NPPase activity observed on the acini under light microscopy. Possible explanations are given regarding distribution of the above mentioned enzymes in relation to the cation transport of the plasma membrane. Structural and functional asymmetrical properties of acinar cells of the dog submandibular gland are also discussed.
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PMID:Histochemical and cytochemical localization of (Na+-K+)-activated adenosine triphosphatase in the acini of dog submandibular glands. 21 93

The activity of the electrolyte transport enzyme, sodium, potassium-activated adenosine triphosphatase (Na+,K+-ATPase), in the gills of the pinfish, Lagodon rhomboides, increased markedly following transfer of fish from brackish water to seawater. Cytochemical localization of Na+,K+-ATPase via its potassium-dependent phosphatase (K+-NPPase) activity in the branchial epithelium of pinfish adapted to seawater demonstrated that chloride cells are the major sites for the enzyme. Subcellularly, the heaviest depositions of reaction product were observed lining the cytoplasmic membrane surfaces of the labyrinth of anastomosing plasma membrane tubules that ramifies throughout the chloride cell cytoplasm. Enzyme activity was demonstrated also on the cytoplasmic surface of the apical crypt membrane and on the cytoplasmic surfaces of vesicles in the cytoplasm subjacent to the crypt. Deletion of potassium from the cytochemical incubation medium or inclusion of 10 mM ouabain abolished the reaction products associated with these membranes. The significance of these cytochemical results is discussed with reference to current hypotheses of chloride cell function.
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PMID:Ultracytochemical localization of Na+,K+-activated ATPase in chloride cells from the gills of a euryhaline teleost. 21 85

The vector characteristics of the interacting Na+, K+-ATPase and ouabaine were studied in experiments on the restored ghosts of erythrocytes. It is shown that the effect of K+ on the enzyme activity is the same as in cases of using ATP and p-nitrophenylphosphate (p-NPP) as phosphorylating agents. ADP removes the p-NPP induced inhibition with ouabain. This effect is explained rather by addition of ADP to the enzyme substrate centre than by a decrease in the concentration of E1 approximately P phosphoform. Incorporation of labelled orthophosphate into p-nitrophenol (NP) in the presence of Na+, K+-ATPase preparations was not detected. It is shown that antibodies against the fraction of the brain microsomes inhibit K+-NPPases to a much less extent than Na+, K+-ATPase. The digitonin treatment does not remove (Na++ATP)-dependent increase in the K+-NPPase activity. A conclusion is drawn that the mechanisms of p-NPP hydrolysis differs from the mechanism of ATP hydrolysis.
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PMID:[Interaction of p-nitrophenylphosphate with Na+,K+-ATPase]. 22 60

The effects of the cholinergic agonist carbachol (Cch) and guanine nucleotides on the Na,K-ATPase and K-dependent p-nitrophenylphosphatase (K-p-NPPase) activities in rabbit and dog myocardial sarcolemma vesicles in the presence of the pore-forming antibiotic alamethicin (20 micrograms/ml), was studied. Cch (0.01-100 microM) inhibited the both enzymatic activities by 40-45% (IC50 = 0.3-0.5 microM) only after addition of GTP (50 microM) or its analogs: GTP gamma S (0.1-1.0 microM) and Gpp(NH)p (10 microM). The muscarinic acetylcholine receptor (mAchR) antagonist atropine (10 microM) blocked the effect of Cch. GTP gamma S alone produced a concentration-dependent decrease in the both Na,K-ATPase and K-p-NPPase activities by 40-45% (IC50 = 1-2 microM) with a lag period of about 3 minutes; this lag disappeared in the presence of the agonist. The GDP analog GDP beta S (0.01-100 microM) neither affected these activities nor promoted the inhibiting effect of Cch. Pretreatment of sarcolemmal vesicles with 20 micrograms/ml of pertussis toxin in the presence of 100 microM NAD abolished the inhibiting effect of Cch on the Na,K-ATPase and phosphatase activities. Under these conditions pertussis toxin catalyzed the ADP-ribosylation of alpha-subunits of the inhibitory GTP-binding protein (G1) which were identified immunochemically as alpha i2, alpha i3 and, possibly, alpha i1. The data obtained testify to the involvement of G1 in the mAchR-mediated inhibition of myocardial sarcolemmal Na,K-ATPase as well as in the signal transduction from the receptor to the enzyme.
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PMID:[The role of a GTP-binding protein in coupling of a muscarinic cholinergic receptor and Na,K-ATPase in myocardial sarcolemma]. 132 37

We have utilized cobalt-reaction technique for histochemical and cytochemical demonstration of ouabain-sensitive, K(+)-dependent p-NPPase (Na(+)-K(+)-ATPase). The incubation medium consisted of: cobalt chloride, tricine buffer, p-nitrophenylphosphate, KCl, and phenylalanine. Final pH 7.4. Ultracytochemically, reaction products were localized along the internal side of sarcolemma and its vesicles, T-tubule membrane, and capillary endothelial cells. These results suggest that the method is reliable and can be used to investigate the localization of Na(+)-K(+)-ATPase activity.
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PMID:Demonstration of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity in the rat cardiac muscle by cobalt-based cytochemistry. 132

Using extracted human deciduous teeth undergoing physiologic root resorption, this author studied the ultrastructural and cytochemical features of odontoclasts. The scanning electron microscopic observation of trypsin-treated dentin and cementum surfaces of resorption lacunae showed the exposure of collagen fibrils and prominent loss of the peritubular matrices around the dentinal tubules. In the resorption lacunae formed in enamel, there was dissolution of either the rod or the interrod regions. The odontoclasts developed extensive ruffled borders apposed to these resorbing matrices and had round phagosomes containing tannic acid-stainable fine amorphous inclusions, which were identical to those in the extracellular canals of the ruffled borders. The odontoclasts did not phagocytose the collagen fibrils. The odontoclasts showed the enzymatic activities of the acid trimetaphosphatase and acid p-nitrophenyl phosphatase (p-NPPase) in the Golgi-lysosome system, the ruffled border region, and along the resorbing dentin surfaces. The p-NPPase activity was inhibited by sodium tartrate. Also, the odontoclasts showed H(+)-K(+)-ATPase activity in the cytoplasm along the plasma membranes including those of ruffled border and the limiting membranes of the lysosomes. These results suggest that: 1) the odontoclasts are associated with resorption of non-collagenous organic matrices and/or extracellularly-degraded collagenous fragments rather than the incorporation of intact collagen fibrils; 2) the odontoclasts release the hydrolytic enzymes onto the lacunal surfaces and/or the lysosomes for the extra/intracellular degradation of the organic matrices; and 3) they also have H(+)-K(+)-ATPase for extracellular demineralization of the inorganic crystals.
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PMID:Ultrastructural and cytochemical study of the odontoclasts in physiologic root resorption of human deciduous teeth. 132 51

Immunocytochemical localization of protein kinase C (PKC) in rabbit ciliary processes was investigated using anti-PKC monoclonal antibodies (MAbs) against rabbit Types 1, 2, and 3 PKC. Specific immunolabeling was observed in nonpigmented epithelial (NPE) cells and in the capillaries of the ciliary processes with anti-Types 2 and 3 MAbs. No apparent staining was seen with anti-Type 1 MAbs. Immunoelectron microscopy of Types 2 and 3 MAbs revealed a diffuse distribution of immunoreactive PKC in the cytoplasm, in the nucleus, and on the plasma membrane in the NPE cells. When incubated with phorbol 12-myristate 13-acetate (PMA), the distribution of PKC was basically similar to that of the untreated group. However, the labelling density on the plasma membrane at basolateral interdigitation increased considerably for anti-Types 2 and 3 PKC MAbs. In addition, the enzyme cytochemical activity of Na-K-ATPase (ouabain-sensitive K-NPPase) and its change after PMA administration in the ciliary processes were observed. An intense reaction was seen on the basolateral plasma membrane of the NPE cells. In the PMA-treated group, the enzyme activity of Na-K-ATPase apparently was decreased. These findings provide evidence that PKC plays a crucial role in the function of the NPE cells of the ciliary processes, possibly in aqueous humor production.
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PMID:Cytochemistry of protein kinase C and Na-K-ATPase in rabbit ciliary processes treated with phorbol ester. 133 Sep 69


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