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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In vitro inhibition of adenosine triphosphatase and carbonic anhydrase by several radiographic contrast media and other compounds was measured. The concentrations required for 50% inhibition were, in general, similar to those obtained for other enzymes. The effect of methylglucamine could not be determined for either enzyme because of interference with the assays.
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PMID:Inhibition of adenosine triphosphatase and carbonic anhydrase by contrast media. 12 74

In this study, enzyme activities of the pancreatic appendages of the ductus hepatoPancreas (the so-called "pancreas") in Sepia officinalis L. have been demonstrated by light and electron micicroscopical methods: Malate dehydrogenase, monoamine oxidase, acid phosphatase, beta-glucuronidase, adenosine triphosphatase and carbonic anhydrase were shown by the former, and monoamine oxidase, catalase, glutamic oxalacetic transaminase, choline esterase (non-specific), alkaline phosphatase, acid phosphatase and carbonic anhydrase by the latter technique. The correlation between enzyme activity and distribution, and the presumed function of the two pancreatic epithelia is discussed.
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PMID:The localization of enzyme activities in the pancreatic appendages of Sepia officinalis L. (Cephalopoda). 15 95

The concentration of calcium-binding protein (CaBP) and the activities of calcium adenosine triphosphatase (Ca(2+)-ATPase) and carbonic anhydrase (CA) were determined in the shell gland mucosa of hens in two experiments. In Experiment 1, laying hens on a proprietary layer mash were compared with hens rested from lay by the feeding of whole grain barley. In Experiment 2 comparisons were made of laying hens fed the proprietary layer mash and producing eggs with either strong or weak shells. These latter comparisons were also made when the shell gland was quiescent or active with respect to daily eggshell formation. Feeding whole grain barley reduced egg production to zero after 11 days. This reduction in rate of lay was accompanied by significant reductions in all three markers, the effect on Ca(2+)-ATPase and CaBP being less than for CA. Control values were regained between 10 and 16 days after the barley was replaced with the layer mash. Relative shell strength and the physiological status of the shell gland with respect to time of daily eggshell formation had no significant effect on any marker in Experiment 2.
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PMID:Calcium and carbonate supply in the shell gland of hens laying eggs with strong and weak shells and during and after a rest from lay. 147 May 88

We examined immunohistochemically the localization of three transport enzymes (carbonic anhydrase, Ca-II; sodium-potassium-activated adenosine triphosphatase, NaK-ATPase; bicarbonate-chloride exchanger, band III) in the anterior segment of the human eye. In accord with earlier studies, NaK-ATPase was primarily found in the corneal endothelium, but also in the corneal basal epithelial cell membranes. In addition, immunoreactivity for NaK-ATPase was observed in the non-pigmented epithelium of the ciliary processes and between the two epithelial cell layers. Ca-II immunoreactivity was found in the corneal endothelium as well as in the non-pigmented epithelial layer of the ciliary processes. Interestingly, band III immunoreactivity was found in the corneal endothelium, as similar to Ca-II, but not in the ciliary processes. These results show that, similar to many other tissues, Ca-II and band III immunoreactivities colocalize in the same cytologic site in the human corneal endothelium. Immunocytochemical detection of these key transport enzymes not only gives their accurate and reliable anatomical distribution, but also provides information on the electrolyte transport at these sites.
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PMID:Immunocytochemical localization of carbonic anhydrase, NaK-ATPase and the bicarbonate chloride exchanger in the anterior segment of the human eye. 165 41

Sodium-potassium-stimulated adenosine triphosphatase and carbonic anhydrase isozymes I and II were localized immunocytochemically in adenomas, adenocarcinomas, and normal epithelium of human colon harboring non-neoplastic lesions. Non-neoplastic control colon showed carbonic anhydrase I and II in the cytoplasm of the columnar cells lining the upper half of the crypts. Antiserum to sodium-potassium-stimulated adenosine triphosphatase bound to the basolateral but not the apical plasmalemma of columnar epithelial cells. Staining was most intense in the superficial cells, which also contained carbonic anhydrase, but was also evident to a lesser degree in cells deep in the crypts. Adenomas and adenocarcinomas failed to stain for content of carbonic anhydrase but retained basolateral sodium-potassium adenosine triphosphatase positivity. The staining characteristics of colonic neoplasms for the two enzymes involved in the transport function of colonic epithelium thus resembled those of the less mature cells lining the base of normal crypts.
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PMID:Immunohistochemical localization of sodium-potassium-stimulated adenosine triphosphatase and carbonic anhydrase in human colon and colonic neoplasms. 169 Sep 78

This study was conducted to determine the effect of feeding vitamin D3(D3) metabolites on BW of hen, weight of uterus, plasma Ca, jejunal and uterine adenosine triphosphatase (ATPase), and carbonic anhydrase. At 416 days of age each of 7 groups of laying hens was fed the basal ration supplemented with one of 7 concentrations (micrograms per kg) of D3 or its metabolites as treatments: 0 micrograms of D3; 27.5 micrograms of D3; 3, 5, or 7 micrograms of 1,25(OH)2D3; 5 micrograms of 24,25(OH)2D3; and 5 micrograms of 24,25(OH)2D3 plus 5 micrograms of 1,25(OH)2D3. Treatment effects were compared at various periods after the start of the study. Hens fed the unsupplemented ration had lower (P less than .05) values for all traits than hens fed the D3-supplemented ration by 162 days after the start of treatment. In a comparison of all dietary treatments except the one involving 0 micrograms D3, from 154 to 161 days after the start of the experiment, treatment effects were significant (P less than or equal to .05) for BW, uterine ATPase, and carbonic anhydrase; hens fed 5 micrograms of 24,25(OH)2D3 per kg of ration ranked the lowest of all treatment groups for these traits. Hens fed 27.5 micrograms of D3 and those fed 5 micrograms of 1,25(OH)2D3 per kg of ration did not differ (P greater than .05) for any traits studied. The results suggest that 5 micrograms of 1,25(OH)2D3 per kg of ration can replace 27.5 micrograms of D3 per kg of ration but that 5 micrograms of 24,25(OH)2D3 per kg of ration tends to have a negative effect on physiological systems of the hen.
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PMID:Effects of vitamin D3 metabolites on physiological traits of White Leghorn hens. 217 50

With immunocytochemistry, we have determined distribution of sodium, potassium-adenosine triphosphatase (Na+, K+-ATPase) and of three isoenzymes of carbonic anhydrase (CA) and have shown absence of the chloride channel, Band 3 protein, in the genital tract of female rodents. Staining for Na+,K+-ATPase was strongest in the ampullary oviduct and uterine glands in the mouse. In the mouse and rat ovary, immunostaining evidenced CA I, II, and III in theca interna cells where the enzyme could affect the pH of follicular fluid. The zona pellucida of the ovary and cytoplasmic foci in follicular granulosa cells stained for content of only CA I in mouse ovary, suggesting synthesis of a zona pellucida component by granulosa cells. CA II in mouse oviductal epithelium increased from the negative infundibulum to the variably positive ampulla and isthmus to the uniformly positive interstitial segment. The content of CA III varied inversely to that of CA II. The prevalence of CA II-positive cells apparently corresponded with that of nonciliated cells, whereas abundance of CA III-positive cells concurred with that of ciliated cells in regions of the mouse oviduct. The rat oviduct lacked CA II but, like that of the mouse, showed CA III in the proximal region. The staining for CA II in surface epithelium exceeded the reactivity in glandular epithelium in the mouse uterus, except during estrus. In contrast, rat uterus evidenced CA II in glandular but not surface epithelium. These results testify to possible significance of various ion transport mechanisms for biologic activities of diverse cells in the female genital tract.
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PMID:Immunocytochemistry of ion transport mediators in the genital tract of female rodents. 245 38

A method is described for histological localization of carbonic anhydrase (CA) in sections of frozen human muscle using the rapid and inexpensive histochemical technique of Hansson. Results obtained in normal subjects indicate clearly that CA reactive fibers are of type 1. Similarly, abnormalities seen with CA in the muscle biopsy of a patient presenting with type 1 fiber hypotrophy and preponderance duplicated almost exactly those observed with the actinomyosine adenosine triphosphatase and the reduced nicotinamide adenine dinucleotide dehydrogenase reactions. Observations of grouped CA-positive muscle fibers in a case of chronic neurogenic atrophy suggest that, like other enzymes, CA expression in muscle is under neurogenic control.
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PMID:Histochemical localization of carbonic anhydrase in normal and diseased human muscle. 296 57

The formation of aqueous humour by the ciliary body is a complex process. Active transport of solutes by the ciliary process epithelium is an energy-dependent mechanism that selectively transports substances against an electrochemical gradient across the cell membranes. Water passively follows the active solute transport. In addition to these active transport processes, ultrafiltration contributes to the formation of aqueous humour. The ciliary epithelium contains enzyme systems that function in the production of aqueous humour. The enzymes sodium-potassium-activated adenosine triphosphatase [(Na+:K+)ATPase] and carbonic anhydrase participate in the active transport across this epithelium. Inhibition of these enzymes lowers intraocular pressure (IOP) by decreasing aqueous humour production. the ciliary epithelium contains both alpha- and beta-adrenergic receptors. Electrophysiologic studies on the isolated iris-ciliary body (I-CB) preparation provide a means to study direct effects of the adrenergic agents on transepithelial properties of the ciliary epithelium. This paper will discuss the enzymatic and adrenergic properties of the ciliary epithelium as they relate to active transport and thereby aqueous humour production.
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PMID:Aqueous production. 302 67

To study whether a proton pump is an integral part of the mechanism responsible for secretin-dependent biliary secretion of HCO-3 ions, the proton pump inhibitor N,N'-dicyclohexylcarbodiimide (DCCD) was systemically administered to six anesthetized, secretin-infused pigs. Because biliary HCO-3 secretion varies with arterial pH, secretion rate was measured at several different arterial pH values, before and after DCCD (25 mumol/kg). At arterial pH 7.45, bile flow was 2.1 (1.6-2.9) ml/min, and HCO-3 secretion was 224 (157-311) mumol/min. DCCD reduced bile flow and HCO-3 secretion by 30% and 40%, respectively, independent of arterial pH. In contrast, bile acid secretion, 46 (41-59) mumol/min, was not changed by DCCD. The hepatic adenosine triphosphatase (ATP) level, 2.0 (1.8-2.1) mumol/g wet tissue, was not changed by DCCD. DCCD (10(-4) mol/l) affected neither Na,K-ATPase nor carbonic anhydrase activities in separate in vitro assay systems. The reduction in biliary HCO-3 secretion induced by the proton pump inhibitor DCCD may indicate that a proton pump is integrated into the mechanism responsible for secretin-dependent biliary secretion of HCO-3.
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PMID:DCCD (N,N'-dicyclohexylcarbodiimide) inhibits biliary secretion of HCO-3. 303 16


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