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)

We have recently shown the presence of receptors for 1,25-dihydroxyvitamin D3 and that 1,25-dihydroxyvitamin D3 stimulates Ca-ATPase in vascular smooth muscle cells presumably via receptor mediated mechanism. These data suggest that the sterol may directly be involved in the regulation of cellular calcium homeostasis. To further define action of vitamin D in smooth muscle cells, we studied effect of the sterol on cellular uptake of calcium. 1,25-dihydroxyvitamin D3 stimulated 45Ca2+ uptake by cultured cells, A7r5, derived from fetal rat aorta, when the cells were incubated with the sterol for 18 hr. The effect was dose-dependent at 10(-10) to 10(-9) M, and three orders of magnitude higher concentration of 25-hydroxyvitamin D3 or 24,25-dihydroxyvitamin D3 was needed to obtain similar effects. Furthermore, the effect of 1,25-dihydroxyvitamin D3 was abolished by cycloheximide (10(-5) M), a protein synthesis inhibitor. These data clearly suggest that 1,25-dihydroxyvitamin D3 may directly regulate cellular calcium homeostasis in vascular smooth muscle cells presumably via receptor mediated mechanism.
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PMID:1,25-Dihydroxyvitamin D3 stimulates 45Ca2+-uptake by cultured vascular smooth muscle cells derived from rat aorta. 283 86

The in vivo effect of vitamin D on (Ca2+ + Mg2+)-ATPase activity was examined in a plasma membrane fraction of rat circulating mononuclear cells (MPM). Although there was no significant difference in the ATPase activities in red blood cell ghosts, (Ca2+ + Mg2+)-ATPase activity in MPM was significantly higher (p less than 0.05) in long-term vitamin D3-replete rats (100 IU/day for 6 months) than that in vitamin D-deplete rats (for 6 months). In rats maintained on vitamin D-deficient diets for 5-7 weeks, in vivo administration of either vitamin D3, 2,000 IU orally, 5 days prior to killing or 1,25-dihydroxyvitamin D3, 2.4 nmol, intraperitoneally, 24 h prior to killing failed to show any significant effect on (Ca2+ + Mg2+)-ATPase activity in MPM. (Ca2+ + Mg2+)-ATPase activity in MPM from rats maintained on vitamin D-deficient diet with high calcium content (1.8%) was significantly higher (p less than 0.05) than that from rats maintained on vitamin D-deficient diet with low calcium content (0.3%). Moreover, in vitro addition of vitamin D3 metabolites did not show any effect on (Ca2+ + Mg2+)-ATPase activity in MPM. These data suggest that decreased (Ca2+ + Mg2+)-ATPase activity in MPM from long-term vitamin D-deplete rats resulted from an adaptation to low extracellular calcium rather than vitamin D depletion.
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PMID:(Ca2+ + Mg2+)-ATPase activity in plasma membrane of circulating mononuclear cells. Lack of a direct effect of vitamin D. 293 94

The vitamin D-dependent, calcium-binding protein from rat kidney, calbindin D28k (renal CaBP) specifically stimulates Ca,Mg-ATPase activity of human erythrocyte plasma membranes in a dose-dependent, calcium-sensitive manner. This stimulation was about two-fold compared to a three-fold stimulation by calmodulin. The effect was specific since other calcium-binding proteins and low molecular weight proteins did not stimulate Ca,Mg-ATPase activity. Renal CaBP did not stimulate cyclic nucleotide phosphodiesterase at concentrations greater than those which stimulated Ca,Mg-ATPase activity. This is the first report of a specific in vitro effect of renal CaBP on an enzyme system.
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PMID:Specific in vitro activation of Ca,Mg-ATPase by vitamin D-dependent rat renal calcium binding protein (calbindin D28K). 294 79

I have recently shown that a vascular smooth muscle cell line has receptors for 1,25-dihydroxyvitamin D. To examine a possible role of 1,25-dihydroxyvitamin D in the regulation of cellular calcium homeostasis, effect of the sterol on Ca-ATPase activity was studied. 1,25-dihydroxyvitamin D3 stimulated the enzyme activity in a dose dependent manner at 10(-10) and 10(-9) M when the cells were incubated with the sterol for 10 hours. By contrast, 60 minutes incubation of the cells with 1,25-dihydroxyvitamin D failed to stimulate the enzyme activity. Both 25-dihydroxyvitamin D3 and 24,25-dihydroxyvitamin D3 did stimulate the enzyme activity, but at three orders of magnitude higher concentrations. Cycloheximide, at 10(-5)M, abolished the action of 1,25-dihydroxyvitamin D3. These data suggest that 1,25-dihydroxyvitamin D3 stimulates Ca-ATPase activity probably via its receptor and may play a role in regulating cellular calcium homeostasis.
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PMID:1,25-Dihydroxyvitamin D3 stimulates Ca-ATPase in a vascular smooth muscle cell line. 296 32

The influence of vitamin D and C deficiency on the kinetic parameters of sucrase and alkali phosphatase activities was studied in the microsomal fraction of the small intestinal mucosa of guinea pigs. It was found that Km values for these enzymes did not depend on the animal providing with these vitamins. Deficiency of one of these vitamins did not influence sucrase activity, however, simultaneous elimination of vitamins D and C resulted in the activity rise by 92%. Alkali phosphatase and Ca-ATPase activities proved to be similarly dependent on providing with vitamin D in the presence of vitamin C in the ration, while in the absence of vitamin C this dependence was not observed.
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PMID:[Enzymatic activity of the microsomal fraction of the mucosa of the small intestine in guinea pigs with vitamin D and C deficiencies]. 296 18

The system of renal Ca transport in the rat is modeled in terms of two classes of processes: a nonsaturable flux that predominates in the proximal tubule, and an active, vitamin D-dependent flux with major expression in the distal convoluted tubule. There transport is against an electrochemical gradient, with much of the efflux probably mediated by the Ca/Mg-ATPase. Calculations of the rate of free Ca diffusion in tubular cells indicate that an unaided flux would be only one-seventy-seventh of that found experimentally. It is suggested that the vitamin D-induced renal calcium binding protein, CaBPr, Mr approximately 28,000, in raising total cellular calcium by three orders of magnitude, increases the transcellular Ca flux and thus the free intracellular Ca ion concentration at the basolateral pole, allowing the Ca/Mg-ATPase to function near its maximum. Analysis of the rate of nonsaturable Ca flux throughout the kidney tubule suggests a paracellular pathway via bulk flow, following water that is driven osmotically. Evaluation of whole animal data in terms of these two classes of calcium fluxes indicates that our model is consistent with experimental observations and assigns a functional role to active calcium transport.
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PMID:CaBPr facilitates intracellular diffusion for Ca pumping in distal convoluted tubule. 297 Aug 2

The migration of intestinal epithelial cells from the crypts to the tips of villi is associated with progressive cell differentiation. The changes in Ca2+-ATPase activity and ATP-dependent Ca2+-transport rates in basolateral membranes from rat duodenum were measured during migration along the crypt-villus axis. In addition, vitamin D-dependent calcium-binding protein and calmodulin content were measured in homogenates of six cell populations which were sequentially derived from villus tip to crypt base. Alkaline phosphatase activity was highest at the tip of the villus (fraction I) and decreased more than 20-fold towards the crypt base (fraction VI). (Na+ + K+)-ATPase activity also decreased along the villus-crypt axis but in a less pronounced manner than alkaline phosphatase. ATP-dependent Ca2+-transport in basolateral membranes was highest in fraction II (8.2 +/- 0.3 nmol Ca2+/min per mg protein) and decreased slightly towards the villus tip and base (fraction V). The youngest cells in the crypt had the lowest Ca2+-transport activity (0.9 +/- 0.1 nmol Ca2+/min per mg protein). The distribution of high-affinity Ca2+-ATPase activity in basolateral membranes correlated with the distribution of ATP-dependent Ca2+-transport. The activity of Na+/Ca2+ exchange was equal in villus and crypt basolateral membranes. Compared to the ATP-dependent Ca2+-transport system, the Na+/Ca2+ exchanger is of minor importance in villus cells but may play a more significant role in crypt cells. Calcium-binding protein decreased from mid-villus towards the villus base and was undetectable in crypt cells. Calmodulin levels were equal along the villus-crypt axis. It is concluded that vitamin D-dependent calcium absorption takes primarily place in villus cells of rat duodenum.
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PMID:Distribution of Ca2+-ATPase, ATP-dependent Ca2+-transport, calmodulin and vitamin D-dependent Ca2+-binding protein along the villus-crypt axis in rat duodenum. 299

Transplacental movement of calcium from mother to fetus is essential for normal fetal development. In most species, fetal plasma calcium levels are higher than maternal levels at term. The role of cholecalciferol metabolites, with specific emphasis on 1,25-dihydroxycholecalciferol (1,25(OH)2D), in placental calcium transport and maintenance of the fetomaternal gradient has been extensively investigated. In rats, there is not an absolute demand for 1,25(OH)2D for maintenance of fetal calcium homeostasis in utero, even though it is essential for maintenance of maternal plasma calcium levels. However, in sheep, the absence of 1,25(OH)2D results in disruption of both maternal and fetal calcium homeostasis. It is known that rat and human placentas contain specific cytosolic binding proteins for 1,25(OH)2D that are similar to the well-characterized intestinal receptor. Two calcium-binding proteins (CaBP) have been detected in rat and human placentas: a protein immunologically identical to the vitamin D-dependent CaBP and a calcium-dependent ATPase. The levels of CaBP in rat placenta have been shown to increase in response to exogenously administered 1,25(OH)2D but cannot be obliterated with maternal vitamin D deficiency. No relationship has been shown between 1,25(OH)2D and placental Ca-ATPase in any species. Thus, the mechanism of action of 1,25(OH)2D in maintenance of the transplacental calcium gradient in sheep is unknown. In the pregnant rat (and perhaps human), 1,25(OH)2D is a critical factor in the maintenance of sufficient maternal calcium for transport to the fetus and may play a role in normal skeletal development of the neonate.
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PMID:Cholecalciferol and placental calcium transport. 301 69

The proximal tubule is the target site for parathyroid hormone (PTH), and conversion of 25(OH)vitamin D3 hormones which impinge on calcium (Ca) homeostasis, as well as a major site for sodium (Na) reabsorption. The effect of changes in PTH and vitamin D status on Na,K-ATPase activity, as a measure of Na transport, were studied in the proximal tubules of adult rat kidneys where Na and Ca reabsorption rates are in parallel. Na,K-ATPase activity and 25(OH)D3 metabolism were determined in cortical and juxtamedullary proximal tubule segments from normal, parathyroidectomized (PTX), and vitamin D-deficient (-D) rats. Na,K-ATPase activity was highest in cortical segments. PTX led to a decrease in activity in convoluted segments but increased activity in straight segments. In -D rats, Na,K-ATPase activity decreased in cortical segments but increased in juxtamedullary segments. 25(OH)D3 was metabolized more to 24,25(OH)2D3 than to 1,25(OH)2D3 in all normal segments. Juxtamedullary segments were more sensitive to PTX and -D conditions. These findings suggest that cortical and juxtamedullary nephrons are inherently different in basal Na,K-ATPase activity, in conversion of 25(OH)D3 to active metabolites, and in response to altered PTH and vitamin D3 status.
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PMID:Na,K-ATPase activity and 25(OH)vitamin D3 hydroxylation in rat proximal tubules. 302 30

Renal proximal tubule cells adapt to dietary phosphate (Pi) restriction by increasing Pi transport independent of parathyroid hormone, vitamin D metabolites, or serum Ca2+. To determine the underlying cellular mechanism(s), brush border (BBM) and basolateral membranes (BLM) were isolated from growing male rats fed a synthetic diet containing variable levels of Pi (0.1-1.4%). Dietary Pi restriction was without effect on either BBM or BLM total lipid phosphorus, individual phospholipid species, or BLM Na+-K+-ATPase specific activity. However, dietary Pi restriction (0.1 vs. 1.0%) did cause a significant reduction in BBM but not BLM cholesterol (0.45 vs. 0.41 mumol/mg protein). Brush border membrane cholesterol was inversely correlated with the tubular reabsorption of Pi (r = 0.77, P less than 0.01) over a broad range (99.9-46.2%). Arrhenius analysis of two intrinsic BBM enzymes revealed a significant reduction in the breakpoint temperature for alkaline phosphatase but no change for Mg2+-ATPase. Fluorescence polarization studies showed increased BBM inner core fluidity due to an alteration in neutral lipids but not phospholipid, fatty acid, or protein membrane components. These data demonstrate that the BBM can regulate its cholesterol content independent of the BLM. Furthermore, they suggest that adaptation to dietary Pi restriction involves a reduction in BBM cholesterol, which may be mediated by an increase in membrane fluidity.
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PMID:Renal apical membrane cholesterol and fluidity in regulation of phosphate transport. 316 Feb 47


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