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 calcium demands of pregnancy and lactation are known to up-regulate intestinal calcium absorption. Intestinal epithelial cells contain calcium ATPases and calcium binding proteins, which are believed to play important roles in intestinal calcium transport. However, the possible role of these two proteins in the up-regulation of intestinal calcium absorption observed in pregnancy and lactation is unknown. In this study, intestinal calcium ATPase (PMCA1), calcium binding protein (9K) (CaBP-9K), and vitamin D receptor (VDR) messenger RNA (mRNA) levels were determined by Northern analysis at different stages of pregnancy and early lactation in rats. Intestinal calcium ATPase and calcium binding protein mRNA levels did not differ significantly among nonpregnant rats and rats pregnant for 7 or 14 days. However, at 21 days gestation both calcium ATPase and calcium binding protein mRNA levels increased 2- to 3-fold. Calcium ATPase and calcium binding protein mRNA remained elevated at 7 days of lactation. Plasma 1,25-dihydroxyvitamin D3 (1,25-D3) concentration exhibited a similar pattern, rising markedly at 21 days gestation and remaining elevated in lactation. VDR mRNA levels did not change during the entire experiment. However, intestinal VDR content increased 2-fold in late pregnancy and lactation. These data suggest that transcription of calcium absorption factors is increased in late gestation and early lactation, perhaps mediated by increased plasma 1,25-dihydroxyvitamin D3 concentrations, and that the effects of gestation and lactation on VDR concentrations are probably posttranscriptional.
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PMID:Pregnancy and lactation increase vitamin D-dependent intestinal membrane calcium adenosine triphosphatase and calcium binding protein messenger ribonucleic acid expression. 968 3

The ECL cells are peptide hormone-producing cells, rich in histamine and chromogranin A (CGA)-derived peptides, that operate under the control of gastrin. Gastrin and the ECL cells form a functional unit, the gastrin-ECL-cell axis. The aims of the present study were to examine (1) if calcitonin (CT), parathyroid hormone (PTH) and vitamin D affect the gastrin-ECL-cell axis (by measuring the activity of the histamine-forming enzyme, histidine decarboxylase (HDC), and the expression of HDC mRNA and CGA mRNA in the ECL cells), and (2) if activation of the gastrin-ECL-cell axis affects the parathyroid glands (by measuring plasma PTH and mRNA expression). We also examined the possibility that the oxyntic mucosa harbours vitamin D receptors. Fasted rats received intravenous infusion of PTH and CT with or without gastrin. PTH raised the blood Ca2+ concentration, whereas CT infusion lowered it. Plasma PTH rose in response to CT, while serum gastrin remained unaffected. ECL-cell HDC was activated by gastrin but not by CT and PTH. Five daily subcutaneous injections of large amounts of ergocalciferol raised the blood Ca2+ concentration, while reducing the oxyntic mucosal HDC activity and the expression of HDC and CGA mRNA. The serum gastrin concentration was not affected. The findings are in line with the idea that the gastrin-ECL-cell axis can be suppressed by vitamin D or by vitamin D-dependent mechanisms. Western blot analysis revealed the presence of vitamin D receptor immunoreactivity and reverse transcription PCR detected vitamin D receptor gene expression in the rat oxyntic mucosa. Hypergastrinemia was induced by daily peroral treatment with the H+/K+-ATPase inhibitor, omeprazole, for 2 weeks or by continuous subcutaneous infusion of gastrin for 7 days. Elevated serum gastrin concentration was associated with increased HDC activity and increased HDC and CGA mRNA expression in the oxyntic mucosa. There was no elevation of plasma PTH or PTH mRNA expression in the parathyroid gland.
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PMID:Rat stomach ECL-cell histidine decarboxylase activity is suppressed by ergocalciferol but unaffected by parathyroid hormone and calcitonin. 1010 Sep 26

Chick kidney and brain were analyzed for the subcellular distribution (if any) of a putative plasma membrane receptor for 1,25-dihydroxyvitamin D3 [1,25(OH)2D3]. Fractionation protocols were found to be based not only on differential centrifugation conditions, but also gentleness of resuspension procedures, and sufficiently dense Percoll gradients. The postnuclear pellets were resolved on 21.85% Percoll gradients overlayed on 2.4 M sucrose cushions. For both kidney and brain, fraction 1 (bottom of tube) was found to be enriched over whole homogenate 5.4- and 1.6-fold, respectively, in acid phosphatase activity, fractions 2 through 5 were enriched four- and eightfold, respectively, in succinate dehydrogenase activity, fraction 8 contained Golgi, as judged by a small peak of alpha-mannosidase activity, and fraction 9 was enriched sevenfold (for each tissue) in Na+,K+-ATPase activity. Western analyses, using a characterized antibody to the putative chick intestinal plasma membrane vitamin D receptor, revealed the highest levels of antigenicity in both chick kidney and brain in plasma membrane and Golgi fractions, followed by unidentified membranes in fractions 6 and 7 of Percoll gradients. Distribution of specific binding of [3H]1,25(OH)2D3 in Percoll gradient fractions paralleled that of antigenicity. Qualitatively, kidney plasma membrane contained more antigen than brain plasma membrane after Western blot analyses; these results were mirrored by differences in specific binding of the tritiated secosteroid (65 +/- 14.5 and 34 +/- 11.9 fmol/mg of protein, respectively).
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PMID:Immunochemical studies on the putative plasmalemmal receptor for 1,25-dihydroxyvitamin D3 II. Chick kidney and brain. 1049

Previously recognized intracellular proteins with an affinity for vitamin D metabolites include the vitamin D receptor and the cytochrome P-450-based vitamin D metabolizing mixed-function oxidases. We recently characterized a third set of high-capacity, intracellular vitamin D binding proteins (IDBPs) in the inducible heat shock protein-70 (hsp-70) family. Here we report the cloning and expression of cDNAs coding for two IDBPs. The full-length cDNAs for IDBP-1 and IDBP-2 demonstrated 95% and 94% nucleotide homology, respectively, with the cDNAs for human constitutively expressed heat shock protein 70 (hsc-70) and hsp-70. Transient expression of the IDBP cDNAs in a vitamin D-responsive primate cell line increased extractable 25-hydroxylated vitamin D metabolite-IDBP-binding 25-fold. Transfection experiments also demonstrated that the majority of the constitutively expressed 25-hydroxylated vitamin D metabolite binding activity was attributable to expression of the hsc-70-related IDBP-1 and that metabolite binding activity sublocalized to the highly conserved ATP-binding/ATPase domain of hsp-70s. Stable overexpression of IDBP-1 in wild-type cells enhanced vitamin D-directed responsiveness of endogenous vitamin D-24-hydroxylase, osteopontin, and osteocalcin genes by several-fold over that observed in cells transfected with an empty vector. These results suggest that IDBP-1 facilitates the intracellular localization of active vitamin D metabolites and vitamin D receptor-mediated transactivation.
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PMID:Intracellular vitamin D binding proteins: novel facilitators of vitamin D-directed transactivation. 1097 17

The physiological mechanisms by which essential fatty acids (EFAs) affect calcium (Ca(2+)) retention is not clear, but suggestions have included changes in membrane fluidity, receptor modulation and induction of second messengers. The vitamin D receptor (VDR) is essential for the functioning of 1,25(OH)(2)D(3)which increases Ca(2+)absorption. Activity of the intestinal basolateral membrane (BLM) Ca(2+)ATPase correlates with the degree of Ca(2+)absorption. Therefore, changes in ATPase activity and VDR availability due to EFAs may influence calcium retention. We have investigated the effect of long-term dietary supplementation with EFAs on Ca(2+)ATPase activity (measured colourimetrically) and VDR availability (measured with the ELISA technique) after the loss of oestrogen induced by ovariectomy (OVX) in female Sprague Dawley rats. Control animals underwent anaesthesia and a surgical procedure but the ovaries were left intact (sham). Ca(2+)ATPase activity was significantly lower in OVX animals than in the intact animals (P<0.05) and following supplementation with EFAs, was significantly higher than in sham controls (P<0.05). A higher number of VDR was measured after OVX and declined due to EFA supplementation; these differences in activity of the ATPase and number of receptors could be ascribed to membrane changes due to EFA supplementation, feedback control by serum calcium or the direct influence of the EFAs.
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PMID:Modulation of intestinal vitamin D receptor availability and calcium ATPase activity by essential fatty acids. 1133 49

The expression of calcitropic genes and proteins was localized within murine placenta during late gestation (the time frame of active calcium transfer) with an analysis of several gene-deletion mouse models by immunohistochemistry and in situ hybridization. Parathyroid hormone-related protein (PTHrP), the PTH/PTHrP receptor, calcium receptor, calbindin-D(9k), Ca(2+)-ATPase, and vitamin D receptor were all highly expressed in a localized structure of the murine placenta, the intraplacental yolk sac, compared with trophoblasts. In the PTHrP gene-deleted or Pthrp-null placenta in which placental calcium transfer is decreased, calbindin-D(9k) expression was downregulated in the intraplacental yolk sac but not in the trophoblasts. These observations indicated that the intraplacental yolk sac contains calcium transfer and calcium-sensing capability and that it is a probable route of maternal-fetal calcium exchange in the mouse.
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PMID:Calcitropic gene expression suggests a role for the intraplacental yolk sac in maternal-fetal calcium exchange. 1183 78

Chaperone proteins in the heat shock protein-70 family possess endogenous ATP binding and ATPase activity and interact with intracellular protein substrates in an ATP-dependent manner; the hydrolysis of ATP to ADP results in an increase in the affinity of the chaperone for protein substrates. Heat shock protein-70s can also specifically interact with 25-hydroxylated vitamin D metabolites. Using constitutively expressed heat shock protein-70 (hsc70) as chaperone, here we demonstrate that vitamin D metabolite binding to hsc70 is also ATP dependent. Transient overexpression of an hsc70-green fluorescent protein chimeric construct in primate kidney cells resulted in a 6-fold increase in specific, extractable 25-hydroxyvitamin D(3) binding. When ATPase capability of hsc70 was disabled, this increase was completely blocked. In solution, the binding of 25-hydroxylated vitamin D metabolites to hsc70 was significantly increased (P < 0.01) in the presence of ATP and a nonmetabolizable ATP analog. The ATP-directed increase in specific binding resulted from an increase in the abundance of relatively high-affinity hormone-binding sites (K(d), approximately 0.24 nM). These results suggest that ATP hydrolysis to ADP would favor the release of vitamin D from a donor hsc70 molecule at a time when an hsc70-bound acceptor protein substrate is anchored to the chaperone with relative avidity. We theorize that the endogenous ATPase activity of hsc70 promotes the transfer of vitamin D sterols to other intracellular vitamin D binding proteins, such as the vitamin D receptor and vitamin D hydroxylases, to which hsc70 is known to bind.
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PMID:Adenosine 5'-triphosphate-dependent vitamin D sterol binding to heat shock protein-70 chaperones. 1614 93

Bufalin, a bufadienolide type cardiotonic steroid that is one of the major components of the toad venom-prepared traditional Chinese medicine called Ch'an Su or Senso, exhibits a cardiotonic action by inhibiting the membranous Na(+),K(+)-ATPase. Bufalin also induces differentiation of leukemia cells alone or in combination with other differentiation inducers including 1alpha,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)]. In this study, we performed a transient cotransfection assay using a vitamin D receptor (VDR) expression vector and a luciferase reporter and found that although bufalin did not transactivate the VDR, it effectively enhanced VDR activity induced by 1,25(OH)(2)D(3). Bufalin also augmented VDR activation by bile acid ligands, such as lithocholic acid and 3-ketocholanic acid. Other cardiotonic steroids including ouabain, digitoxigenin and cinobufagin did not enhance VDR activation. Bufalin did not bind directly to VDR but did modulate the interaction of VDR and cofactors, such as steroid receptor coactivator-1 and nuclear receptor corepressor. Bufalin treatment significantly increased the expression of an endogenous VDR target gene, CYP24, in kidney- and monocyte-derived cell lines treated with 1,25(OH)(2)D(3). The data indicate that bufalin-mediated cellular mechanisms such as interaction with Na(+), K(+)-ATPase may affect VDR transcriptional activity. Bufalin may be a useful tool in the investigation of VDR regulation by membrane-originating cellular signals and of pathophysiological mechanisms linking VDR to cardiovascular dysfunction.
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PMID:Enhancement of ligand-dependent vitamin D receptor transactivation by the cardiotonic steroid bufalin. 1618 38

Intestinal epithelial cells contain calcium-binding proteins and Ca2+-transporting adenosine triphosphatase (Ca2+-ATPase), which play important roles in intestinal Ca transport. However, the factors that affect the expression of these transepithelial Ca-transporting proteins in dairy cattle are unknown. In this study, a semi-quantitative reverse transcription polymerase chain reaction was used to determine the expression of the mRNAs for intestinal Ca-binding protein calbindin-D9k (CaBP9k), two isoforms of plasma membrane Ca2+-ATPase (PMCA1 and PMCA4), and vitamin D receptor (VDR) in duodenal tissue samples from 20 non-lactating, non-pregnant Holstein dairy cattle (0.4-135.9 months old). The correlations between the expressions of transepithelial Ca-transporting proteins, the ages of the cattle, and the presence of several plasma components were evaluated. The duodenal CaBP9k mRNA content had a significant negative correlation with age and positive correlations with plasma inorganic phosphorus (iP) and 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) concentrations. The PMCA1 mRNA content was negatively correlated with the plasma Ca concentration. The duodenal PMCA4 mRNA content was correlated negatively with the plasma iP. The VDR mRNA content had a positive correlation with the plasma magnesium concentration.
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PMID:The expression of genes for transepithelial calcium-transporting proteins in the bovine duodenum. 1649 Jul 22

Clinical observations show that an increase in serum inorganic phosphorus (Pi) is linked to higher cardiovascular (CV) mortality, while vitamin D receptor (VDR) agonist therapy is associated with survival benefit in stage 5 chronic kidney disease. Smooth muscle cells (SMCs) play an important role in CV pathophysiology, but the interaction between Pi and the VDR signaling pathway in SMCs is not known. Real-time RT-PCR studies revealed that elevated Pi (2.06 mM) modulated VDR-mediated regulation of a panel of genes including thrombomodulin and osteopontin in SMCs. DNA microarray results demonstrated that increasing Pi from 0.9 to 2.06 mM exerted a widespread modulating effect on VDR-mediated gene expression. A total of 325 target genes were affected by paricalcitol at 0.9 mM Pi, with 195 up- and 130 downregulated. The number of target genes affected by paricalcitol at 2.06 mM Pi decreased to 86, with 55 up- and 31 downregulated. VDR-mediated gene expression in As4.1 cells (a juxtaglomerular cell-like cell line derived from kidney tumors in SV40 T-antigen transgenic mice) and peroxisome proliferator-activated receptor (PPAR)gamma-mediated gene expression in SMCs were also altered by elevated Pi, suggesting that the observation is not unique to VDR in SMCs. Mechanism analysis showed that elevated Pi had no significant effect on VDR or PPARgamma protein level but altered the cytosolic vs. nuclear distribution of NF-kappaB or nuclear receptor corepressor 1 (NCoR1). Our results demonstrate for the first time that elevated Pi affects VDR-mediated gene expression in human coronary artery SMCs and the effect is not limited to VDR in SMCs.
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PMID:Elevated phosphorus modulates vitamin D receptor-mediated gene expression in human vascular smooth muscle cells. 1771 59


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