Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.14 (ATP synthase)
 7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of interleukin 1, transforming growth factor-beta (coupling factors), prostaglandin E1, and prostaglandin E2 on incorporation of 45Ca2+ and on alkaline phosphatase activity were studied using cultured ROS 17/2.8 cells, one of cell lines derived from rat osteosarcoma. We found that all these factors stimulate both the incorporation of 45Ca2+ and alkaline phosphatase activity of these cells. On the other hand, one of the bone resorption hormones, parathyroid hormone (PTH), suppressed the proliferation of cells and decreased the alkaline phosphatase activity at considerably low concentrations (1 X 10(-12)-1 X 10(-11) M). However, the hormone stimulated the incorporation of 45Ca2+ by these cells in a dose-dependent manner; the maximum stimulation on day 3 was observed at 1 X 10(-7) M and it was approximately 3 times the control value. The data suggest therefore, that the osteoblasts incorporated calcium ions and transported them while bone resorption was occurring. Thus the ROS 17/2.8 cell line appears to be an advantageous experimental system for the study of calcium metabolism of osteoblasts in vitro.
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PMID:[Effects of various factors involved in bone metabolism on 45Ca2+ incorporation and alkaline phosphatase activity of ROS 17/2.8 cells]. 260 4

A protein which specifically binds the amino terminal domain of parathyroid hormone (PTH) on nitrocellulose blots of polyacrylamide gels was fragmented with cyanogen bromide (CNBr), and two fragments were sequenced through 20 residues. The sequence obtained was 100% homologous with the beta-subunit of bovine F1 mitochondrial ATPase. Purified F1 ATPase from bovine heart and Escherichia coli were obtained and the binding of PTH examined on the blots. The beta-subunit of the bovine enzyme bound PTH specifically through its amino terminal domain. However, both the alpha- and beta-subunit of the E. coli enzyme were found to bind the hormone. This binding was also specific for the amino terminal domain of the hormone. The subcellular distribution of the PTH-binding protein from bovine kidney was also examined further. While the mitochondria and plasma membrane appear to possess similar PTH-binding capability, submitochondrial particles enriched in F1 ATPase were also enriched in PTH-binding activity.
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PMID:The beta-subunit of the bovine mitochondrial F1 ATPase specifically binds the amino terminal domain of parathyroid hormone. 290 85

Ca-ATPase is thought to function as a calcium extrusion pump that may regulate cytosolic calcium concentration. Because the parathyroid gland is among the few tissues that are directly regulated by extracellular calcium and because cytosolic calcium may be a mediator of the effects of extracellular calcium on parathyroid hormone secretion, we have investigated the presence of this enzyme in homogenates of parathyroid cells. High performance liquid chromatography (HPLC) was used to quantify the formation of ADP from ATP following incubation of ATP with cellular homogenate in a buffer containing ethylenedioxy- (diethylenedinitrilo) tetra acetic acid (EGTA), ouabain, and calcium. Enzyme activity was calcium-dependent, with Ca-ATPase showing two Km (Ca) values, 31 and 853 nM. High affinity Ca-ATPase activity was reduced by the calmodulin inhibitor, trifluoperazine (TFP), with half-maximal inhibition occurring at 7 X 10(-5) M. Monovalent cations stimulated high affinity Ca-ATPase activity (K+ greater than Na+ greater than Rb+ greater than Li+) in the presence of calcium. Magnesium (0.8 mM) also stimulated cleavage of ATP. Sodium increased Ca-dependent ATPase activity by 82% but had no significant effect on Mg-stimulated activity. Furthermore, azide, an inhibitor of mitochondrial ATPase(s), had a significantly greater inhibitory effect on Mg-dependent than on Ca-dependent activity. In summary, a high affinity Ca-ATPase is present in bovine parathyroid cells which has a Km in the range of the cytosolic calcium concentration that is found in other cells. Ca-ATPase(s) may be of importance in regulating the cytosolic calcium concentration and, therefore, hormonal secretion in this cell type.
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PMID:Ca-ATPase activity in bovine parathyroid cells. 622 2

In an effort to understand the mechanism of action of parathyroid hormone (PTH) on the myocardium, we examined the effect of PTH on the function of isolated heart mitochondria. The hormone inhibited mitochondrial respiration in the presence of malate or beta-hydroxybutyrate but not succinate as substrates. It also inhibited phosphorylation and uncoupled oxidative phosphorylation. These effects of PTH were dose dependent and occurred only in the presence of calcium. A change in calcium concentration from zero to 2 mM did not affect mitochondrial function. PTH also stimulated mitochondrial ATPase. The inhibitory effect of PTH on mitochondrial respiration and on oxidative phosphorylation would result in decreased ATP synthesis and, hence, reduced availability of ATP. Such a sequence of events may provide an explanation for a potential long-term adverse effect of the hormone on the myocardium.
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PMID:Effects of parathyroid hormone on oxidative phosphorylation of heart mitochondria. 716 81