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)

While Western blot analysis clearly revealed the presence of the alpha- and beta-subunits of Na(+)-K(+)-ATPase in a variety of rat tissues, beta was not readily detectable in liver. This observation was consistent with a previous report indicating that Na(+)-K(+)-ATPase immunoprecipitated from rat liver gives no clear evidence for the presence of a beta-subunit (Hubert et al. Biochemistry 25: 4156-4163, 1986). However, Western blot analysis of density gradient-purified lamb and rat liver microsomes showed the presence of a protein with an approximate molecular mass of 42 kDa that was immunoreactive with beta-specific polyclonal antibodies as well as beta-directed monoclonal antibodies. Deglycosylation of this protein by N-glycosidase F generated a core protein (beta c, M(r) approximately 32,000) that had the identical electrophoretic mobility as the beta c protein of the purified kidney enzyme. Isoform-specific monoclonal and synthetic peptide-directed polyclonal antibodies were used to demonstrate the presence of only the alpha 1- and beta 1-proteins in the liver and the presence of beta 2 in rat brain. Functional studies then showed that although both rat and lamb liver enzymes had sensitivities to cardiac glycoside inhibition similar to that of their corresponding kidney enzyme, the lamb liver enzyme had higher affinities for Na+, K+, and ATP than the kidney enzyme.
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PMID:Determination of Na(+)-K(+)-ATPase alpha- and beta-isoforms and kinetic properties in mammalian liver. 131 75

Isoform 4b of the human plasma membrane Ca2+ pump was expressed in COS cells and in the baculovirus system (Sf9 cells). A 105-kDa pump fragment lacking the first two transmembrane domains and the so-called transduction domain was also expressed. The expression level was 2-4 times the background in COS cells and at least 7 times in the baculovirus system. Tests on membranes from both systems showed that the expressed pump was active. The expressed pump and the 105-kDa fragment were isolated from Sf9 cell membranes by calmodulin affinity chromatography. The pump had Ca(2+)-dependent ATPase activity with a calmodulin stimulation factor of 3, formed a La(3+)-stabilized phosphoenzyme, and had a KM (Ca2+) in the presence of calmodulin of about 1 microM. The 105-kDa fragment, assayed by the phosphoenzyme test on COS or Sf9 cell membranes or by ATPase measurements after isolation from Sf9 cells, proved inactive. Laser confocal microscopy on Sf9 cells showed that both the pump and the 105-kDa fragment were apparently associated with the plasma membrane. The expressed pump in COS and Sf9 cells and the endogenous pump in a number of other cell lines had a slower gel mobility (i.e. a higher apparent molecular mass) than the erythrocyte pump.
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PMID:Expression, purification, and properties of the plasma membrane Ca2+ pump and of its N-terminally truncated 105-kDa fragment. 133 59

The expression pattern of the multiple isoforms of Na,K-ATPase was examined in the human heart. Isoform specific oligonucleotide probes for the alpha 1, alpha 2, alpha 3 and beta 1 subunits were used to probe Northern blots. The adult human ventricle expresses mRNAs for all three alpha subunit isoforms in addition to beta 1 subunit mRNA.
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PMID:Expression of Na,K-ATPase isoforms in human heart. 165 51

Isoform expression of mammalian red cell Na,K-ATPase was analyzed using messenger RNA isolated from red cell precursor-enriched bone marrow of anemic sheep. Expression of the catalytic alpha subunit was analyzed using rat isoform-specific cDNA probes and expression of the beta 1 subunit, using a sheep beta 1-specific cDNA probe. RNA isolated from sheep kidney and brain were analyzed concurrently. In the red cell, as in the kidney, messenger RNA encoding only one isoform (alpha 1) of the catalytic subunit is detected; neither of the other isoforms (alpha 2 or alpha 3) could be detected. This holds true for bone marrow of sheep of either the low potassium or high potassium phenotype. Relative to the expression of alpha 1, beta subunit-specific message (beta 1) was extremely low in the red cell compared to either kidney (less than 5%) or brain (less than 3%). Using a rat cDNA probe specific for a beta 1-like subunit, beta 2, message was detected in brain but not in either kidney or bone marrow.
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PMID:Na,K-ATPase isoform expression in sheep red blood cell precursors. 216 13

We have characterized cDNAs coding for three Na,K-ATPase alpha subunit isoforms from the rat, a species resistant to ouabain. Northern blot and S1-nuclease mapping analyses revealed that these alpha subunit mRNAs are expressed in a tissue-specific and developmentally regulated fashion. The mRNA for the alpha 1 isoform, approximately equal to 4.5 kb long, is expressed in all fetal and adult rat tissues examined. The alpha 2 mRNA, also approximately equal to 4.5 kb long, is expressed predominantly in brain and fetal heart. The alpha 3 cDNA detected two mRNA species: a approximately equal to 4.5 kb mRNA present in most tissues and a approximately equal to 6 kb mRNA, found only in fetal brain, adult brain, heart, and skeletal muscle. The deduced amino acid sequences of these isoforms are highly conserved. However, significant differences in codon usage and patterns of genomic DNA hybridization indicate that the alpha subunits are encoded by a multigene family. Structural analysis of the alpha subunits from rat and other species predicts a polytopic protein with seven membrane-spanning regions. Isoform diversity of the alpha subunit may provide a biochemical basis for Na,K-ATPase functional diversity.
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PMID:Three differentially expressed Na,K-ATPase alpha subunit isoforms: structural and functional implications. 282 26

The ontogeny of Na(+)-K(+)-adenosinetriphosphatase (ATPase) mRNA in the mouse lung was examined, using alpha- and beta-isoform-specific probes in Northern blot assays and for in situ hybridization analysis. Northern blot assays demonstrated an increase in Na(+)-K(+)-ATPase expression in the perinatal period, peaking at birth (D1), with alpha 1- and beta 1-isoform levels reaching six to eight times adult levels. In situ alpha 1-isoform hybridization signals were localized primarily to developing airway epithelium and were most intense on D1. Postnatally, alpha 1-isoform hybridization signals persisted in airway epithelium, although progressively diminishing in intensity relative to perinatal levels. In developing alveolar regions, alpha 1-isoform hybridization signals remained slightly above background during this period. beta 1-Isoform hybridization signals increased dramatically during the perinatal period in both developing airway and alveolar epithelia. Postnatally, beta 1-isoform hybridization signals declined slightly in airway epithelium and developed a punctate pattern in alveolar epithelium. These data indicate that the perinatal increase in Na(+)-K(+)-ATPase expression observed in the developing mouse lung is localized primarily to epithelial structures and is therefore likely to be related to the changes in transepithelial ion and fluid transport known to occur in the perinatal period.
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PMID:In situ localization of sodium-potassium ATPase mRNA in developing mouse lung epithelium. 757 62

Ca2+ transport mediated by the plasma membrane Ca(2+)-ATPase (PMCA) serves an important role in regulation of cytosolic-free Ca2+ in a variety of cells. Isoform PMCA4 mRNA distribution in rat brain was studied by in situ hybridization using 33P-labeled antisense oligodeoxynucleotide probes. Very high levels of hybridization were found in piriform cortex with high levels in amygdaloid nucleus and laminae 2 and 6 of cerebral cortex. Significantly lower levels were found in hypothalamic nuclei and very low or undetectable levels were found in cerebellum, habenula, olfactory bulb, thalamus, choroid plexus of the third and fourth ventricles and in CA1 and CA3 cells of the hippocampus. These results suggest that PMCA4 is not a housekeeping form of the Ca(2+)-ATPase.
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PMID:The plasma membrane Ca(2+)-ATPase mRNA isoform PMCA 4 is expressed at high levels in neurons of rat piriform cortex and neocortex. 782 8

The plasma membrane Ca2+ pump is responsible for the fine regulation of the intracellular Ca2+ level and is thus involved in the control of several cellular processes. The activity of the pump is regulated by a multiplicity of mechanisms, among which are calmodulin, acidic phospholipids, kinase-mediated phosphorylation, or an oligomerization process. The C-terminal part of the molecule interacts with the region of the pump close to the active site, leading to the decrease of the activity in the resting state. Four genes coding for different isoforms of the plasma membrane Ca2+ ATPase are known in humans. Isoform 1 and 4 represent housekeeping isoforms, whereas isoforms 2 and 3 are only present in specialized tissues. The variability of the protein is further increased by alternative RNA splicing at two sites (A, C). Alternative splicing occurs within (splice site C) or near (splice site A) regions coding for regulatory domains of the protein. In all isoforms a corresponding splice form exists at both splice sites. These common splice forms are present in all tissues, whereas isoform unique splice forms are normally only present in specialized tissues. In neuronal tissues all isoforms and almost the complete set of splice forms are found. The transcripts of the different isoforms are distributed in a region-specific manner in neuronal tissues.
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PMID:The plasma membrane calcium pump: functional domains, regulation of the activity, and tissue specificity of isoform expression. 819 92

Na+,K(+)-ATPase (the sodium pump) is a family of proteins consisting of catalytic (alpha) and glycoprotein (beta) subunit isoforms which are differentially expressed in excitable tissue. To gain insight into the cell-type distribution of sodium pump protein, we determined the expression pattern of fetal rat telencephalic cultures, of telencephalic cultures depleted of neurons, and of pure astrocyte cultures. Isoform-specific antibodies were used for immunoblotting and immunohistochemistry, with supplemental [3H]ouabain binding to assess levels of functional alpha 2/alpha 3 protein. The results show that neurons of mixed telencephalic cultures uniquely express alpha 3 and high levels of alpha 1. The marked similarity in the distribution of microtubule-associated protein-2 and alpha 1 immunocytochemical staining strongly suggests that alpha 1 subunits are enriched in dendrites. Further, highly correlative growth cone-associated protein-43 and alpha 3 staining is consistent with a preferential expression of alpha 3 subunits in axons, which are also characterized by low levels of alpha 1 and no alpha 2 immunoreactivity. Process-bearing glia are intimately associated with neuronal aggregates and express high levels of both alpha 1 and alpha 2 protein, as well as GFAP. Interestingly, polygonal, flat glia not within neuronal aggregates are weakly immunopositive only for alpha 1 and GFAP. Pure astrocytic cultures possess appreciable alpha 1 protein and GFAP, but lack both alpha 2 and alpha 3 immunoreactivity. As predicted by the immunohistochemical findings, [3H]ouabain binding was low in pure astrocytic cultures, and much higher in the neuron-enriched mixed cultures. These observations confirm that neurons express all three catalytic isoforms of the sodium pump. They also suggest that specific alpha-isoforms may be polarized to targeted membrane regions of neurons. Further, glia intimately associated with neurons express alpha 2, bind significant amounts of [3H]ouabain, and possess much higher levels of alpha 1 and GFAP compared to glia not near neurons. Thus, neurons may regulate glial sodium pump expression.
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PMID:Cell-type specific expression of Na+, K(+)-ATPase catalytic subunits in cultured neurons and glia: evidence for polarized distribution in neurons. 829 81

We have used isoform-specific antisera against the Na,K-ATPase beta 1 (SpETb1) and beta 2(AMOG) (SpETb2) subunit isoforms in order to establish their specific cellular and subcellular localization in several developmental stages of the rat central nervous system. Immunocytochemical preparations revealed beta 1 Isoform protein in most neural cells, being predominantly located in the soma of neurons and astrocytes, with no appreciable developmental variations. In the newborn rat, beta 2(AMOG) immunoreactivity was present in cellular processes of astroglia and in the somas of neurons and decreasing in intensity with maturation until adulthood, where no beta 2 isoform was detected in neurons. The differential location of these isoforms, both developmentally and at the cellular level suggest a complex regulation of their genes expression and mechanisms of subcellular distribution, as well as functional differences.
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PMID:Expression of the beta 1 and beta 2(AMOG) subunits of the Na,K-ATPase in neural tissues: cellular and developmental distribution patterns. 873 77


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