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 expression of gap junction protein was examined immunohistochemically using affinity-purified antibody against rat liver gap junction protein, connexin 32 (Cx32), in the kidneys of fetal (gestation days 13-16) and adult Syrian golden hamsters. Phalloidin histochemical staining, PNA- and RCA I-lectin staining, NCAM immunostaining, and alkaline phosphatase and Na(+)-K(+)-ATPase enzyme-histochemical staining were performed in combination with Cx32 immunostaining. The kidney sections were observed with a confocal scanning laser microscope. By gestation day 13, Cx32 immunoreactivity was observed in the differentiating tubules. The Cx32 staining was localized on the lateral cell membrane of the cells lining the developing proximal tubules, while the S-shaped bodies, developing distal tubules, and collecting tubules showed no positive immunostaining. As the kidney developed, the density of Cx32 immunoreactivity increased. As the gap junction provides pathways for cell-cell communication, the development of Cx32 expression may imply that this structure plays an important role in renal tubule development. Confocal scanning laser microscopy provided a clear image of the fluorescence-labeled cell structures, free from out-of-focus blur. Using the same sections, stereoscopic images were easily reconstructed from serial optical sections, and were helpful in understanding the spatial distribution of Cx32 expression in the developing fetal proximal tubules.
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PMID:Expression of connexin 32 gap junction protein in the kidneys during fetal development of the hamster (Mesocricetus auratus). 854 31

Superfast-contracting muscle fibres (II M) were identified by ATPase staining and after incubation with an antiserum raised against myosin type II M and with an antibody raised against the Galalpha1-3Galbeta1-4GlcNAc structure. II M fibres were present in masseter muscles from cat, dog and Macaca fascicularis but not in limb muscles from the same animals and not in masseter muscles from rat, pig, cow or man. Electrophoresis and staining of blots from myosin preparations showed that the anticarbohydrate antibody detected myosin heavy chains from cat masseter but not myosin heavy chains from cat biceps. The alpha-galactose specific lectin Griffonia simplicifolia isolectin B4 (GS I B4) did not stain muscle fibres or myosin heavy chains. Therefore, the epitope on myosin heavy chains defined by the anticarbohydrate antibody is presumably not Galalpha1-3Galbeta1-4GlcNAc although the antibody staining was strongly inhibited after absorption by 10mM of this trisaccharide. Antibody staining of the muscle fibres was totally inhibited by adding 10mM p-nitrophenyl beta-D-glucuronide to the incubation medium. The results thus imply that an anticarbohydrate antibody distinctively detects a carbohydrate epitope specific for myosin in superfast contracting muscle fibres from jaw-closing muscles and confirm that this epitope is not present in other muscle fibre types. This appears to be the first report on differentiated glycosylation among myosin isoforms.
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PMID:A monoclonal anticarbohydrate antibody detecting superfast myosin in the masseter muscle. 858 62

The present cytochemical study was undertaken to provide more information on the localization of enzymatic and glycoconjugates in the germinal membrane of the Echinococcus granulosus cyst. The distinctive distribution of binding sites for two lectins (peanut agglutinin and Dilochos biflorus agglutinin) in the germinal membrane are described. An investigation is made of the distribution and specific activity of adenosine triphosphatase, alkaline phosphatase and acid phosphatase. The results suggest that cells located in the deeper layer of the germinal membrane are intrinsic in the cellular differentiation process. The dissimilarities detected in both the enzymatic activity and the lectin-binding receptors could be associated with metacestode development or degeneration.
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PMID:Cytochemical study of the germinal membrane of the Echinococcus granulosus cyst. 863 82

The present study was designed to test the hypothesis that Ca2+ is required for the successful induction of the decidual cell reaction (DCR) in mice following stimulation with concanavalin A (Con A). Con A (125 micrograms) administered intraluminally on Day 4 of pseudopregnancy increased uterine vascular permeability increased uterine weight, and induced morphological and histological transformations that were clearly indicative of decidualization. Radioactive CaCl2 (1 mmol liter-1, 600 mCi mmol-1 introduced into the uterine lumen with either Con A or saline was subsequently incorporated into the uterine tissue and detected only in the luminal epithelium by microautoradiography techniques. The intraluminal administration of CaCl2 in combination with Con A increased the magnitude of the lectin-induced DCR. In contrast, the administration of other cationic chloride solutions, at various concentrations and tonicity, either had no effect (viz. Na+, Mg2+, and Ba2+) or reduced (viz. K+, Zn2+, Cd2+, and La3+) this uterine response. While ionophore A23187 was also deciduogenic, it suppressed the DCR when administered before Con A and enhanced the DCR when administered after Con A. The Ca2+ channel blockers, nifedipine, verapamil, nicardipine, and diltiazem, the Ca(2+)-calmodulin inhibitor, W7, and the Ca(+)-ATPase inhibitor, thapsigargin also effectively reduced the uterine response to Con A when administered intraluminally. However, the Con A A-induced DCR was not influenced by the Ca+ chelators, EGTA, EDTA, BAPTA, and BAPTA-AM. The results confirm that Con A is deciduogenic in pseudopregnant mice and suggest that luminal Ca2+ plays an important role in facilitating the induction of the lectin-induced DCR by influencing the metabolism of the luminal epithelium.
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PMID:The role of calcium in the artificially induced decidual cell reaction in pseudopregnant mice. 873 85

Autoimmune gastritis spontaneously develops following thymectomy of 3-day-old BALB/c mice (d3Tx). These mice develop autoantibodies to the gastric parietal cell proton pump, H/K ATPase, and aberrant expression of the H/K ATPase in the neonatal thymus prevents the induction of disease post-thymectomy. To characterize the effector cells mediating autoimmune gastritis, we isolated H/K ATPase-enriched preparations of parietal cell microsomes and further purified the enzyme by lectin affinity chromatography. Both preparations induced significant proliferative responses of gastric lymph node cells, which were mediated by CD4+, MHC class II-restricted T cells. Surprisingly, T cells reactive to the Ag could only be demonstrated in lymph nodes in the immediate proximity of the stomach; little or no response was seen when mesenteric or peripheral lymph nodes were tested. It is likely that the H/K ATPase-reactive T cells are actually the effector cells in this disease, as they could only be detected in mice that developed gastritis, as indicated by anti-parietal cell Ab, gastric inflammation, and the presence of cells capable of transferring disease into nu/nu mice. H/K ATPase-specific T cell proliferative responses could first be detected 5 wk post-thymectomy and were accompanied by high background responses at this time point. These latter responses may represent enhanced syngeneic MLRs, which we have previously shown to be elevated in d3Tx mice. Characterizations of the H/K ATPase-reactive and self-reactive T cell populations may reveal the factors that break peripheral T cell tolerance and lead to the development of organ-specific autoimmune disease.
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PMID:Pathogenesis of post-thymectomy autoimmune gastritis. Identification of anti-H/K adenosine triphosphatase-reactive T cells. 875 70

The role of H(+)-K(+)-adenosinetriphosphatase (H(+)-K(+)-ATPase) in the cortical collecting duct (CCD) B-type intercalated cell (B cell) is unclear. This study examined whether H(+)-K(+)-ATPase contributes to B cell intracellular pH (pHi) regulation and, if so, whether it is present at the apical or basolateral membrane. B cell Na(+)-independent pHi recovery from an acid load was only partially inhibited by peritubular N-ethylmaleimide (NEM). Complete inhibition required combining peritubular NEM either with luminal Sch-28080 or with luminal K+ removal. In contrast, neither peritubular Sch-28080 nor peritubular K+ removal altered pHi regulation. Tomato lectin, which binds to the gastric H(+)-K(+)-ATPase beta-subunit, labeled the B cell apical membrane. We conclude that the rabbit CCD B cell possesses an apical H(+)-K(+)-ATPase that plays an important role in pHi recovery from an in vitro acid load.
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PMID:H(+)-K(+)-ATPase in rabbit cortical collecting duct B-type intercalated cell. 878 Feb 56

This study evaluated the role of H-K-adenosinetriphosphatase (H-K-ATPase) with chronic metabolic acidosis (CMA) in intercalated cells (ICs) of rabbit cortical collecting duct (CCD). CMA was induced by replacing drinking water with 75 mM NH4Cl in 5% sucrose for 10-14 days. CCDs isolated from CMA and control rabbits were split open and exposed to the intracellular pH (pHi) indicator 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein. In N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid-buffered solutions, the resting pHi in ICs was similar for both groups. K-dependent pHi recovery (5 mM K, 140 mM N-methyl-D-glucamine) was monitored in response to a pulse of NH4Cl (10 mM). The K-dependent pHi recovery rate was threefold higher in CMAICs compared with controls and was abolished with the gastric H-K-ATPase inhibitor, Sch-28080 (10(-5) M). Polarity of the H-K-ATPase was studied in microperfused CMA and control CCDs. Luminal K-dependent pHi recovery was monitored in response to an acute pulse of NH4Cl in individual peanut lectin agglutinin (PNA)-binding ICs. The apical Sch-28080-inhibitable K-dependent pHi recovery rate was significantly greater in CMA ICs than control ICs. In summary, CMA enhances functional activity of an apical H-K-ATPase in PNA-binding ICs of rabbit CCD.
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PMID:Stimulation of apical H-K-ATPase in intercalated cells of cortical collecting duct with chronic metabolic acidosis. 878 Feb 58

Hepatocyte plasma membranes contain a glycosylated 230-kDa Ca(2+) -dependent, Mg(2+)-stimulated ATPase (pgp230), which consists of two subunits, one of 120 kDa and the other of 110 kDa. pgp230 can be enriched by the use of affinity chromatography on Concanavalin A-Sepharose, wheat germ lectin-Sepharose, and 5'-AMP-Sepharose. It has a high-affinity Ca2+ binding site. In the presence of Ca2+, it forms a phosphorylated intermediate by autocatalytic transfer of the terminal phosphate residue from ATP. Maximal Ca(2+)-dependent autophosphorylation is observed at pH 5-6. Photoaffinity labeling using 8-azido-[alpha-32P]ATP or [y-32P]ATP confirms the presence of ATP binding sites. Incubation with [alpha-32P]ATP leads to a rapid but transient labeling of pgp230. Various nucleotides, nucleotide receptor agonists, or antagonists inhibit Ca(2+)-dependent phosphorylation by [y-32P]ATP. The concentrations of half-maximal inhibition range from 10(-7) M to 10(-3) M. The rank order of inhibitory potency is: ATP > alpha,beta-methylene-ATP > CTP = TTP > y-4-amino-phenyl-ATP = 2-methyl-thio-ATP > UTP = GTP > GDP = ADP = beta,y-methylene-ATP = beta, y-methylene-TTP = beta,y-methylene-GTP = adenosine-5'-O-2-thiodiphosphate = CMP = AMP > adenosine > cytidine > guanosine = suramin > Reactive blue 2 > iso-butyl-methyl-xanthine > thymidine > uridine. These data suggest a nucleotide binding capacity of this new hepatocyte membrane glycoprotein. Further investigations should be carried out to reveal its biological function.
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PMID:Partial characterization of a new nucleotide binding glycoprotein of hepatocyte plasma membrane. 878 41

Two forms of intercalated cells are present in kidney collecting tubules, the alpha cell has apical endocytosis, apical H+-ATPase and basolateral band 3, while beta cells have reversed polarity of these proteins and no apical endocytosis. When a beta cell line was seeded at high density, it changed into the alpha form. We previously showed that a partially purified 230 kD extracellular matrix protein of high density cells was able to retarget band 3 from apical to basolateral domains and stimulated apical endocytosis in vitro (Van Adelsberg, J., J.C. Edwards, J. Takito, B. Kiss, and Q. Al-Awqati. 1994. Cell. 76:1053-1061). We now purify this protein, which was named hensin, to near homogeneity and find that it belongs to the macrophage scavenger receptor cysteine rich (SRCR) family. An antibody, generated against a fusion protein made from a partial cDNA recognized a 230-kD protein in rabbit kidney and in the intercalated cell line. In vitro, the hensin antibody inhibited expression of apical endocytosis. Hensin was secreted in a polarized manner and bound to the basolateral membrane and extracellular matrix. Immunohistochemistry of the kidney showed that it was expressed only in collecting tubules. Double immunofluorescence with hensin and peanut lectin, H+-ATPase, or band 3 showed many patterns; most alpha-cells had hensin staining while 50% of beta-cells did not. These results suggest that hensin may also be involved in the polarity reversal of intercalated cells in vivo.
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PMID:Hensin, a new collecting duct protein involved in the in vitro plasticity of intercalated cell polarity. 894 50

Glycoprotein IV of bovine adrenal chromaffin granule membranes was purified by membrane fractionation with Triton X-114 and lectin affinity chromatography. An antiserum raised against this protein recognized the same component as one directed against subunit Ac45 of the proton-translocating adenosine triphosphatase in the granule membrane. Amino acid sequencing confirmed that glycoprotein IV and Ac45 are identical proteins, and also showed that they are derived from a larger precursor by removal of a 246-amino acid N-terminal sequence. Enzymatic deglycosylation indicated an apparent polypeptide molecular mass of 29 kDa for the mature Ac45/glycoprotein IV. Blue Native electrophoresis confirmed that this protein is a component of the membrane sector of the V-ATPase.
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PMID:Chromaffin granule membrane glycoprotein IV is identical with Ac45, a membrane-integral subunit of the granule's H(+)-ATPase. 896 Dec 92


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