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)

This study establishes an in vitro model for examining endochondral cartilage cell metabolism. Chondrocytes derived from the resting cell zone and adjacent growth zone of rat costochondral cartilage were compared for retention of phenotype in culture. At third passage confluence, two cell populations differ morphologically and biochemically. Resting zone cells are fibroblast-like, with smooth cell membranes and little rough endoplasmic reticulum. Growth zone cells are more polygonal, smaller in diameter, with numerous cytoplasmic extensions of the plasma membranes and abundant rough endoplasmic reticulum. Both cell populations produce matrix vesicles that are comparable morphologically to matrix vesicles isolated enzymatically from epiphyseal cartilage. While membrane vesicles are released into the media by cells derived from the resting zone as well as from the growth cartilage, alkaline phosphatase activity is enriched in media vesicles produced by growth cartilage cells. Alkaline phosphatase enriched vesicles appear to be preferentially incorporated into the extracellular matrix. Both the plasma membrane marker enzyme activity and the membrane phospholipid composition are differentially expressed in matrix vesicles and plasma membranes and are cell specific. Matrix vesicles produced by resting zone cells are enriched in alkaline phosphatase, 5'-nucleotidase, ouabain sensitive Na+/K+ ATPase and cardiolipin when compared to the cell membrane. In addition, the plasma membranes of these cells contain more phosphatidylcholine plus sphingomyelin than do growth cartilage plasma membranes. Resting zone cell matrix vesicles have less phosphatidylethanolamine than do vesicles from growth cartilage cultures. Matrix vesicles produced by growth cartilage cells contain one proteolipid at 43,000 Mr which comigrates with plasma membrane proteolipid and an additional proteolipid at approximately 3,000 Mr. These data indicate that both cells retain differential expression of phenotype in culture and that one expression of this phenotype is production of specific extracellular matrix vesicles.
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PMID:Differential expression of phenotype by resting zone and growth region costochondral chondrocytes in vitro. 316 34

Epithelial brush-border membrane vesicles (BBMV) were made from lobster hepatopancreas by using Mg2+ precipitation. Alkaline phosphatase, Na+-K+-ATPase, and cytochrome c oxidase activities in these vesicles were enriched 15.0-, 1.0-, and 0.19-fold, respectively, compared with activities of a washed original homogenate pellet, indicating a relatively pure apical membrane preparation reduced in basolateral or organelle contamination. Complete vesicular closure was confirmed with electron microscopy and equilibrium [3H]D-glucose uptake experiments using various transmembrane osmotic gradients. Glucose uptake was stimulated by a transmembrane Na+ gradient but not by an identical K+ gradient or by a Na+ gradient in the presence of phloridzin. Electrogenicity of Na+-dependent glucose transport was confirmed in two ways. First, an anion permeability sequence indicated glucose uptake was stimulated in the following order: SCN- greater than Cl- greater than gluconate- greater than SO4(2-). Second, an outwardly directed valinomycin-induced K+ diffusion potential, rendering the vesicle interior electrically negative, enhanced glucose uptake compared with K+-loaded vesicles lacking the ionophore. Glucose influx occurred by a combination of carrier-mediated transfer, illustrating Michaelis-Menten kinetics, and nonsaturable "apparent diffusion." pH (same on both sides) strongly influenced Na+-dependent glucose uptake according to the sequence: pH 6.0 greater than pH 7.4 greater than pH 8.0. Increased proton concentration lowered the Michaelis constant for glucose transport and increased the apparent diffusional permeability of the membrane to the sugar. Maximal carrier-mediated glucose transport rate was largely unaffected by pH.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Glucose transport by lobster hepatopancreatic brush-border membrane vesicles. 397 Feb 30

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1mum-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.
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PMID:The inhibition of enzymes by beryllium. 428 87

1. A technique is described for the removal of subcellular contaminants from intact rat intestinal brush borders, and for the subsequent separation of a microvillus membrane fraction from a fibrillar residue. 2. Increments in invertase activity, microscopic homogeneity and low nucleic acid content indicate that the microvillus plasma membrane has been extensively purified. Multiple membrane preparations have been shown to be highly reproducible with respect to their invertase specific activity, cholesterol content and phospholipid content. Alkaline phosphatase, leucine aminopeptidase, Mg(2+)- and Ca(2+)-dependent adenosine triphosphatase and seven separate disaccharidases were shown to be predominantly confined to the membrane fraction. 3. The fibrillar fraction has been shown to contain approximately 30% of the total protein of purified brush borders, plus most of the residual nucleic acid contaminant. No evidence was found for the localization of any specific enzyme in this fraction.
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PMID:Rat intestinal microvillus membranes. Purification and biochemical characterization. 429 31

Plasma membranes were isolated from the ameba Acanthamoeba castellanii by low-speed velocity centrifugation followed by equilibrium centrifugation in a sucrose gradient. The isolated membranes had a high ratio of sterol to phospholipid (0.98 moles/mole) and of phospholipid to protein (0.43 mg/mg). The plasma membranes had very low concentrations of DNA, RNA, lipid inositol, and glycerides. Glycolipids and glycoproteins were enriched in the plasma membranes relative to their concentrations in the whole cell. The plasma membranes were also judged to be of high purity by the absence, or very low level, of enzymatic activities considered to be indicative of other cell membranes, and by electron microscope examination. Alkaline phosphatase and 5'-nucleotidase activities were enriched in the plasma membranes 13-fold relative to the whole homogenate and had higher specific activities in the plasma membranes than in any other cell fractions. A Mg(++) adenosine triphosphatase (ATPase) was enriched sixfold in the plasma membranes relative to the whole homogenate. The phospholipids of the plasma membranes contained more phosphatidylethanolamine and phosphatidylserine and less phosphatidylcholine than did the phospholipids of the whole cells. There were differences in the fatty acid compositions of corresponding phospholipids in the plasma membranes and whole cells but no difference in the ratios of total saturated to unsaturated fatty acids. The membranes of phagosomes isolated from amebae that had ingested polystyrene latex had essentially the same phospholipid, sterol, and enzymatic composition as plasma membranes.
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PMID:Plasma and phagosome membranes of Acanthamoeba castellanii. 432 20

The authors utilized the technic of plastic embedding with enzyme histochemistry for the evaluation of enzymatic expression by epithelium of the lower urinary tract in humans. Alpha-naphthyl acetate esterase and acid phosphatase generally were expressed by normal and neoplastic urothelium. Expression of 5'-nucleotidase and ATPase was more restricted. Alkaline phosphatase, prominent in the transitional cells of lower mammalian species, generally was not present in human urothelium. Enzyme histochemistry has not been applied generally to the study of disease of the lower urinary tract, but this study suggests it may be of value in understanding the biology of this tissue and be of potential use in histopathologic diagnosis of diseases of this region.
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PMID:Enzyme histochemistry of normal and neoplastic transitional epithelium. 609 41

Cultures of osteoblastlike cells obtained from the endosteal surfaces of rabbit long bones formed and mineralized an extracellular matrix when they were supplied daily with medium containing fresh ascorbate. No matrix formed without this supplementation. The matrix mineralized whether or not beta-glycerophosphate, a substrate of alkaline phosphatase, was added to the medium. The ion-transporting ATPase activities of untreated, ascorbate-treated, and ascorbate plus beta-glycerophosphate-treated cells were measured. Ascorbate-treated and ascorbate plus beta-glycerophosphate-treated cells had similar enzyme activities. The activities of the Ca2+-ATPase; Ca2+,Mg2+-ATPase; and alkaline phosphatase in treated cells were elevated over the activities in untreated cells. Na+,K+-ATPase activity was lower in treated than in untreated cells. HCO3--ATPase activity was not changed by treatment. Alkaline phosphatase activity was 20 times higher in freshly isolated osteoblastlike cells than in cells grown to confluence in primary culture. In addition, subculturing further reduced the activity of this osteoblast-marker enzyme. The activities of the ion-transporting ATPases and alkaline phosphatase in second passage cells were similar to the activities of these enzymes in fresh, noncalcifying tissues. Nevertheless, second passage cells retain the ability to mineralize an extracellular matrix, and their ion-transporting ATPase and alkaline phosphatase activities are altered when the cells mineralize a matrix.
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PMID:Ion-transporting ATPases and matrix mineralization in cultured osteoblastlike cells. 609 28

The study deals with the histoenzymological architecture of the rhomencephalon and mesencephalon of a fresh water turtle. Attempt has been made to see the location of phosphatases (acid and alkaline phosphatases, 5-nucleotidase, adenosine triphosphatase) in the different constituents of these brain areas. The distribution of acid phosphatase is similar to Nissl staining, hence the enzyme has been used as a marker to differentiate various nuclei in the different brain areas. Moreover, the concentration of acid phosphatase is higher in large neurons like that of Nissl substance and, therefore, all such cells are quite distinct. Alkaline phosphatase predominates in blood vessels. Neuropil and neuronal activity of this enzyme is restricted to limited nuclei, only. 5-nucleotidase is localized in all the cells as well as in the neuropil. Adenosine triphosphatase activity is quite strong in all the brain areas irrespective of their sensory and motor nature. In turtle brain it has not been possible to distinguish sensory and motor areas on the basis of phosphatases distribution as calimed in fishes and mammals by several workers. Significance of the enzymes at various locales has been brought out in the contribution.
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PMID:A comparative study of phosphatases in the rhombencephalon and mesencephalon of fresh water turtle (Lissemys punctata granosa). 609 5

The ultrastructural and enzyme cytochemical features of two follicular ameloblastomas were investigated. The peripheral cells of the follicular areas in both lesions had several types of tall columnar cells which were highly polarized and showed varying degrees of cellular differentiation. These polarized cells had their nuclei situated away from the basal lamina, and often contained dilated strands of endoplasmic reticulum in the subnuclear cytoplasm. Some of these cells also contained dense-cored secretory granules, condensing granules and coated vesicles in the cytoplasm adjacent to the basal plasma membrane. These cells bore a striking resemblance to pre-ameloblasts and early secretory ameloblasts. Alkaline phosphatase and ATPase cytochemistry supported these morphologic observations. Interestingly, the central cells of the follicular areas were consistently negative for alkaline phosphatase activity as were the peripheral cells, while both cell types had ATPase activity demonstrable at their cell surface.
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PMID:An electron-microscopic and cytochemical study of follicular ameloblastoma. 614 Mar 4

Stimulation of Mg2+, Ca2+ and Mg2+HCO-3 dependent ATPase activity in mitochondrial and microsomal fractions from the uteri of laying hens is demonstrated. ATPase activity was greatest with 5 mM concentrations of Mg2+ at pH 8.5, and at pH 7.4-7.8 following the addition of bicarbonate. Suppression of eggshell calcification, induced by insertion of a thread into the uterus, did not alter Mg2+, Ca2+ and Mg2+HCO-3 ATPase activities. Alkaline phosphatase activity was generally low, and was unaffected by suppression of eggshell calcification. Levels of carbonic anhydrase and calcium binding protein were lower in the uteri of hens laying shell-less eggs. Injections of 1,25(OH)2D3 in hens laying shell-less eggs did not alter CaBP levels or enzyme activities. It is concluded that factors other than 1,25(OH)2D3 and gonadal hormones are involved in the regulation of uterine CaBP levels.
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PMID:Effects of suppression of eggshell calcification and of 1,25(OH)2D3 on Mg2+, Ca2+ and Mg2+HCO-3 ATPase, alkaline phosphatase, carbonic anhydrase and CaBP levels--I. The laying hen uterus. 614 58


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