Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The plasma membrane enzymes, alkaline phosphatase, bicarbonate-dependent adenosine triphosphatase, 5'-nucleotidase, and carbonate dehydratase, were measured in ductal and acinar preparations of bovine pancreas. Epithelial cells were scraped from the main duct and a piece of acinar tissue was dissected from the whole pancreas for homogenization. All enzymes studied demonstrated higher levels in the duct per milligram protein than in the acinus: bicarbonate-dependent adenosine triphosphatase was 2.8 times higher; 5'-nucleotidase, 4.1 times higher; carbonate dehydratase, 16.9 times higher, while alkaline phosphatase showed only a slight increase in the duct compared to acini.
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PMID:Enzymic profiles of bovine pancreatic ductal and acinar tissues. 15 38

Part of the carbonic anhydrase activity of hepatocytes has been reported to be located in the plasma membrane. This strategic location suggests a physiological role other than that located within the cell and probably related to the specific secretory function of these cells. Furthermore, after two-thirds hepatectomy an enzymatic retrodifferentiation has been reported. We reasoned that liver regeneration probably affects the carbonic anhydrase activity in different ways depending upon its location and hence presumably physiological role. We measured, therefore, carbonic anhydrase activity in a soluble fraction or in a plasma membrane-enriched fraction obtained from liver homogenate from rats undergoing hepatectomy (two-thirds) one, three or seven days before liver resection and homogenation. No changes in carbonic anhydrase activity were found as far as soluble fraction was concerned. However, the carbonic anhydrase activity in plasma membrane was reduced (by 55%) soon after hepatectomy, there after it increased, returning to near control value at seven days. Lactate dehydrogenase activities in soluble and plasma membrane fractions were not modified by the regenerative process. Neither was 5'-nucleotidase activity determined in plasma membrane affected by liver regeneration. In summary, these results indicate a higher sensitivity of plasma membrane carbonic anhydrase activity to the regenerative process than soluble carbonic anhydrase activity. This suggests a different control of the turnover of these isoenzymes during rat liver regeneration. The phenomenon is consistent with a different physiological role for these activities; i.e., one (plasma membrane-bound carbonic anhydrase activity) may be involved in specific functions of differentiated hepatocytes, and another (soluble carbonic anhydrase activity) may be involved in general functions shared by both differentiated and undifferentiated cells.
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PMID:Plasma membrane-bound carbonic anhydrase activity in the regenerating rat liver. 189 2

Immunocytochemical staining with the antibody against mouse liver 5'-nucleotidase revealed 5'-nucleotidase antigenicity in myelinated fibers in the brains and in myelinated fibers and some interfascicular oligodendroglia in the spinal cords of normal adult mice. Although the 5'-nucleotidase specific activity in adult shiverer mouse CNS tissue homogenates had been shown to be normal, immunocytochemical staining with anti-mouse-5'-nucleotidase could be demonstrated in CNS tissue sections from only 2 out of 10 of the mutant animals. In tissue from these animals the staining, which was relatively faint, was localized specifically to cell-bodies, usually arranged in rows, and to material oriented parallel to nerve fibers. This pattern of immunostaining with anti-5'-nucleotidase resembled the immunostaining with anti-carbonic anhydrase but not with anti-glial-fibrillary-acidic-protein. This suggested that the rows of cells were oligodendrocytes, not astrocytes, and that the material parallel to nerve fibers might consist of oligodendrocyte processes wrapped loosely around axons. The antibody against rat 5'-nucleotidase, as distinguished from mouse, immunostained only the blood vessels in the shiverer mouse CNS, a finding similar to a previous observation in the normal mouse CNS. From these findings it was inferred that the primary loci of 5'-nucleotidase in the shiverer mouse CNS were interfascicular oligodendrocytes, their processes, and blood vessels, and in the normal mouse CNS, the myelin in some tracts, the blood vessels, and some interfascicular oligodendrocytes.
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PMID:5'-nucleotidase localization in the brains and spinal cords of adult normal and dysmyelinating mutant (shiverer) mice. 301 64

Carbonic anhydrase was assayed and carbonic anhydrase and 5'-nucleotidase were localized in the CNS of myelin-deficient mutant rats and normal littermates. The carbonic anhydrase specific activities were reduced by 61% and 29% in the mutants' forebrains and cerebella, respectively, and the total carbonic anhydrase activity in the spinal cords was reduced by 35%. Immunostained cells were found in gray matter from both normal and mutant rats, but, in the mutants, there was a marked deficiency of interfascicular oligodendrocytes in the regions that are normally occupied by white matter. It is suggested that a developmental study could indicate the step(s) at which normal differentiation of interfascicular oligodendroglia is blocked in this mutant.
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PMID:Biochemical and immunocytochemical evidence for a deficiency of normal interfascicular oligodendroglia in the CNS of the dysmyelinating mutant (md) rat. 301 56

Analytical subcellular fractionation of tissue whole homogenates and microanalysis of organelle marker enzymes were used to study the activity and subcellular localization of enzymes implicated in HCO3 secretion in rat duodenal and gastric antral mucosae. The following organelles, characterized by their marker enzymes, were located in the density gradients: cytosol (lactate dehydrogenase), plasma membrane (5'-nucleotidase), peroxisomes (catalase), mitochondria (succinate dehydrogenase), endoplasmic reticulum (Tris-resistant alpha-glucosidase), lysosomes (N-beta-acetylglucosaminidase), and brush-border membrane (Zn2+-resistant alpha-glucosidase and alkaline phosphatase). Compared with gastric antrum, rat duodenal mucosa contained over twice the activity of HCO3-ATPase and of Na+-K+-ATPase but less than one-tenth the activity of carbonic anhydrase. Duodenal HCO3-ATPase activity was observed in both mitochondrial and brush-border membrane fractions, whereas antral HCO3-ATPase activity was confined to mitochondria. Na+-K+-ATPase activity was found largely in the basolateral membrane (duodenum) and plasma membrane (antrum). In both tissues carbonic anhydrase activity was localized to the cytosolic fraction. These observations offer further evidence that differing biochemical mechanisms underlie HCO3 secretion by gastric and duodenal epithelia.
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PMID:Activities and subcellular localizations of enzymes implicated in gastroduodenal bicarbonate secretion. 608 73

Heterosis (hybrid vigor) for brain myelin content has been examined in detail in (C57BL/6J x DBA/2J)F1 hybrid mice at 17 days of age. The amount of myelin isolated from the F1 hybrid brain is greater than that isolated from either parental strain. In addition, the total protein content in the myelin of the three genotypes showed the following trend: F1 greater than DBA greater than C57. However, no discernible differences in myelin protein compositions could be detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Analysis of the whole brain for several myelin-associated constituents such as GM1 ganglioside, 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNPase), 5'-nucleotidase, and carbonic anhydrase indicated that heterosis exists for these components. No heterosis was found for such nonmyelin constituents as gangliosides GD1a, GT, GQ, RNA, DNA, and choline acetyltransferase. A developmental study of the whole brain CNPase indicated that the heterotic effect was greatest during the most active period of myelination (17-30 days). We conclude that the heterotic effect is specific for myelin content and is probably the result of an accelerated myelin synthesis. The heterotic effect should have great potential as a new model for studying aspects of myelinogenesis.
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PMID:Biochemical study of heterosis for brain myelin content in mice. 618 36

Myelin partially purified from spinal cords of dysmyelinating mutant (shiverer) mice had almost three-fold the specific activity of 5'-nucleotidase found in the respective myelin fraction from normal mice. The specific activities of two other normally myelin-associated enzymes, 2',3'-cyclic nucleotide-3'-phosphohydrolase and carbonic anhydrase, were only slightly higher in the myelin membranes from shiverers, compared to those from controls. In the mutants, the three enzymes probably occur in oligodendrocyte processes. Hypothetically, the 5'-nucleotidase in the myelin sheath in shiverer and normal mice may be localized in specialized structures.
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PMID:Elevated specific activity of 5'-nucleotidase in a spinal cord myelin fraction from shiverer mice. Comparison with other myelin-associated enzymes and myelin proteins. 619 24

The activities of 5'-nucleotidase, measured in brain homogenates and myelin isolated from rats at 21, 60 and greater than 90 days of age, were compared to values for two other myelin-associated enzymes, 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP) and carbonic anhydrase. Whereas the activities of all 3 enzymes were higher in brain homogenates from 60-day-old rats than in those from 21-day-old rats, only 5'-nucleotidase increased significantly in specific activity in both homogenates and myelin after the age of 60 days. The ratios of 5'-nucleotidase to the myelin basic and proteolipid proteins in subcellular fractions from adult rat brain suggested that the microsomal fraction was the only fraction containing 5'-nucleotidase levels not attributable to contamination by myelin membranes. Like carbonic anhydrase, 5'-nucleotidase had a greater distribution than CNP into microsomes of adult rats. When purified myelin was fractionated on a density gradient, the specific activity of 5'-nucleotidase was highest in the heaviest subfraction, with recovery of significant activity occurring, however, in all 3 subfractions. In rats over 60 days of age the recovery of 5'-nucleotidase in myelin was almost as high as that of the relatively myelin-specific enzyme CNP, suggesting that myelin may be the predominant, although not exclusive locus of 5'-nucleotidase in the adult rat brain.
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PMID:Rat brain 5'-nucleotidase: developmental changes in myelin and activities in subcellular fractions and myelin subfractions. 626 11

The activities of three myelin-associated enzymes, carbonic anhydrase, 5'-nucleotidase, and 2',3'-cyclic nucleotide-3'-phosphodiesterase (CNP), were measured in oligodendrocytes, neurons, and astrocytes isolated from the brain of rats 10, 20, 60, and 120 days old. The carbonic anhydrase specific activity in oligodendrocytes was three- to fivefold higher than that in brain homogenates at each age, and, at all the ages, low activities of this enzyme were measured in neurons and astrocytes. The oligodendrocytes and astrocytes from the brains of rats at all ages had higher activities of the membrane-bound enzyme 5'-nucleotidase than was observed in neurons. In oligodendrocytes from 10- and 20-day-old rats, the 5'-nucleotidase activity was two-to threefold the activity in the homogenates (i.e., relative specific activity = 2.0-3.0), and the relative specific activity of this enzyme in the oligodendrocytes declined to less than 1.0 at the later ages, concomitant with the accumulation of 5'-nucleotidase in myelin. The CNP activity was always higher in oligodendrocytes than in neurons, but not appreciably different from that in astrocytes from 20 days of age onward. The relative specific activity of CNP was highest in the oligodendrocytes from 10-day-old rats but was lower, at all ages, than we had observed in bovine oligodendrocytes. These enzyme activities in oligodendroglia are quite different in amount and developmental pattern from those reported previously for myelin.
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PMID:Carbonic anhydrase, 5'-nucleotidase, and 2',3'-cyclic nucleotide-3'-phosphodiesterase activities in oligodendrocytes, astrocytes, and neurons isolated from the brains of developing rats. 629 43

Shiverer, an autosomal recessive mutation in the mouse, is characterized by a severe deficiency in CNS myelin. The concentrations of the myelin basic and proteolipid proteins in the brains of two-month-old shiverer mice, although high enough to be measured, were much lower than in the control (+/+) brains. In contrast, the specific activities of the myelin-associated enzymes, 2',3'-cyclic nucleotide-3'-phosphohydrolase (CNP), 5'-nucleotidase, and carbonic anhydrase, were close to normal in the brains of the mutants. The activities of these enzymes and the concentrations of the myelin large basic and proteolipid proteins were compared in membrane fractions prepared, by differential and density gradient centrifugation, from the brains of shiverer and +/+ control mice. In myelin purified from the brains of shiverer mice the specific activities of 5'-nucleotidase and CNP were close to normal, and the specific activities of all three enzymes were normal in a crude myelin fraction from brains of the mutants. However, in the shi/shi brains abnormally high proportions of the three myelin-associated enzymes were distributed into the P3 (microsomal) fraction and into membrane fractions denser than myelin. The major myelin proteins, although low in total amounts in the mutants' brains, were distributed into the membrane fractions from control and shiverer brains in relative proportions similar to the relative proportions observed for the three enzymes. Thus, carbonic anhydrase, 5'-nucleotidase and CNP in the brains of shiverer mice are not truly dissociated from the major myelin proteins but are, rather, distributed for the most part into the same populations of membranes as are the residual, small amounts of the myelin basic and proteolipid proteins.
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PMID:Distribution of myelin-associated enzymes and myelin proteins into membrane fractions from the brains of adult shiverer and control (+/+) mice. 630 9


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