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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)
Insulin treatment of isolated liver plasma membranes induced the release of
5'-nucleotidase
and alkaline phosphatase. This effect was maximal at physiological hormone concentrations, being 36% and 17% for
5'-nucleotidase
and alkaline phosphatase respectively, and was fully mimicked by the phosphatidylinositol specific phospholipase C (PI-PLC), thus confirming the presence of a glycosylphosphatidylinositol anchoring-system for these exofacial enzymatic proteins. The complete inhibition of insulin dependent enzyme release by neomycin is strongly supportive of an involvement of membrane-located PI-PLC activity. In addition, the insulin-like effect on enzyme release induced by the GTP non-hydrolysable analog, GTP-gamma-S, and its sensitivity to the
pertussis
toxin are in favour of a mediatory role exerted by the G proteins system, in the transduction of some actions of insulin.
...
PMID:Insulin-dependent release of 5'-nucleotidase and alkaline phosphatase from liver plasma membranes. 133 52
A plasma membrane enriched fraction from the insulin-secreting cell line RINm5F was used to characterize [3H]clonidine binding. After a single self-generating Percoll gradient, the specific activity of
5'-nucleotidase
(a plasma membrane marker) of the membrane fraction was enriched about 8-fold over that of the homogenate and nearly 30% of the total amount was recovered. The fraction was essentially free of mitochondria and secretory granules. [3H]clonidine binding to this membrane fraction revealed a single, high affinity binding site with a Kd of 2.3 nmol/l. The binding was competitively inhibited by adrenergic agonists in the following order of potency: clonidine greater than epinephrine greater than phenylephrine greater than isoproterenol, and by antagonists in the order of potency: idazoxan greater than yohimbine greater than propranolol greater than prazosin.
Pertussis
toxin pretreatment of the cells did not alter the inhibition of [3H]clonidine binding by epinephrine and clonidine nor the estimated receptor number for [3H]clonidine. In conclusion, the pharmacologic characteristics of [3H]clonidine binding sites on a plasma membrane enriched fraction from insulin-secreting RINm5F cells demonstrate that the receptor is of the alpha 2-adrenergic subtype.
...
PMID:Characterization of alpha 2-adrenoceptors in a plasma membrane enriched fraction from the insulin-secreting cell line RINm5F. 257 28
The penetration of Bordetella
pertussis
adenylate cyclase into various mammalian cells exhibits similar kinetics; the accumulation of both intracellular cyclase activity and cyclic AMP is rapid, reaching constant levels after 15-60 min of incubation. The kinetics of enzyme penetration into turkey erythrocytes is different; cyclase activity and cyclic AMP accumulate linearly and do not reach constant levels even after 6 h of incubation. In the preceding paper [Friedman, Farfel & Hanski (1987) Biochem. J. 243, 145-151] we have suggested that the constant level of intracellular cyclase activity reflects a steady state formed by continuous penetration and intracellular inactivation of the enzyme. In contrast with other mammalian cells, no inactivation of cyclase is observed in turkey erythrocytes. These results further support the notion that there is continuous penetration and deactivation of the invasive enzyme in mammalian cells. A 5-6-fold increase in specific activity of the invasive cyclase is detected in a pellet fraction of human lymphocytes in which a similar increase in specific activity of the plasma-membrane marker
5'-nucleotidase
is observed. A similar increase in the invasive-cyclase specific activity is detected in a membrane fraction of human erythrocytes. Cyclase activity in a membrane-enriched fraction of human lymphocytes reached a constant level after 20 min of cell exposure to the enzyme. Similar time courses were observed for accumulation of cyclase activity and cyclic AMP in whole lymphocytes [Friedman, Farfel & Hanski (1987) Biochem, J. 243, 145-151]. We suggest therefore that cyclic AMP generation by the invasive enzyme as well as the intracellular inactivation process occur while it is associated with a membrane fraction identical, or closely associated, with the plasma membrane.
...
PMID:The invasive adenylate cyclase of Bordetella pertussis. Intracellular localization and kinetics of penetration into various cells. 288 20
The effect of blastolysin, a glycopeptide of the cell walls of L. bulgaricus, on the resistance of mice to infections caused by S. typhimurium and B.
pertussis
, lysozyme levels in the blood serum and
5'-nucleotidase
activity of peritoneal macrophages was studied. The changes in the nonspecific resistance of mice due to the effect of blastolysin depended on the administration route and the type of the developing infection. It activated the enzymatic activity of the peritoneal macrophages and changed the lysozyme levels in the blood serum of mice. The optimal protective effect of blastolysin was achieved on intramuscular injection in a dose of 100 micrograms.
...
PMID:[Change in the natural immunity of mice after administration of blastolysin, a glycopeptide from the Lactobacillus bulgaricus cell wall]. 299 70
The influence of extracts from oak bark, St. John's-wort leaves and pine buds on natural immunity characteristics of mice has been studied. The injection of these extracts into mice has been found to enhance their resistance to infection with Staphylococcus aureus and Bordetella
pertussis
virulent cultures, to decrease the enzymatic activity of
5'-nucleotidase
in the peritoneal exudate macrophages of mice and to increase the level of lysozyme in their blood. The action of these extracts has proved to depend on their dosage and the time of observation.
...
PMID:[Action of plant extracts on the natural immunity indices of animals]. 301 9
Adenosine, an important regulator of many cardiac functions, is produced by ectosolic and cytosolic
5'-nucleotidase
. The activity of these enzymes is influenced by several ischemia-sensitive metabolic factors, e.g., ATP, ADP, H+, and inorganic phosphate. However, there is no clear evidence that adenosine itself affects
5'-nucleotidase
activity. This study tested whether adenosine decreases the activity of ectosolic and cytosolic
5'-nucleotidase
. Cardiomyocytes were isolated from adult male Wistar rats and suspended in the modified Hepes-Tyrode buffer solution. After stabilization, isolated cardiomyocytes were incubated with and without adenosine (10(-9) - 10(-4) M). Ectosolic and cytosolic
5'-nucleotidase
activity was decreased by exogenous adenosine (ectosolic
5'-nucleotidase
activity, 20.6 +/- 2.3 vs. 8.6 +/- 1.6 mumol/min per 10(6) cells [P < 0.05]; cytosolic
5'-nucleotidase
activity, 2.47 +/- 0.58 vs. 1.61 +/- 0.54 mumol/min per 10(6) cells [P < 0.05] at 10(-6) M adenosine) after 30 min. The decrease in ectosolic and cytosolic
5'-nucleotidase
activity was inhibited by 8-phenyltheophylline and
pertussis
toxin, and was mimicked by N6-cyclohexyladenosine, an adenosine A1 receptor agonist. Neither CGS21680C, and A2 receptor agonist, nor cycloheximide deactivated ectosolic and cytosolic
5'-nucleotidase
. Thus, we conclude that activation of adenosine A1 receptors is coupled to Gi proteins and attenuates ectosolic and cytosolic
5'-nucleotidase
activity in rat cardiomyocytes.
...
PMID:Evidence for deactivation of both ectosolic and cytosolic 5'-nucleotidase by adenosine A1 receptor activation in the rat cardiomyocytes. 798 2
GH, in the presence of glucocorticoid, produces a delayed increase in lipolysis in rat adipose tissue, but the biochemical mechanisms that account for this action have not been established. Other lipolytic agents rapidly activate adenylyl cyclase (AC) and the resulting production of cAMP initiates a chain of reactions that culminates in the activation of hormone-sensitive lipase. We compared responses of segments of rat epididymal fat or isolated adipocytes to 30 ng/ml GH and 0.1 microg/ml dexamethasone (Dex) with 0.1 ng/ml isoproterenol (ISO), which evoked a similar increase in lipolysis. All measurements were made during the fourth hour after the addition of GH+Dex or immediately after the addition of ISO to cells or tissues that had been preincubated for 3 h without hormone. Although no significant increases in cAMP were discernible in homogenates of GH+Dex-treated tissues, Rp-cAMPS (Rp-adenosine 3'5'-phosphothioate), a competitive inhibitor of cAMP, was equally effective in decreasing lipolysis induced by GH+Dex or ISO. The proportion of PKA that was present in the active form was determined by measuring the incorporation of 32P from [gamma-32P]ATP into kemptide in the absence and presence of saturating amounts of cAMP. GH+Dex and ISO produced similar increases in protein kinase A activity in tissue extracts. Treatment with GH+Dex did not change the total forskolin-stimulated AC present in either a crude membrane pellet sedimented at 16K x g or a less dense membrane pellet sedimented at 100K x g, but doubled the AC activity in the 16K pellet when assayed in the absence of forskolin. To evaluate possible effects on G proteins, pellets obtained from centrifugation of adipocyte homogenates at 16K x g and 100K x g were solubilized and subjected to PAGE and Western analysis. GH+Dex decreased Gi alpha2 by 44% (P < 0.02) in the 16K pellets and increased it by 52% (P < 0.01) in the 100K pellets. Gs alpha in the 16K pellet was unaffected by GH+Dex and was decreased (P < 0.05) in the 100K pellet. Sucrose density fractionation of the 16K pellets revealed a similar GH+Dex-dependent shift of Gi alpha2 to less dense fractions as determined by both Western analysis and [32P]NAD ribosylation catalyzed by
pertussis
toxin. No such changes were seen in the distribution of Gs alpha or
5'-nucleotidase
. Colchicine (100 microM) blocked the GH+Dex-dependent shift of Gi alpha2 from the 16K to the 100K pellet and blocked the lipolytic effects of GH+Dex, but not those of ISO. We conclude that by modifying the relationship between AC and Gi alpha2, GH+Dex relieves some inhibition of cAMP production and consequently increases lipolysis.
...
PMID:Growth hormone and dexamethasone stimulate lipolysis and activate adenylyl cyclase in rat adipocytes by selectively shifting Gi alpha2 to lower density membrane fractions. 1006 47
The influence of whole-cell and acellular
pertussis
vaccines, introduced both alone and in combination with N-acetylglucosaminylmuramyl-2-alanine-D-isoglutamine (GMDP) on the activity of two enzymes of peritoneal exudate macrophages (
5'-nucleotidase
and Na+K(+)-adenosine triphosphatase) was studied. The study revealed that both
pertussis
vaccines exhibited immunomodulating properties, these properties being most pronounced in whole-cell
pertussis
vaccine. The use of GMDP in combination with
pertussis
vaccines led to changes in the enzymatic activity of peritoneal exudate macrophages, which was indicative of a decrease in the immunomodulating action of
pertussis
preparations.
...
PMID:[The action of pertussis vaccines and GMDP on the change in the enzymatic activity of macrophages from peritoneal exudate]. 1087 52