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:3.1.3.5 (5'-nucleotidase)
3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sodium metavanadate (10(-4)-10(-6) M) stimulates the activity of adenylate cyclase and decreases the activity of Na+, K+-ATRase and 5'-nucleotidase in the sarcolemma fraction of chicken skeletal muscles at the embryonal and postembryonal developmental stages. Under conditions of a combined action of vanadate and guanylic nucleotides on the adenylate cyclase activity their effects are found to be potentiated. Epinephrine in vitro removes an inhibitory influence of vanadate on Na+, K+-ATPase from the third week of twe embryonal period. The restoring effect of epinephrine is blocked by propranol--a beta-adrenoblocker.
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PMID:[Effect of vanadium compounds on the enzymic activity in sarcolemma of developing muscles]. 628 70

In rabbit liver plasma membranes (LPM), specific binding of 125I-insulin rapidly increased in late gestation and peaked at birth, declining thereafter. In contrast, 125I-glucagon binding was lowest in late gestation, somewhat higher at birth, and increased by 48 h although only to 20-25% of adult. These changes in binding were due to changing numbers of receptors involving predominantly high affinity sites for insulin and low affinity sites for glucagon, with only minor changes in affinity. Despite measurable glucagon receptors by birth, fetal LPM produced no increment above basal in cAMP production with maximal doses of glucagon (10(-6) M), prostaglandin E1 (10(-4) M), or epinephrine (10(-4) M). Near birth only NaF (10 mM) produced a modest but significant increment in cAMP. By 2 h postbirth, all stimuli evoked significant increments in cAMP production that increased progressively but was still only 15-20% of adult at 48 h. Furthermore, although specific binding of cholera toxin was greater in fetal LPM (11 +/- 1 vs. 6 +/- 1%), cholera toxin-stimulated cAMP production increased by only 12-26% above basal in the fetus compared with 220% in adult. Markers of membrane purity including 5'-nucleotidase, phosphodiesterase, and insulin or glucagon degradation were not different in fetus and adult. We conclude that receptors and components of the adenylate cyclase complex mature independently; initial coupling occurs between the G/F regulatory protein and the catalytic unit (NaF but not hormonal activation) followed within hours of birth by coupling to the hormone receptor.
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PMID:Ontogeny of hepatic insulin and glucagon receptors and adenylate cyclase in rabbit. 630 5

A progressive increase in activity of some brain membrane-bound enzymes is shown after 2 and 4 weeks of ethanol administration. After 4 weeks the activities in brain homogenate of (Na+, K+) ATPase, Ca++ ATPase, 5'-nucleotidase, acetylcholinesterase and adenylate cyclase increased 150, 200, 140, 125 and 129 percent, respectively. Arrhenius plots of synaptosomal (Na+, K+) ATPase and acetylcholinesterase from alcohol-treated rats showed a lower transition temperature than control rats after two weeks, and this changed to a higher transition temperature after 4 and 8 weeks. Also, when ethanol was added in vitro to the control membranes, the transition temperature was lowered. However, if the alcohol was added to the membranes from alcohol-treated animals, the transition temperature was lowered to a value similar to that of controls. Fluorescence studies with l-anilinonaphthalene-8-sulfonate (ANS) demonstrate that ethanol induces a decrease in the fluorescence of ANS bound to brain synaptic membranes. This decrease in fluorescence is less than when these membranes are derived from chronically ethanol-treated rats. Also, when the synaptosomal enzymes were exposed to exogenous agents such as detergents, the enzyme obtained from alcohol-treated rats was more stable than that from control rats. These findings indicate a protein conformation change, probably due to the alteration of the physical properties of membrane lipids following chronic ethanol administration. These findings also demonstrate that there is a resistance to the effect of ethanol in membranes of animals habituated to ethanol that may be related to the adaptative modifications that underlie tolerance to and physical dependence on alcohol.
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PMID:Chronic ethanol treatment affects synaptosomal membrane-bound enzymes. 631 83

Activities of 5'-nucleotidase and adenylate cyclase were decreased in liver cells of rats one day after thermic burns. Distinct alterations in the enzymatic activity were observed within 3 days.
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PMID:[Alteration in the activity of 5'-nucleotidase and adenylate cyclase of the rat liver in thermic burns]. 631 65

The adenylate cyclase and 5'-nucleotidase activity was measured biochemically in the thyroid glands from patients with various thyroid diseases in comparison with normal thyroid. The basal adenylate cyclase activity in normal thyroid was 159.3 p-moles cAMP/min./g tissue. The activity was elevated to 230% of basal with 20 mM NaF and 190% of basal with 100 mU/ml TSH. These values in chronic thyroiditis and Graves' disease were not significantly different from the values of normal thyroid. In adenomatous goiter, adenoma and carcinoma, the basal adenylate cyclase activity was significantly higher than that of normal thyroid. Parallel to the biochemical determination of both enzyme activities, the distribution of histochemically demonstrable adenylate cyclase and 5'-nucleotidase activity was described in the follicular cells with normal and various thyroid diseases. The reaction product of adenylate cyclase and 5'-nucleotidase activity was restricted to the plasma membrane of the follicular cells. However, the distribution and intensity of the adenylate cyclase reaction varied in each thyroid disease, except for the absence of reaction product in the basal plasma membrane. The lack of demonstrable adenylate cyclase activity in the basal plasma membrane suggests the possibility that the basal plasma membrane may not play an important role of TSH-reception.
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PMID:Histochemical and biochemical study on adenylate cyclase and 5'-nucleotidase activity in thyroid glands with normal and various thyroid diseases. 631 19

A preparation of cardiac sarcolemmal membranes is described. These membranes exhibit 9-24-fold purification of (Na+ + K+)-ATPase, potassium-stimulated nitrophenolphosphatase, 5'-nucleotidase, adenylate cyclase, sialic acid content, and beta-receptor number. Sarcolemmal membranes have two classes of binding sites for the calcium entry blocker, bepridil, 70 X 10(12) high-affinity sites/mg, Kd 25-40 nM; and 30 X 10(15) low-affinity sites/mg, Kd 54-70 microM. Binding of bepridil to these sites appears responsible for inhibition of isoprenaline-stimulated and activation of fluoride-stimulated adenylate cyclase. Since basal adenylate cyclase activity is not influenced, bepridil must act not at the catalytic site, but by altering the interactions between beta-receptor and catalytic and regulatory components of adenylate cyclase.
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PMID:Two site binding of bepridil and modulation of adenylate cyclase in cardiac sarcolemmal membranes. 631 30

The effect of isoproterenol perfusion on cAMP levels and phosphorylase activity was investigated in the spontaneously hypertensive rat (SHR) and Kyoto Wistar normotensive control rat (WKY) heart. The basal force of contraction in physiological salt solution perfused hearts was comparable between SHR and WKY. However, the force of contraction in response to 10 nM isoproterenol perfusion was decreased approximately 20-30% in SHR heart as compared to WKY heart. Basal cAMP levels were reduced in SHR hearts as compared to WKY hearts. Isoproterenol perfusion resulted in an increase in cAMP levels over the basal cAMP values which was 50% and 100% in SHR and WKY hearts, respectively. Basal phosphorylase activity was higher in SHR hearts as compared to WKY hearts. However, the percentage increase in phosphorylase activity by isoproterenol perfusion over the basal values was approximately 400% in WKY hearts and only 200% in SHR hearts. The ouabain-sensitive (Na+, K+)-ATPase activity, Ca2+ binding in the absence of ATP, sialic acid content, and 5'-nucleotidase activity of purified cardiac plasma membranes was not altered in SHR as compared to WKY. These results would suggest beta-adrenergic mediated adenylate cyclase stimulation is decreased in SHR myocardium while other plasma membrane properties and associated enzymes may not be altered.
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PMID:Reduced cAMP levels and glycogen phosphorylase activation in isoproterenol perfused SHR myocardium. 631 20

A method has been developed for routine high yield separation of canalicular (cLPM) from basolateral (blLPM) liver plasma membrane vesicles of rat liver. Using a combination of rate zonal floatation (TZ-28 zonal rotor, Sorvall) and high speed centrifugation through discontinuous sucrose gradients, 9-16 mg of cLPM and 15-28 mg of blLPM protein can be isolated in 1 d. cLPM are free of the basolateral markers Na+/K+-ATPase and glucagon-stimulatable adenylate cyclase activities, but are highly enriched with respect to homogenate in the "canalicular marker" enzyme activities leucylnaphthylamidase (48-fold), gamma-glutamyl-transpeptidase (60-fold), 5'-nucleotidase (64-fold), alkaline phosphatase (71-fold), Mg++-ATPase (83-fold), and alkaline phosphodiesterase I (116-fold). In contrast, blLPM are 34-fold enriched in Na+/K+-ATPase activity, exhibit considerable glucagon-stimulatable adenylate cyclase activity, and demonstrate a 4- to 15-fold increase over homogenate in the various "canalicular markers." cLPM have a twofold higher content of sialic acids, cholesterol; and sphingomyelin compared with blLPM. At least three canalicular-(130,000, 100,000, and 58,000 mol wt) and several basolateral-specific protein bands have been detected after SDS PAGE of the two LPM subfractions. Specifically, the immunoglobin A-binding secretory component is restricted to blLPM as demonstrated by immunochemical techniques. These data indicate virtually complete separation of basolateral from canalicular LPM and demonstrate multiple functional and compositional polarity between the two surface domains of hepatocytes.
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PMID:Structural and functional polarity of canalicular and basolateral plasma membrane vesicles isolated in high yield from rat liver. 669 96

The purpose of this study was to compare the adenylate cyclase of a tumour (rat osteosarcoma) growing in vivo with that of fast-growing embryonic bone. In the tumour the enzyme activity per total protein or DNA (under the same assay conditions) was 6--10-fold lower than in embryonic bone. To characterize this difference, we examined the kinetic properties of the enzyme in partially purified plasma membranes from the two tissues. A purification procedure based on differential centrifugation and discontinuous-sucrose-gradient centrifugation yielded a 10-fold increase in the specific activities of adenylate cyclase and 5'-nucleotidase in bone. The same procedure yielded an enriched membrane preparation from the tumour, but, relative to 5'-nucleotidase, a loss of 30% in adenylate cyclase occurred, which could not be recovered from another fraction. Kinetic analysis revealed that the lower adenylate cyclase activity in the tumour was due to a decrease in Vmax.. There was no significant difference in Ks (approx. 0.15 mM), and in the Km for GTP and p[NH]ppG. There were marked differences, however, in the extent of stimulation by p[NH]ppG, GTP and hormone, which was greater in tumour, and in the K1 for adenosine inhibition, which was 140 microM in bone and 500 microM in tumour. Under maximum stimulatory conditions, the enzyme activity in the tumour approached that in bone. The kinetic differences between bone and tumour enzyme were decreased by detergent solubilization, suggesting that the membrane environment plays a role in the generation of the observed differences.
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PMID:Comparison of bone and osteosarcoma adenylate cyclase. Partial purification of membranes and kinetic properties of enzyme. 693 Feb 65

The role of phosphatidylinositol-specific phospholipase C (PIase C) in a) the enigmatic phosphatidylinositol (PI) turnover and b) in our understanding of membrane enzyme-PI interactions is the subject matter of this article. PIase C is present in both procaryotes and eukaryotes. This enzyme is considered to be involved in the cells PI breakdown which occurs in response to several external stimuli. Recent information on the physical properties, Ca2+ requirement, cellular localization and modulation of the activity of PIase C of mammalian systems can help to evaluate the PI turnover from a new angle. Existing evidence suggests that Ca2+-dependent PI breakdown is probably mediated through the cytosolic and particulate PIase C while a Ca2+ independent pathway is catalyzed by a lysosomal enzyme. Apparently PI turnover may be operating through more than one mechanism. The association of this phenomenon with a membrane receptor event linked with "Ca2+ gating" may have to be reconsidered. Modulation of the PIase C activity by unsaturated amphiphiles or the presence of this enzyme in different physico-chemical forms could be a potential regulatory feature. Hydrolysis of membrane PI of a number of cells and tissues by the bacterial PIase C has been shown to cause substantial release of acetylcholinesterase, alkaline phosphatase and 5'-nucleotidase in free, soluble form. Other membrane enzymes, e.g., alkaline phosphodiesterase I, L-leucyl-beta naphthyl amidase and Ca2+ or Mg2+ ATPase are not affected. These results indicate a specific interaction between PI and certain enzymes in membranes. The chemical nature of this linkage, whether it is covalent or non-covalent, has also been explored and has provided intriguing insight into this phenomenon. New findings also indicate that hydrolysis of PI by PIase C also can cause modifications in membrane-enzyme activities, e.g., adenylate cyclase.
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PMID:Minireview. Phosphatidylinositol specific phospholipases C. 708 67


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