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:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The small-size adenosine deaminase (Mr = 35,000 and 43,000) in calf intestinal mucosa, frog liver and scallop adductor muscle and the large-size deaminase (Mr = 100,000) in frog liver probably formed by adding a conversion protein to the small enzyme, were tightly bound to the purine riboside affinity column. Binding of the other large-size enzymes (Mr = 140,000) in the midgut gland of scallop and mussel to the column was not successful. It seems that the binding difference does not depend on a change in affinity between active site and ligand but rather on the stereospecific positioning of active site in the enzyme molecules.
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PMID:Affinity difference of adenosine deaminases for the purine riboside-epoxyactivated Sepharose 6B column. 350 59

The antiadrenergic effect of adenosine was investigated using isolated guinea-pig heart and guinea-pig and rabbit papillary muscle. Adenosine, 15 microM, completely abolished the increased tension stimulated by 0.1-1.0 nM isoprenaline in Langendorff-perfused guinea-pig hearts. With guinea-pig papillary muscles, adenosine decreased by 40% the increased force stimulated by 1-10 nM isoprenaline. When 5 microM 2-chloroadenosine was used in conjunction with 1 unit ml-1 adenosine deaminase, a complete inhibition of the isoprenaline-stimulated tension was seen in guinea-pig papillary muscles. The antiadrenergic effect of 2-chloroadenosine was blocked by 8-phenyltheophylline. In rabbit, there was little effect of 2-chloroadenosine (plus deaminase) on isoprenaline-stimulated tension. (-)-N6 (R-phenylisopropyl)-adenosine (PIA) had no effect on basal or isoprenaline-stimulated adenylate cyclase activity of guinea-pig or rabbit sarcolemmal membranes. We conclude that the antiadrenergic effect of adenosine is mediated by A type receptors and is seen in guinea-pig but not rabbit. Production of adenosine by superfused papillary muscle may obscure the effect of added adenosine. We find no evidence that the antiadrenergic effect is mediated by inhibition of adenylate cyclase.
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PMID:An antiadrenergic effect of adenosine on guinea-pig but not rabbit ventricles. 360 35

Purine and pyrimidine enzyme profiles of human cell lines have been investigated. A novel observation was the finding that most of the cell lines showed very low or undetectable levels of cytidine (deoxycytidine) deaminase, while they possessed pyrimidine 5'-nucleotidase, cytidine and deoxycytidine kinase activities. Most cell lines showed high levels of adenosine deaminase and purine nucleoside phosphorylase activities and low levels of purine 5'-nucleotidase. We propose that high adenosine deaminase and purine nucleoside phosphorylase activities and low cytidine deaminase activity may be of importance for immature hematopoietic cells in order to ensure a balanced synthesis of the DNA precursors.
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PMID:Low cytidine deaminase levels in human hematopoietic cell lines. 362 11

Intravenous norepinephrine increases glycerol release and blood flow in adipose tissue. The vasodilation may be an indirect effect of norepinephrine through the production of adenosine. Adenosine increases glucose uptake and inhibits lipolysis in vitro. To test whether adenosine regulates blood flow and/or metabolism in vivo, adenosine deaminase (ADA) was infused intra-arterially into the inguinal fat pads of anesthetized dogs. In unstimulated tissues, ADA (n = 7) significantly increased vascular resistance and significantly decreased glucose uptake compared with the effects of a control (boiled deaminase, n = 6) infusion. ADA completely blocked the norepinephrine-induced vasodilation (n = 6). No potentiation of basal or catecholamine-stimulated lipolysis was observed with ADA. The presence of ADA in the interstitial space was verified by analysis of lymph effluents. Interstitial levels of ADA were inversely correlated with the tissue contents of adenosine. These data support the hypothesis that adenosine is a regulator of blood flow in basal and stimulated adipose tissue. Adenosine also appears to regulate glucose uptake, but not lipolysis, in vivo.
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PMID:Adenosine regulates blood flow and glucose uptake in adipose tissue of dogs. 371 62

To test whether extracellular adenosine participates in the local regulation of intestinal blood flow during nutrient absorption, the serosa of the jejunum was continuously suffused with adenosine deaminase (7 micrograms protein/ml) or theophylline (10(-4) M) in Ringer's solution. Using video microscopy, blood flow was calculated in submucosal arterioles from diameter and red cell velocity measurements. After a steady-state baseline, oleic acid (20 mM) + glucose (56 mM) were added to a bile salt solution suffusing the mucosa. Baseline arteriolar diameters and blood flows were 52 +/- 2 micron and 20 +/- 2 nl/sec with the serosal suffusate containing Ringer's; these values were not significantly altered by theophylline or deaminase treatment. During suffusion of the mucosa with a nutrient solution, diameter and blood flow transiently increased and these responses were not altered by deaminase or theophylline. Thereafter, diameter and blood flow stabilized at lower values for the duration of absorption. Diameter and blood flow were increased to 111 +/- 1% and 134 +/- 5% of control during absorption with Ringer's; the corresponding values were significantly lower with deaminase or theophylline. After absorption, diameter and blood flow stabilized near baseline with Ringer's within 7-12 minutes; the corresponding values were significantly lower with deaminase or theophylline for at least 30 minutes. Since deaminase and theophylline produced similar effects on absorptive hyperemia, adenosine might participate with other factors in the local regulation of that response. Adenosine applied to the serosa caused dose-dependent increases in calculated blood flow with a threshold near 10(-5) M and a maximum near 10(-3) M. In contrast, even 10(-2) M adenosine in the mucosal suffusate did not increase blood flow above baseline.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Possible role for adenosine in local regulation of absorptive hyperemia in rat intestine. 379 85

In adipocytes, adenylate cyclase is positively regulated by beta-adrenergic agents and negatively regulated by adenosine. Incubation of adipocytes with adenosine deaminase relieves the inhibition of adenylate cyclase by destroying the adenosine that the cells release into the medium. When adipocytes are incubated with adenosine deaminase and the beta-adrenergic agent isoproterenol, most of their ATP is converted to AMP in 5 min. Either isoproterenol or adenosine deaminase alone has little or no effect. In the additional presence of the phosphodiesterase inhibitor 4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one (Ro 20-1724) cAMP accumulates instead of AMP. Under these conditions, cAMP represents 40-50% of the total intracellular adenine nucleotides, and ATP only 5%. N6-(L-2-phenylisopropyl)adenosine, a deaminase-resistant adenosine agonist, prevents beta-adrenergic stimulation. 8-(p-Sulfophenyl)theophylline and 3-isobutyl-1-methylxanthine are both adenosine antagonists that can replace the deaminase in permitting beta-adrenergic stimulation of adenylate cyclase, but only the latter also inhibits the phosphodiesterase and causes accumulation of cAMP. When the ATP-depleted adipocytes are washed with fresh medium, the nucleoside triphosphate level can be restored within 5 min. The ATP-restored adipocytes can respond rapidly to a second dose of isoproterenol and adenosine antagonist. These findings point out the important role of adenosine in controlling adenylate cyclase activity and the possible involvement of adenylate cyclase in the control of energy flow in rat adipocytes.
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PMID:Extensive but reversible depletion of ATP via adenylate cyclase in rat adipocytes. 385 40

Cerebral blood flow in the rat was monitored by a venous outflow technique with an extracorporeal circulation, which allows for the continuous recording of flow over periods of several hours. The adenosine deaminase inhibitors erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA) (1.0-100 micrograms/kg) and deoxycoformycin (0.1-1 micrograms/kg) potentiated the reactive hyperemia elicited by a brief (24-s) anoxic challenge. Basal flow rate was unaltered by EHNA administration and slightly enhanced by deoxycoformycin. The results are consistent with the hypothesis that adenosine plays a significant role in cerebral vascular regulation and suggest that low doses of these deaminase inhibitors may be useful in the treatment of cerebral vascular insufficiency.
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PMID:Adenosine deaminase inhibitors enhance cerebral anoxic hyperemia in the rat. 387 75

Immunomorphological methods were used to localize adenosine deaminase in tissues of the rat at different stages of ontogeny. In the thymus, lymphocytes began to express significant amounts of the enzyme with the appearance of demarcation between the cortex and medulla at 17 days of gestation. At any stage of ontogeny studied, strong adenosine deaminase staining was seen predominantly in cortical thymocytes. In the spleen and lymph node, the enzyme was initially detected in T cell areas, whereas primary follicles did not show positive adenosine deaminase staining. During further development, the enzyme was demonstrated in some lymphocytes of germinal centres and plasma cells. In the duodenum, epithelial cells of villi and the neck of crypts showed positive adenosine deaminase staining whereas no staining for the enzyme was observed in the epithelial cells of the base of crypts. Strongly positive staining for adenosine deaminase appeared in plasma cells of the lamina propria by four weeks after birth. The transient positive reaction for the deaminase could be recognized in epithelial cells of tubules of the kidney during late foetal and early postnatal development. The tubules of adult rats did not stain for the enzyme. In the cartilage of 15-day foetuses, positive adenosine deaminase staining was seen only in perichondrial cells and hypertrophic cells. Kupffer cells in the liver and endothelial cells of blood vessels stained positively for the enzyme at every stage of ontogeny studied.
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PMID:Immunomorphological localization of adenosine deaminase in rat tissues during ontogeny. 389 99

A radioisotopic assay for adenosine deaminase (EC 3.5.4.4) is described together with its application in investigating the activity of the enzyme in rat cerebral cortex. Activity of the adenosine deaminase was determined to be 115nmol/min per g of tissue, measured in isoosmotic sucrose dispersions of the neocortex, and to be 170nmol/min per g of tissue after treatment with Triton X-100. The enzyme was concluded to be largely cytoplasmic, with a K(m) of 54-57mum for adenosine. Action of the deaminase, and other aspects of the metabolism of adenosine in intact neocortical tissue, were quantitatively appraised on the basis of the newly determined characteristics.
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PMID:Rat cerebral-cortex adenosine deaminase activity and its subcellular distribution. 446 74

9-beta-d-Arabinofuranosyladenine (ara-A) was deaminated to 9-beta-d-arabinofuranosylhypoxanthine by adenosine deaminase present in fetal bovine serum, newborn calf serum, and calf serum used to supplement tissue culture media. Heating newborn calf serum or calf serum for 12 h at 56 C completely eliminated the enzymatic deamination of ara-A. The deaminase activity associated with fetal bovine serum was more refractory to heating, requiring 24 h for complete inactivation. The nutritive value of heat-inactivated calf serum did not differ significantly from that of unheated serum based on considerations of population doubling times, deoxyribonucleic acid synthesis, and relative cloning efficiencies of KB cells.
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PMID:Thermal inactivation as a means of inhibiting the serum-associated deamination of 9-beta-D Arabinofuranosyladenine in tissue culture media. 484 Apr 42


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