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)

The activity of acetylcholinesterase (AChE), 5'-nucleotidase (NT), adenylate cyclase (AC) in P2 fraction of sensory-motor cortex was studied in right-handed, left-handed and ambidexters rats on the 2-nd and 45-th day after revealing preferable forepaw at taking feedstuff out of horizontal tube (1 case, 10 presentations). By bilateral (averaging right and left hemispheres) values of AChE, NT and AC ambidexters differ from animals with absolute motor preference and right-handed rats differ from left-handed ones (2-nd day). In 1.5 month differences between ambidexter and animals with preferable extremity are revealed by NT and AC activity. Chemical brain asymmetry is revealed for ambidexters (AChE, 45-th day), right-handed rats (NT, 45-th day) and left-handed animals (AC, 2-nd day). Functional importance of biochemical characteristics studied is discussed.
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PMID:[The biochemical characteristics of the sensorimotor cortex in right-handed, left-handed and ambidextrous rats]. 876 33

Many enzymes are tethered to the extracellular face of the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. These proteins can be released in soluble form by the action of GPI-specific phospholipase. Little is currently known about the factors modulating this release. We investigated the effects of several experimental variables on the cleavage of the GPI-anchored proteins 5'nucleotidase, acetylcholinesterase, and alkaline phosphatase by phospholipases from Bacillus thuringiensis and Staphylococcus aureus. Phospholipase activity was not inhibited by isotonic salt and was relatively unaffected by buffer type and concentration. In both cases, the optimum pH for cleavage was approximately 6.5. Over 80% of 5'-nucleotidase activity present in the lymphocyte plasma membrane was cleaved by the B. thuringiensis enzyme, and the initial rate of release was linear with phospholipase concentration. All three GPI-anchored proteins were released from lymphocyte plasma membrane at comparable phospholipase concentrations, suggesting that they have similar anchor structures. The catalytic activity of 5'-nucleotidase appeared to increase following conversion to the soluble form. The relative surface charge of the host plasma membrane modulated catalytic activity towards GPI-anchored proteins, depending on the net charge of the phospholipase. Studies on purified lymphocyte 5'-nucleotidase reconstituted into bilayers of dimyristoylphosphatidylcholine indicated that the efficiency of phospholipase cleavage was 12- to 50-fold lower when compared with the native plasma membrane. The ability of the phospholipase to cleave the GPI anchor was further reduced when the bilayer was in the gel phase.
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PMID:Modulation of the cleavage of glycosylphosphatidylinositol-anchored proteins by specific bacterial phospholipases. 901 79

1. 9-Amino-1,2,3,4-tetrahydroacridine (THA), an acetylcholinesterase inhibitor, significantly inhibited in vitro the ATP diphosphohydrolase activity of synaptosomes from the cerebral cortex and hippocampus of adult rats. 2. THA did not inhibit in vitro the 5'-nucleotidase activity of synaptosomes from cerebral cortex and hippocampus of rats. 3. THA exerted an uncompetitive inhibition on ATP diphosphohydrolase activity. This mechanism of inhibition was the same in the 2 different synaptosomal fractions (cerebral cortex and hippocampus) studied. 4. THA, proposed as a drug for the treatment of Alzheimer's disease, can alter in vitro ATP degradation in synaptosomes from the central nervous system.
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PMID:Effects of 9-amino-1,2,3,4-tetrahydroacridine (THA) on ATP diphosphohydrolase (EC 3.6.1.5) and 5'-nucleotidase (EC 3.1.3.5) from rat brain synaptosomes. 918 16

Several mammalian enzymes are anchored to the outer surface of the plasma membrane by a covalently attached glycosyl-phosphatidylinositol (GPI) structure. These include acetylcholinesterase, alkaline phosphatase, membrane dipeptidase and 5'-nucleotidase. All GPI anchors determined to date have the conserved core structure ethanolamine-PO4-6Man alpha 1-2Man alpha 1-6Man alpha 1-4GlcNH2 alpha 1-6myo-inositol-1-PO4- lipid. In most mammalian GPI anchors the lipid is 1-alkyl-2-acyl-glycerol, although in porcine membrane dipeptidase it is diacylglycerol. Attached to the conserved core are various side chain residues that appear to be either protein- or tissue-specific. In addition to membrane attachment, a GPI anchor may confer additional properties on the protein, such as the susceptibility to cleavage by phospholipases and the potential to cluster in detergent-insoluble domains. GPI anchors can also act as intracellular targeting signals, in transmembrane signalling, in the clathrin-independent endocytic process of potocytosis and as hormone mediators. Thus, a GPI anchor can confer additional properties on enzymes that may be important in their physiological and pathophysiological functioning.
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PMID:Glycosyl-phosphatidylinositol anchored membrane enzymes. 943 83

The topographic relationship between the lymphatic network and the nerve plexus in the myenteric layer of the monkey jejunum was studied by an enzyme-histochemical method. Identification of the lymphatics was achieved by a 5'-nucleotidase staining method, and the enteric neural components were visualized by acetylcholinesterase staining. A well-developed lymphatic network and a dense nerve plexus were demonstrated throughout the myenteric layer. Numerous segments of the initial lymphatics, with their blind endings at the apical parts, tended to gather toward the ganglion and run along the primary nerve strands. Elements of the tissue interstitium separated the lymphatics from the enteric nerves. Nerve terminals were often located closely beneath the endothelium of the initial lymphatics and were exposed to the subendothelial tissue on the side facing the abluminal surface of the lymphatic endothelium. These findings suggest that the lymph flow in the initial lymphatics might be regulated by the enteric nervous system, and that the transport of tissue fluid by the lymphatics might serve as a suitable microenvironment for the enteric nerves.
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PMID:Lymphatic network and nerve plexus in the myenteric layer of the monkey jejunum: a topographic study using an enzyme-histochemical method. 955 69

Histochemical staining techniques for 5'-nucleotidase (5'-Nase) and acetylcholinesterase (AChE) were undertaken to localize the lymphatic network and nerve plexus in the monkey urinary bladder. Abundant 5'-Nase-positive lymphatic networks were characterized by increased number of valve-like structures and decreased calibre of blind-ends from the subepithelium to the subserosa. AChE-positive nerve fibers were visible throughout the vesical walls as fine plexuses, the densest being the neuromuscular plexus among the detrusor muscle cells or in each muscle bundle. AChE-positive nerve fibers or terminals were more frequently discernible around blood vessels than around lymphatics, and showed more intimate association with the lymphatics in the muscularis than those in the subepithelium. The nerve terminals in the subepithelium were frequently separated from attenuated lymphatic endothelium by the long processes of fibroblasts or some connective tissue cells. An ultrastructural observation revealed that unmyelinated nerve fibers with numerous neurofilaments and neurotubules run in close apposition to the lymphatic endothelium. Noteworthily, fewer terminal varicosities containing numerous small agranular vesicles (30-50 nm) and mitochondria, partially or completely bare of their Schwann cell covering in the vicinity of the lymphatic endothelium, were found in the subendothelium of initial lymphatics than in collecting ones. These terminals were occasionally identified at a distance of 120-350 nm from the subendothelial aspect of valve-originating roots, although no direct innervation of the vascular muscle cells could be found. A loose fibro-elastic connective tissue was usually interlaced between glial cell covering and lymphatic endothelium. The intrinsic interrelation of the lymphatic wall with the nerve plexus implies that the twisted subendothelial nerve terminals might be involved in intramural lymph drainage of the bladder.
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PMID:Intrinsic interrelation of lymphatic endothelia with nerve elements in the monkey urinary bladder. 1076 Jul 47

Snake envenomation employs three well integrated strategies: prey immobilization via hypotension, prey immobilization via paralysis, and prey digestion. Purines (adenosine, guanosine and inosine) evidently play a central role in the envenomation strategies of most advanced snakes. Purines constitute the perfect multifunctional toxins, participating simultaneously in all three envenomation strategies. Because they are endogenous regulatory compounds in all vertebrates, it is impossible for any prey organism to develop resistance to them. Purine generation from endogenous precursors in the prey explains the presence of many hitherto unexplained enzyme activities in snake venoms: 5'-nucleotidase, endonucleases (including ribonuclease), phosphodiesterase, ATPase, ADPase, phosphomonoesterase, and NADase. Phospholipases A(2), cytotoxins, myotoxins, and heparinase also participate in purine liberation, in addition to their better known functions. Adenosine contributes to prey immobilization by activation of neuronal adenosine A(1) receptors, suppressing acetylcholine release from motor neurons and excitatory neurotransmitters from central sites. It also exacerbates venom-induced hypotension by activating A(2) receptors in the vasculature. Adenosine and inosine both activate mast cell A(3) receptors, liberating vasoactive substances and increasing vascular permeability. Guanosine probably contributes to hypotension, by augmenting vascular endothelial cGMP levels via an unknown mechanism. Novel functions are suggested for toxins that act upon blood coagulation factors, including nitric oxide production, using the prey's carboxypeptidases. Leucine aminopeptidase may link venom hemorrhagic metalloproteases and endogenous chymotrypsin-like proteases with venom L-amino acid oxidase (LAO), accelerating the latter. The primary function of LAO is probably to promote prey hypotension by activating soluble guanylate cyclase in the presence of superoxide dismutase. LAO's apoptotic activity, too slow to be relevant to prey capture, is undoubtedly secondary and probably serves principally a digestive function. It is concluded that the principal function of L-type Ca(2+) channel antagonists and muscarinic toxins, in Dendroaspis venoms, and acetylcholinesterase in other elapid venoms, is to promote hypotension. Venom dipeptidyl peptidase IV-like enzymes probably also contribute to hypotension by destroying vasoconstrictive peptides such as Peptide YY, neuropeptide Y and substance P. Purines apparently bind to other toxins which then serve as molecular chaperones to deposit the bound purines at specific subsets of purine receptors. The assignment of pharmacological activities such as transient neurotransmitter suppression, histamine release and antinociception, to a variety of proteinaceous toxins, is probably erroneous. Such effects are probably due instead to purines bound to these toxins, and/or to free venom purines.
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PMID:Ophidian envenomation strategies and the role of purines. 1173 31

The aim of the present investigation was to evaluate the effect of a subchronic treatment (30 days/30 doses) with subcutaneous injections (0.1 mg/kg) of HgCl2 on NTPDase (E.C. 3.6.1.5), 5'-nucleotidase (E.C 3.1.3.5) and acetylcholinesterase (AChE, E.C. 3.1.1.7) activities in brain from adult rats. NTPDase and 5'-nucleotidase were measured in cortical synaptosomal fraction and AChE was measured in the homogenate of cerebral cortex and hippocampus. After the subchronic treatment (30 days), NTPDase activity was enhanced approximately 35% (p < 0.05) with ATP and ADP as substrates and no difference was observed in 5'-nucleotidase activity (AMP hydrolysis). In addition, AChE activity was enhanced in the cerebral cortex (22%, p < 0.05) and hippocampus (26%, p < 0.05) after the subchronic treatment. Mercury deposited in brain was measured by cold vapor (atomic absorption spectrometry) and no difference between the control and the subchronically treated group was observed. Here we showed for the first time that exposure to low levels of Hg2+, which resembles occupational exposure to low levels of mercury, caused a marked increase in NTPDase and AChE activities. The relationship of these alterations with the neurotoxicity of inorganic mercury deserves further studies.
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PMID:Effect of subchronic treatment with mercury chloride on NTPDase, 5'-nucleotidase and acetylcholinesterase from cerebral cortex of rats. 1513 88

Carbofuran and malathion are broad spectrum pesticides widely used in agricultural practice throughout the world. Toxicity of these pesticides has been correlated with their inhibitory effects on acetylcholinesterase activity. Nucleotides are extracellular signaling molecules, which trigger multiple biological effects. Studies have demonstrated the co-transmission of acetylcholine and ATP at the nerve endings. The control of neurotransmitter ATP levels is promoted by enzymes named ectonucleotidases, which include nucleoside triphosphate diphosphohydrolase (NTPDase) family and ecto-5'-nucleotidase. Since acetylcholine and ATP are co-released at the synapse and the acetylcholinesterase inhibition is an important target for pesticide action, here we verified the effect of exposure in vitro and in vivo to carbofuran and malathion on ectonucleotidase activities from brain membranes of zebrafish. To verify if carbofuran and malathion have a direct inhibitory effect on NTPDase and 5'-nucleotidase activities in brain membranes of zebrafish, we have tested in vitro concentrations of pesticides varying from 0.25 to 5 mM. Carbofuran, in vitro, inhibited ATP and ADP hydrolysis in an uncompetitive manner, but no effect was observed on AMP hydrolysis. Malathion decreased ATP and ADP hydrolysis in competitive and an uncompetitive manner, respectively, but not altered AMP hydrolysis. After exposure to carbofuran (50 and 500 microg/L) during 7 days, ADP hydrolysis was significantly decreased in both concentrations tested (by 19 and 24.5%, respectively). Malathion, at 500 microg/L, was able to inhibit ADP and AMP hydrolysis (by 28 and 58.5%, respectively). This study has shown that ectonucleotidases from brain membranes of zebrafish can be a potential target for pesticide neurotoxicity.
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PMID:Carbofuran and malathion inhibit nucleotide hydrolysis in zebrafish (Danio rerio) brain membranes. 1595 Oct 93

Zinc and cadmium are environmental contaminants that induce a wide range of effects on CNS. Here we tested the in vitro effect of these metals on acetylcholinesterase (AChE) and ectonucleotidase (NTPDase and ecto-5'-nucleotidase) activities in zebrafish brain. Both zinc and cadmium treatments did not alter significantly the zebrafish brain AChE activity. ATP hydrolysis presented a significant increase at 1 mM zinc (17%) and the AMPase activity had a dose-dependent increase at 0.5 and 1 mM zinc exposure (188% and 199%). After cadmium treatment, ATPase activity was significantly increased (53% and 48%) at 0.5 and 1 mM, respectively. Cadmium, in the range 0.25-1 mM, inhibited ADP hydrolysis in a dose-dependent manner (13.4-69%). Ecto-5'-nucleotidase activity was only inhibited (38%) in the presence of 1 mM cadmium. It is possible to suggest that changes on NTPDase and ecto-5'-nucleotidase activities can be an important mechanism involved in neurotoxic effects promoted by zinc and cadmium.
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PMID:In vitro effect of zinc and cadmium on acetylcholinesterase and ectonucleotidase activities in zebrafish (Danio rerio) brain. 1644 75


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