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 inducible cholinesterase of Pseudomonas aeruginosa strain K (ATCC 25102) degraded propionylcholine, acetylthiocholine, acetylcholine and acetyl-beta-methylcholine at a high rate and butyrylcholine and succinylcholine at very low rates. The localization of the enzyme in the periplasmic space was indicated by a similar rate of acetylcholine degradation by intact cells or their extracts, by release of cholinesterase together with alkaline phosphatase into the culture medium during cell growth in a low phosphate-containing medium, by liberation of cholinesterase and alkaline phosphatase during lysozyme-induced conversion of cells to spheroplasts and by freezing and thawing. Threatment of cells with diazo-7-amino-1,3-naphthalenedisulphonic acid, which inactivates surface-located enzymes, abolished most of the cholinesterase and 5'-nucleotidase activities.
J Gen Microbiol 1980 Mar
PMID:Localization of cholinesterase in Pseudomonas aeruginosa strain K. 677 68

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.
Gen Pharmacol 1997 May
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

An electron microscopy study was aimed to correlate structural differentiation of the epithelium in mesonephric proximal tubules (PT) with the expression of membrane activities of alkaline phosphatase (AP) and 5'-nucleotidase (AMP). Tissue samples of mesonephros were taken from 5 to 16 days old chick embryos. Both enzymes were detected with cerium technique, Mayahara modification of lead capture method was used also for localization of AP. Control incubation was performed with levamisole. The formation of absorptive apparatus was characterized by the differentiation of PT epithelium. Activities of AP and AMP appeared to increase rapidly with the differentiation of epithelium. Reaction products of AP and AMP were detected on brush border as well as on membranes of tubular invaginations, transport tubules and endocytotic vacuoles. The basolateral cell surfaces of epithelium were projected in short interdigitating microvilli and the expression of AP and AMP activities on their membranes suggested the transport role of this structural specialization.
Gen Physiol Biophys 1999 Dec
PMID:Functional specialization of the epithelium in the mesonephric tubules. 1070 53

Over the last few years, the effects of steroid hormones on the brain have been intensively discussed. It has been demonstrated that ATP (acting as a neurotransmitter) is hydrolyzed to adenosine in the synaptic cleft by the conjugated action of ectonucleotidases, which include an enzyme of the E-NTPDase family (NTPDase3, apyrase, EC 3.6.1.5) and a 5'-nucleotidase (EC 3.1.3.5). The 5'-nucleotidase enzyme is able to hydrolyze AMP as well as other monophosphate nucleotides. The importance of this enzyme in the central nervous system is to participate in the adenosine formation, a nucleoside with neuroprotective properties and modulatory effects. However, several questions have been raised about the mechanisms of steroid hormones and the possible neuroprotective effects of estrogen. Thus, we examined the effects of gonadal steroid hormone deprivation, induced by ovary removal (OVX) and estradiol replacement therapy, on the ectonucleotidase activities in synaptosomes from hippocampus and cerebral cortex of adult rats. ATP and ADP hydrolysis in synaptosomes from cerebral cortex and hippocampus did not change as a function of OVX and results demonstrated an increase in AMP hydrolysis (82%) in the animals submitted to OVX in cerebral cortex, but not in hippocampus, when compared to control and sham-operated groups. Estradiol replacement therapy reversed this effect. RT-PCR analysis showed that the enhancement of enzyme activity in cerebral cortex could be explained by the higher expression of 5'-nucleotidase, following OVX. The hormones 17beta-estradiol (cyclodextrin-encapsulated 17beta-estradiol), DHEAS, and pregnenolone (1.0, 2.5, and 5.0 microM) did not alter the nucleotide hydrolysis, in vitro, in synaptosomes from cortex and hippocampus of female adult rats. Results presented, herein, should be considered relevant for hormone replacement therapy, since much controversy exists surrounding this area and the relationship between adenosine and sex steroids is still poorly understood.
Gen Comp Endocrinol 2005 Jan 15
PMID:Effects of steroid hormones on synaptosomal ectonucleotidase activities from hippocampus and cortex of adult female rats. 1561 71


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