Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Albino rats were kept for a year under conditions of everyday motor loading or of a constant hypokinesia. An increase of the motor activity results in rise in the acetylcholinesterase activity determined in the synaptosomal and purified mitochondrial fractions while hypokinesia induces a pronounced decrease in this enzyme activity. The butyrylcholinesterase activity somewhat decreases in the synaptosomal fraction after hypokinesa but does not change under the motor loading regime. Motor loading causes an increase in the amount of synaptosomal water-soluble proteins possessing an intermediate electrophoretic mobility and seem to correspond to the brain-specific protein 14-3-2. In the synaptosomal fraction the amount of membrane proteins with a low electrophoretic mobility and with the cholinesterase activity rises. Hypokinesia, on the contrary, decreases the amount of these membrane proteins.
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PMID:[Effect of motor regimes on water-soluble and membrane proteins and cholinesterase activity in subcellular fractions of rat brain tissue]. 62 7

Changes in immature rats in motor neurones after axotomy were studied by enzyme-histochemical methods. Increased activity of dehydrogenases in these neurones demonstrates enhanced metabolism and there was also increase of acid phosphatases. Decreased activity of acetylcholinesterase and indoxylacetate esterase in the neurones and their processes seems to indicate impaired neuronal function to transmit impulses. "Retrograde" reaction in the immature and the grown up animal is in general of the same kind but takes place quicker in the immature rat. However, in new-born and very young animals, it is difficult to recognize alterations in the anterior horn of the spinal cord. Therefore, nervous tissue of new-born animals seems not to respond as it does some days later in ontogenesis.
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PMID:Enzyme-histochemical studies of "retrograde" reaction in motor neurones of immature rats. 124 Jul 20

Circadian and ultradian rhythms of blood acetylcholinesterase (ACE) and rectal temperature were investigated during hypokinesia and administration of a toxic organic phosphate compound in various doses. Hypokinesia was found to produce a strong desynchronizing effect on ACE and thermal regulation. It is maintained that the use of chemicals with a well documented mechanism of action may yield reliable information about biorhythm restructuring in response to exogenous effects. It is emphasized that biorhythm changes should be taken into consideration when arranging work schedules in hypokinetic conditions.
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PMID:[Circadian rhythm of blood acetylcholinesterase after administration of organophosphate compounds during hypokinesia]. 270 48

A single dose (200 mg/kg body weight, i.p.) of 2,4-dichlorophenoxyacetic acid (2,4-D), commonly used as a herbicide, caused significant decreases in acetylcholinesterase (AChE) activity in diaphragm and other muscles of the rat. The 4S, 10S, and 16S forms of AChE were affected. The effect was maximal 15 to 24 h after injection. Choline acetyltransferase (CAT) activity was not affected. Neither AChE nor CAT activities changed in sciatic nerve from 2,4-D-treated animals. Spontaneous locomotor activity decreased dramatically 4 h after 2,4-D treatment. Myotonia that was present 1.5 h after 2,4-D injection became maximal at 2 to 6 h. Twenty-four hours after drug injection, when animals were recovering from myotonia, spontaneous locomotor activity was still depressed to 50% of control values. Prolonged distal motor latencies were observed 15 to 24 h after drug administration. AChE activity and spontaneous locomotor activity returned to control values at 48 h. Thus, 2,4-D causes a decrement of end-plate AChE, as well as behavioral and electrophysiologic changes. Decreased activity of AChE may be an early step in development of the myopathy that occurs after large dose 2,4-D.
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PMID:2,4-Dichlorophenoxyacetic acid (2,4-D) reduces acetylcholinesterase activity in rat muscle. 397 54

Decreased activity of plasma cholinesterase is responsible for prolonged apnea during anesthesia using neuromuscular blockers such as suxamethonium and mivacurium. More than 20 mutations have been identified so far in the BCHE gene resulting in impaired plasma cholinesterase activity. Biochemical tests are not always able to differentiate between pathological and normal sera; hence in some cases unanticipated complications can still occur during anesthesia even after measurements of enzyme activity and dibucaine numbers within the normal range. Therefore, molecular genetic testing is required for the accurate diagnosis of this deficiency. Here we present a study of plasma cholinesterase activity and BCHE genotyping of patients with a history of prolonged neuromuscular block and most of their pedigrees. All four exons of the BCHE gene were directly sequenced from samples and a number of mutations responsible for the reduction of plasma cholinesterase activity were identified. In most cases the atypical mutation in exon 2 (nt 209A --> G, Asp70 --> Gly) was found together with the K-variant mutation in exon 4 (nt 1615G --> A, Ala539 --> Thr), which is in good agreement with previous data suggesting that these mutations along with two others (at nt -116 and nt 1914) are in linkage disequilibrium.
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PMID:Analysis of mutations in the plasma cholinesterase gene of patients with a history of prolonged neuromuscular block during anesthesia. 1174 53