Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Young male albino rats (120+/-5 g) were kept for 30 d on the following synthetic diets--High Protein Diet (HPD): 59% casein; Low Protein Diet (LPD): 5% casein; High Fat Diet (HFD): 51% fat; and Standard Diet (SD); 19% casein, 11% fat, and 60% sucrose. Composition of diet per se did not significantly affect plasma and RBC cholinesterase (ChE) activity, Mortality of animals on different diets, due to administration of DDVP (Vapona, dichlorovos) 50 mg/kg i.p. was: SD: 37%; HPD: 26.5%, LPD: 53%; and HFD: 44%. Plasma ChE inhibition after 24 h of DDVP administration (in surviving animals) was SD: 42%; HPD: 52%; LPD: 55%; and HFD: 47%. Erythrocyte ChE inhibition was 40% in SD, HPD, and HFD and 60% in the LPD rats. Five days following DDVP administration, plasma ChE was normal and erythrocyte ChE was still significantly increased and erythrocyte ChE was normal.
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PMID:Effect of diet on dichlorovinyl dimethyl phosphate toxicity in rats. 47 5

The effect of organic and inorganic forms of nitrogen on biomass accumulation and cholinesterase synthesis was studied with Arthrobacter simplex var. cholinesterasus. The culture assimilates nitrogen of ammonium compounds better than other forms of inorganic nitrogen; the best nitrogen source for biosynthesis of cholinesterase is ammonium phosphate. Nitrogen of nitrates is not assimilated. The amount of biomass is almost twice as high on the medium with peptone, casein or casein hydrolysate as on the medium with mineral nitrogen, while the activity of cholinesterase on these nitrogen sources decreases 1.5--2.0 times. Yeast extract as a nitrogen source increases biomass accumulation by a factor of 2.5 and does not supress synthesis of cholinesterase. The concentration of the enzyme synthesized per unit biomass on the medium with yeast extract is the same as on the medium containing ammonium phosphate. The effect of amino acids and amides, i.e. beta-alanine, proline, amides of aspartic and glutamic acids, and their mixtures, is similar to the action of yeast extract: they stimulate biomass accumulation and do not inhibit synthesis of the enzyme. Other amino acids supress synthesis of cholinesterase. The amount of accumulated biomass in the presence of glutamic acid is twice as high as in the case of any other amino acid, and three times as high as on the medium containing ammonium phosphate. Similar action of glutamic acid is manifested when it is used in mixtures with other amino acids. On the medium containing glutamic acid as a sole source of nitrogen, an increase in biomass production is accompanied with a decrease in biosynthesis of the enzyme by 50%. Repression of the biosynthesis is less if glutamic acid is added in mixtures with proline, beta-alanine and asparagine.
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PMID:[Effect of nitrogen source on growth of Arthrobacter simplex and its biosynthesis of cholinesterase]. 97 79

Male rat pups were undernourished in energy and protein by assigning them at birth to lactating dams receiving a low-protein diet (12% casein) to decrease the maternal milk supply. A normal diet (25% casein) was fed to the dams of control pups. On day 21 the pups were killed and hearts were removed and examined from both groups. Hearts from the undernourished animals weighed less and contained less DNA, RNA, and protein. The chemical indices of cell number (DNA) and cell size (wt/DNA) were reduced in the hearts from undernourished animals. Assays of the cardiac tissue for the activity of acetylcholinesterase and butyrocholinesterase indicated that undernutrition altered the activities of both enzymes, but in opposite directions. Protein-energy undernutrition resulted in an increase in acetylcholinesterase activity and a decrease in butyrocholinesterase activity. The specific activities of choline acetyltransferase and cholinesterase were unchanged. The total activity of both cholinesterase and butyrocholinesterase was reduced in the hearts of the undernourished animals. The data indicate that nutritional status can alter the activity of cardiac enzymes which have been associated with controlling the rate and rhythmic contractions of the heart.
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PMID:Nutritional effects on heart acetylcholinesterase and butyrocholinesterase activity. 121 85

In previous work, we studied, under conditions of ad libitum food consumption, the effect of amount and type of dietary fat on plasma esterase-1 (ES-1) and butyryl cholinesterase activity in rats. This was done by the isoenergetic replacement of dietary fat by carbohydrates or by another fat source. The observed change in enzyme activity could theoretically be determined by either the dietary omission or the addition or by the combination. In the present work, we studied under restricted feeding conditions the effect of supplemental energy in various forms to determine the effect of the supplement alone. Supplemental coconut fat, but not isoenergetic amounts of either glucose or casein, raised plasma ES-1 activity. None of these supplements influenced butyryl cholinesterase activity. In a second experiment, we demonstrated that the ES-1 enhancing effect of supplemental coconut fat also occurred with fish oil, whereas the stimulatory effects of olive oil and corn oil were less pronounced. Supplemental fish oil, but not the three other fats, significantly reduced the depression in butyryl cholinesterase activity. Plasma cholesterol concentration was negatively associated with butyryl cholinesterase activity, but was not related to ES-1 activity. The two esterases were not correlated with plasma triglyceride concentration. We conclude that both the amount and type of fat in the diet of rats have specific influences on plasma ES-1 activity and that butyryl cholinesterase activity is affected by the type of fat.
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PMID:Plasma esterase-1 (ES-1) activity in rats is influenced by the amount and type of dietary fat, and butyryl cholinesterase activity by the type of dietary fat. 143 52

Growing male rats that weighed 120 +/- 5 g were kept for 30 days on the following synthetic diets: high protein diet (HPD), 59% casein; high fat diet (HFD), 50% saturated fat; and normal diet (ND), 19% casein, 10% saturated fat, and 60% sucrose. Other essential dietary ingredients were included in all the diets. All animals were injected at the end of the 30-day period with parathion [10 mg/kg intraperitoneal (ip) injection as a single dose] or dichlorvos (30 mg/kg ip as a single dose) to compare the effect of dietary pretreatments on mortality from parathion and dichlorvos. A lower dose of parathion (7.5 mg/kg) and dichlorvos (20 mg/kg) was employed in another set of experiments to compare the spontaneous regeneration of plasma and red blood cell (RBC) cholinesterase (ChE) activity at 2 hr, 1 day, 3 days, and 5 days after administration of parathion or dichlorvos. The effect of these diets on hepatic microsomal oxidases was also determined. Results showed that diets per se did not affect initial plasma and RBC ChE activity. The HPD and HFD significantly protected against mortality from parathion but not from dichlorvos. Hepatic microsomal cytochrome P-450 and aminopyrine demethylase activity were unchanged, but aniline hydroxylase activity was increased significantly by HPD and HFD. Parathion oxidase in hepatic microsomes was significantly increased in rats fed HFD only. For the HPD, spontaneous regeneration of ChE diminished in RBCs in parathion-intoxicated rats and in plasma and RBCs of dichlorvos-intoxicated rats.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of high-fat and high-protein diets on toxicity of parathion and dichlorvos. 652 63

Rats were maintained on a vitamin E free diet containing 20% safflower oil for a period of 12 weeks at two dietary protein levels, 20% and 10% casein. Enhanced in vitro tissue lipid peroxidation and lysis of erythrocytes were noticed at both the protein levels. A reduction in body mass and tissue weights were observed in both the protein groups but more so at 20% protein level. Feeding of retinyl palmitate (100 000 IU/100 g body weight) for 4 consecutive days to -E rats inhibited liver and kidney in vitro lipid peroxidation. Ascorbic acid (150 mg/100 g body weight) given orally for 5 days to -E rats inhibited liver brain and kidney in vitro peroxidation. Lysis of erythrocytes from -E rats was further increased by dosing with both the vitamins "A" and "C", the latter being more effective. The stromal enzymes acetyl choline esterase and ATPase were lowered, following the hemolysis profile of the erythrocytes from the different groups. Glutathione content of erythrocytes were unaffected except in -E +C group. In all groups the higher protein level (20%) produced greater lysis as compared to 10% level. It is concluded that 20% protein is more injurious in vitamin E deficiency simultaneously made hypervitaminosis A or C.
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PMID:Effect of dietary protein and hypervitaminosis A or C on tissue peroxidation and erythrocyte lysis of vitamin E deficiency. 716 Sep 64

Various proteins/enzymes obtained commercially were tested for the presence of endogenously nitrated tyrosine by Western blot analysis omitting reducing agent in the step of SDS-PAGE. Histones II-S and VIII-S, IgG, cAMP-dependent protein kinase (PKA), phosphorylase b, and phosphorylase kinase exhibited strong immunoreactive bands. Histone VI-S, glycogen synthase, lactate dehydrogenase, actin, thyroglobulin, and macroglobulin exhibited moderate immunoreactivity. Histone III-S, casein, acetyl cholinesterase, DNase I, and lipase had only traceable immunoreactivity. Whereas histone VII-S, pyruvate kinase, trypsin, pepsin, chymotrypsin, protease IV, and protease XIII, and glutathione S-transferase lacked immunoreactivity. A variation of immunoreactivity between hypertensive and normaltensive rat hearts was found in the histone-agarose fractions of crude extracts. Additionally, nitrotyrosine immunoreactivity was observed in non-mammalian organisms including Eschericia coli, Saccharomyces cerevisiae and Triticum vulgaris. Upon the treatment of 15 microM peroxynitrite (PN), strong oxidant derived from nitric oxide (NO), the apparent Km of PKA for cAMP increased from approximately 10(-8) to 10(-6) M. The results imply that the varied nitration of tyrosine residues in proteins/enzymes may occur as a post-translational modification in vivo, and such discriminative nitration may be vital in PN/NO-regulated signal transduction cascade.
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PMID:Protein nitration. 1119 83

We have found that protein malnutrition (PM) causes a significant impairment of memory-related behavior on the 15th and 20th day after the start of PM (5% casein) feeding in prepubertal mice but not in postpubertal mice, as measured by a passive-avoidance task. This impairment was almost completely reversed by merely switching to a standard protein (20% casein) diet on the 10th day after the start of PM. However, the reversal was not observed when the switching to a standard protein regimen was done on the 15th day of the PM diet. Interestingly, the impairment of memory-related behavior on the 20th day was improved by the chronic administration of physostigmine (0.1 mg/kg/day x last 10 days, i.p.), a cholinesterase inhibitor. To correlate brain cholinergic neuron function with the memory-related behavior impairment induced by PM, microphotometry was used to determine the histological distribution of the imunofluorescence intensity for choline acetyltransferase (ChAT), a functional marker of presynapse in cholinergic neurons. The change in the intensity of fluorescence indicated that ChAT protein was decreased in the hippocampus (CA1, CA3 and dentate gyrus) on the 20th day after PM feeding in comparison with controls. These results suggest the possibility that the memory-related behavior deficits observed in prepubertal mice with PM are caused by a dysfunction of the cholinergic neurons in the hippocampus.
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PMID:Alterations in cognitive function in prepubertal mice with protein malnutrition: relationship to changes in choline acetyltransferase. 1624 90

Since a previous study demonstrated that ovariectomized rats present an activation of Na(+), K(+)-ATPase and acetylcholinesterase (AChE) activities, in the present study we investigated the influence of vitamins E plus C or soy isoflavones on the effects elicited by ovariectomy on the activities of these enzyme in hippocampus of ovariectomized rats. We also determined the effect of the same compounds on the reduction of serum butyrylcholinesterase (BuChE) activity caused by ovariectomy. Female adult Wistar rats were assigned to one of the following groups: sham (submitted to surgery without removal of the ovaries) and ovariectomized. Seven days after surgery, animals were treated for 30 days with a single daily intraperitoneous injection of vitamins E (40 mg/kg) plus C (100 mg/kg) or saline (control). In another set of experiments, the rats were fed for 30 days on a special diet with soy protein or a standard diet with casein (control). Rats were sacrificed after treatments and the hippocampus was dissected and serum was separated. Data demonstrate that vitamins E plus C reversed the activation of Na(+), K(+)-ATPase and AChE in hippocampus of ovariectomized rats. Conversely, soy protein supplementation reversed the increase of AChE activity, but not of Na(+), K(+)-ATPase activity, caused by ovariectomized group. Neither treatment was able to reverse the reduction of serum BuChE activity. Furthermore, treatments with vitamins E plus C or soy were unable to reverse the decrease in estradiol levels caused by ovariectomy. Our findings show that the treatment with vitamins E plus C significantly reversed the effect of ovariectomy on hippocampal Na(+), K(+)-ATPase and AChE activities. However, a soy diet that was rich in isoflavones was able to reverse just the increase of AChE. Neither treatment altered the reduction in serum BuChE activity. Taken together, these vitamins and soy may have a protective role against the possible brain dysfunction observed in some menopause women. Vitamins E plus C and soy isoflavones may be a good alternative as a novel therapeutic strategy.
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PMID:Supplementation with vitamins E plus C or soy isoflavones in ovariectomized rats: effect on the activities of Na(+), K (+)-ATPase and cholinesterases. 1751 15

The use of the mammary gland of transgenic goats as a bioreactor is a well established platform for the efficient production of recombinant proteins, especially for molecules that cannot be adequately produced in traditional systems using genetically engineered microorganisms and cells. However, the extraordinary demand placed on the secretory epithelium by the expression of large amounts of the recombinant protein, may result in a compromised mammary physiology. In this study, milk composition was compared between control and transgenic goats expressing high levels (1-5 g/l) of recombinant human butyrylcholinesterase in the milk. Casein concentration, as evaluated by acid precipitation, was significantly reduced in the transgenic compared with the control goats throughout lactation (P < 0.01). Milk fatty acid composition for transgenic goats, as determined by gas chromatography, was found to have significantly fewer short chain fatty acids (P < 0.01) and more saturated fatty acids (P < 0.05) compared to controls, suggesting an overall metabolic stress and/or decreased expression of key enzymes (e.g. fatty acid synthase, stearoyl-CoA desaturase). The concentration of Na(+), K(+), assessed by atomic absorption spectrophotometry, and serum albumin, determined by bromocresol green dye and scanning densitometry, were similar in transgenic and control goats during the first several weeks of lactation. However, as lactation progressed, a significant increase in Na and serum albumin concentrations and a decrease in K(+) concentration were found in the milk of transgenic goats, while control animals remained unchanged (P < 0.01). These findings suggest that: (a) high expression of recombinant proteins may be associated with a slow-down in other synthetic activities at the mammary epithelium, as evidenced by a reduced casein expression and a decreased de-novo synthesis of fatty acids; (b) the development of permeable tight junctions may be the main mechanism involved in the premature cessation of milk secretion observed in these transgenic goats.
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PMID:Milk composition studies in transgenic goats expressing recombinant human butyrylcholinesterase in the mammary gland. 1848 75


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