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)

The effects of age-specific peculiarities and the duration of maintaining rats on a ration with 4 per cent of protein (the initial mass of rats in the 1st group 100 g each; duration of the experiment--30 days. Initial mass rats in the 2d group--200 g each; duration of experiment--90 days on the activity of the lysosomal hydrolase was studied. The latter included beta-glucosidase, beta-galactosidase, beta-glucoronidase, beta-N-acetylglucosaminidase, arylsulfatase A and B, acid phosphatase, phospholipase A1 and A2, cholinesterase, the total proteolytic activity and that of catepsines A, B, C and D. An ambiguity of changes in the enzymes activity in the animals of the 1st and 2d groups was revealed. Placing the growing animals on a ration containing 4 per cent of protein produces an activation of the most of the lysosomal enzymes, whereas in animals of the 2d test group the nature of changes in the activity of individual enzymes proved to differ quite appreciably. Thus, the summary activity of catepsines, beta-glucoronidase and cholinesterase was below the control level, while the activity of beta-galactosidase, beta-N-acetyl-glucoseaminidase and phospholipase A1 and A2 went up. A prolonged maintenance of rats on a protein-poor ration led to upsetting the stability of the lysosomal membranes, which manifested itself in a higher solubilization of lysosomal enzymes in vitro.
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PMID:[Characteristics of the enzymatic adaptation of rat liver lysosomes to protein deficiency]. 68 19

Acute single dose (ip) administration of two rare earth elements like lanthanum chloride (250 mg/kg body wt) and neodymium chloride (200 mg/kg body wt) to chicks have been found to reduce the activity of certain erythrocyte membrane bound enzymes, viz. acetylcholinesterase, NADH dehydrogenase, Mg(2+)-ATPase, p-nitrophenyl phosphatase. Erythrocyte membrane bound glycosidases e.g. beta-D-glucosidase, beta-D-galactosidase and beta-D-glucuronidase were also reduced. Other components such as cholesterol and phospholipid residues were reduced but their ratio (cholesterol/phospholipid) remaining unchanged. Membrane sulfhydryl groups were also significantly inhibited by these rare earth elements.
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PMID:Chicken erythrocyte membrane: lipid profile and enzymatic activity under lanthanum chloride and neodymium chloride administration. 187 35

Target size analysis by radiation inactivation is widely used for molecular weight determination of membrane enzymes and receptors in situ without the need for prior solubilization or purification. However, since most molecular weight data available in the literature on membrane proteins involve the use of detergents for solubilization, the target sizes of membrane proteins in situ and after solubilization by detergent treatment have been compared. Using data from the literature and personal results, three different types of behavior of membrane proteins in presence of detergents were found: (i) uncoupling of subunits (electric eel acetylcholinesterase, placental steroid sulfatase, and human nonspecific beta-glucosidase); (ii) coupling of protein molecules (mouse liver neuraminidase, and rat liver insulin receptor regulatory component); and (iii) no major change in quaternary structure (rat liver insulin receptor, kidney gamma-glutamyltransferase, asialoglycoprotein receptor, insulin degrading enzyme, and human leucocyte neuraminidase). For all these proteins, there is a statistically significant increase in target size of about 24% over the value obtained in situ without detergent. A relatively large body of literature data involving a variety of membrane proteins, membrane types, and irradiation conditions (electron accelerators or 60Co sources, and proteins irradiated in lyophilized form or frozen solution) was examined, and it was concluded that target sizes of membrane proteins, irradiated in the presence of Triton X-100, should be diminished by a factor of about 24% to obtain the molecular weight value.
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PMID:Radiation inactivation of membrane proteins: molecular weight estimates in situ and after Triton X-100 solubilization. 614 6

In an attempt to provide additional quantitative markers of senescence in the nematode Caenorhabditis elegans, we have identified age-dependent increases in four lysosomal enzymes: acid phosphatase, beta-N-acetyl-D-glucosaminidase, beta-D-glucosidase, and alpha-D-mannosidase. These enzymes were judged to be lysosomal on the basis of their resemblance to analogous mammalian lysosomal enzymes with regard to subcellular fractionation, lectin binding, Km, molecular weights, inhibitor sensitivities, and pH optima. In nematode populations which had a median lifespan of 8.9 +/- 0.7 days and a maximum lifespan of 14-16 days, we observed the following increases in acid hydrolase activities per animal from day 3 (early adulthood) to day 10: (1) up to 2.5-fold for acid phosphatase; (2) 8-fold for beta-N-acetyl-D-glucosaminidase; (3) 9-fold for beta-D-glucosidase; and (4) 4-fold for alpha-D-mannosidase. Three forms of acid phosphatase and two forms of beta-D-glucosidase were separated by ion-exchange chromatography, but in each case only one form of the enzyme was primarily responsible for the age-dependent increase in total activity: acid phosphatase I increased 18-fold, while beta-D-glucosidase I increased 100-fold. By contrast, there were only slight age-dependent changes in choline acetyltransferase, acetylcholinesterase, or alpha-D-glucosidase activities after early adulthood. The age-dependent increases in acid phosphatase, beta-N-acetyl-D-glucosaminidase, beta-D-glucosidase, and alpha-D-mannosidase activities are sufficiently large and reproducible to be useful quantitative markers of senescence in C. elegans.
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PMID:Quantitative measures of aging in the nematode Caenorhabditis elegans: II. Lysosomal hydrolases as markers of senescence. 641

Polymorphonuclear leucocytes were isolated from pig blood relatively free from other cells and were characterised biochemically and morphologically and compared with human PMNLs. The activities of 16 enzymes of porcine and human PMNLs were measured and compared. Alkaline phosphatase, acid phosphatase, phosphodiesterase, gamma-glutamyl transpeptidase, NADH-cytochrome c oxidoreductase, malate dehydrogenase and acetylcholinesterase had higher specific activities in procine than in human cells. Alkaline phosphatase has an 87-fold higher specific activity in porcine than in human cells. beta-glucuronidase, lysozyme, beta-galactosidase, N-acetyl-glucosaminidase, beta-glucosidase, myeloperoxidase and catalase had higher specific activities in human than in porcine cells. beta-glucuronidase and myeloperoxidase showed over a 1000- and a 13-fold higher specific activity, respectively, in human than in porcine cells. Porcine PMNLs are readily available in large numbers and are recommended for studies of phagocytosis, chemotaxis and membrane biochemistry.
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PMID:Biochemical characterisation of porcine polymorphonuclear leucocytes: comparison with human polymorphonuclear leucocytes. 687 22

In order to understand how lepidopteran insects react physiologically to Bacillus thuringiensis crystal toxin ingestion, transcriptional profiling of Choristoneura fumiferana larvae exposed to sublethal doses of Cry1Ab protoxin were monitored using a C. fumiferana-specific cDNA microarray derived from a protoxin-specific subtractive library. Differential gene expression occurred primarily between 2 and 5 h postingestion. Metabolic enzymes such as lipases and proteases were generally repressed, whereas genes involved in detoxification, immune system regulation or general stress response were upregulated. A similar protoxin-specific transcriptional pattern was also observed with Manduca sexta larvae, using three upregulated genes (serpin, cytochrome P450 and carboxyl/cholinesterase) and one downregulated gene (beta-glucosidase), suggesting that a susceptible larval response to Cry toxin exposure might be universal among lepidopterous insects.
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PMID:Altered gene expression in Choristoneura fumiferana and Manduca sexta in response to sublethal intoxication by Bacillus thuringiensis Cry1Ab toxin. 1725 6

Polygonum sachalinensis is a widespread invasive plant in Europe. Chemical profiles of its different organs were studied by HPLC-UV-ESI/MS. Seven major constituents quercetin-3-O-beta-D-galactopyranoside, quercetin-3-O-arabinopyranoside, lapathoside D, N-trans-feruloyltyramine, lapathoside C, hydropiperoside, and vanicoside B were isolated and identified. The free radical-scavenging, alpha/beta-glucosidase, and acetylcholinesterase inhibitory activities of crude MeOH extracts and isolated compounds were studied. The structure-activity relationships were discussed. The chemical profiles revealed flavonoids and phenylpropanoids are the major compounds of all the organs of this plant. Quercetin-3-O-arabinopyranoside, lapathoside D, N-trans-feruloyltyramine, lapathoside C and hydropiperoside were isolated from this species for the first time. In the alpha-glucosidase bioassay, quercetin-3-O-beta-D-galactopyranoside, lapathoside D and N-trans-feruloyltyramine demonstrated stronger activities than the positive reference acarbose. The trend in scavenging power showed no relation to enzyme inhibition in the test models.
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PMID:Antioxidant and enzyme inhibition activities and chemical profiles of Polygonum sachalinensis F.Schmidt ex Maxim (Polygonaceae). 1969 67

In this era, major community worldwide is suffering from diabetes type II, cancer and neurodegenerative disorders. To overcome these diseases, in the screening of Korean medicinal plants, we studied the whole plant of Boehmeria nivea (B. nivea). The methanolic leaf, stem and root extracts of B. nivea and their respective n-hexane, methylene chloride (CH(2)Cl(2)), ethyl acetate (EtOAc), n-butanol (BuOH) and aqueous fractions were investigated for their total phenolic content (TPC), 1,1-diphenyl-2-picrylhydrazyl (DPPH) free radical scavenging activity, alpha-glucosidase, beta-glucosidase, alpha-galactosidase, beta-galactosidase, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzyme inhibition activities. Profound TPC and DPPH free radical scavenging activities were observed in the EtOAc and BuOH fractions of root, where the BuOH fraction showed high-pitched alpha-glucosidase inhibition and the EtOAc layer showed the maximum beta-glucosidase inhibition. Furthermore, the leaf extract demonstrated the highest beta-galactosidase inhibitory activity, but no alpha-galactosidase inhibition was seen in any of the plant parts. Notable BChE and moderate AChE inhibitory activity was found in whole plant. It can be suggested that whole plant of B. nivea provides a strong biochemical rationale as one of the good choices for the treatment of diabetes type II, cancer and neurodegenerative diseases (AD, etc).
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PMID:Evaluation of antiglycosidase and anticholinesterase activities of Boehmeria nivea. 2036 6