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)

Chloroquine (CQ), an antimalarial and anti-inflammatory drug, is known to concentrate within lysosomes. 1H-NMR studies were conducted using the resonances of CQ itself during binding interactions with various polymers and proteins including lysosome fractions isolated from rodent livers by tritosome technique. Albumin, butyrylcholinesterase, and high molecular weight DNA interact with CQ, producing marked line-width changes that correlate with effective molecular weight. Triton WR-1339 and sucrose, probable contaminants of the lysosomal materials isolated, produced essentially no effect beyond a viscosity component. Lysosomal matrix and membrane fractions exhibited relatively weak interactions, membranes being the more tenacious toward CQ. Estimated binding constants are too small to permit explanation of CQ uptake in terms of protein affinity. The evidence is more consistent with a proton-pump trapping model proposed by de Duve et al.
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PMID:1H-NMR effects in chloroquine-biopolymer binding interactions. 23 Dec 65

Plasma lipid concentrations in NAR (Nagase Analbuminemia Rats) of 4 to 52 weeks old were examined. Plasma enzymes of NAR were also measured in relation to liver function. The concentrations of total lipid, total cholesterol, phospholipid and triglyceride tended to be increased in NAR, while that of non-esterified fatty acid (NEFA) was decreased. The lipid levels (except NEFA) were especially high in female adult NAR, and they were increased with aging. The effect of 17 beta-estradiol or testosterone administration on serum lipid concentrations was studied in gonadectomized NAR. Administration of 17 beta-estradiol to gonadectomized NAR increased lipid concentrations, while testosterone administration did not affect lipid levels. The effect of albumin injection on lipid concentrations in female NAR was also investigated. Albumin treatment to female NAR lowered serum lipid concentrations. Plasma glutamic oxaloacetic transaminase, glutamic pyruvic transaminase, lactate dehydrogenase and leucine aminopeptidase activities were higher in NAR than in normal rats. Plasma alkaline phosphatase and cholinesterase activities of NAR were similar to those of normal rats.
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PMID:Plasma lipid concentrations and enzyme activities in Nagase analbuminemia rats (NAR). 685 19

Serum pseudocholinesterase (PCHE) activity and serum albumin concentration have been used as markers for inflammatory activity as well as malnutrition in Crohn's disease (CD) with controversial results. Therefore we investigated the valence of both proteins as markers of inflammation and/or malnutrition in 50 patients with active CD [Crohn's disease activity index (CDAI): median = 243; interquartile range = 191-288] and 70 patients with quiescent CD (CDAI: 62; 25-96). Thirty patients were malnourished, 18 with active [body weight: 84%; 79-88% IBW (ideal body weight)] and 12 with quiescent CD (87.5%; 81.5-88% IBW), and 90 patients were well nourished, 32 with active (96%; 93-112% IBW) and 58 with quiescent CD (104.5%; 96-116% IBW). Median values of PCHE activity and albumin concentration were within the normal range in both groups, in patients with active as well as quiescent CD. PCHE activity was decreased only in 24 patients (48%) with active, but also in 11 (15.7%) patients with quiescent disease. Albumin concentration was decreased in 12 patients (24%) with active and in one patient (1.4%) with quiescent disease. Comparing the two patient groups PCHE activity and albumin concentration were significantly lower in active than in quiescent CD [PCHE: 3.70 kU/l; 3.00-4.30 kU/l vs. 4.80 kU/l; 3.75-5.82 kU/l, p < 0.001; Albumin: 38.0 g/l; 35.1-39.9 g/l vs. 43.8 g/l; 40.8-46.3 g/l, p < 0.001]. Both proteins were significantly lower in malnourished than in well nourished patients, except albumin in patients with quiescent CD. Repeated measurements of PCHE and albumin in patients during and after active phases showed significant increases of both proteins.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Are single measurements of pseudocholinesterase and albumin markers for inflammatory activity or nutritional status in Crohn's disease? 845 51

The genetic variants of the cholinesterase (ChE) are frequently misdiagnosed as a liver dysfunction. We compared three extraction methods for screening of ChE abnormalities. Employing these three methods, total 31 cases were found to be genetic abnormalities from 2985 patients of Hamamatsu University Hospital. We picked up 11 of candidates with low enzyme activities less than 100U/l as group 1 using the first method and effectively detected 9 cases (82%) with genetic abnormalities. The second extraction method was based on the ratio between Albumin (Alb) and ChE and subsequently, 48 of high risk patients were picked up as group 2 and 28 cases (58%) showed genetic abnormalities. Furthermore, all cases of group 1 were contained in the second group. The third method was based on the discrimination function from Alb and total cholesterol (TC) as group 3 and 32 cases were picked up. Fourteen cases (44%) out of them showed the genetic abnormalities using this method, and surprisingly, 13 cases (93%) of them were estimated to be K-variant. Although the three methods showed the different characteristics to extract genetic abnormalities of ChE, the second extraction method could pick up the largest population with genetic abnormalities. Further phenotypic extraction methods should be compared to understand the relationship between phenotype and genotype.
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PMID:[Evaluation of screening methods for cholinesterase variants from daily laboratory data]. 1051 7

A retrospective case-control study was performed with TB patients who were admitted to our hospital over the two years from Jan. 1997 to Dec. 1998 and healthy men who underwent a health screening in April 2000 in the same hospital. Thirty-two non-homeless TB patients (the first control group) and 32 healthy men (the second control group) were matched with 32 homeless TB patients according to age. All 3 groups were male. Total protein, albumin, cholesterol, cholinesterase, hemoglobin level and lymphocyte count on admission were significantly lower in the homeless patients than in the non-homeless patients and healthy men. Albumin, cholesterol, cholinesterase, hemoglobin level, white blood cell count and lymphocyte count on admission were significantly lower in non-homeless patients than healthy men. Height, weight and body mass index were significantly lower in the homeless patients than in the healthy men. However, there were no significant differences in these body characteristics between the homeless and non-homeless patients. Twenty-five percent of homeless patients died during hospitalization, compared with 6.3 percent of non-homeless patients. Lymphocyte counts among homeless patients who died during hospitalization were significantly lower than among those who survived during hospitalization. Total protein, albumin, cholesterol, cholinesterase, hemoglobin level and weight were lower in patients who died than in those who survived, although the differences were statistically not significant.
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PMID:[A nutritional investigation of homeless patients with tuberculosis]. 1139 27

The classical laboratory tests for exposure to organophosphorus toxicants (OP) are inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) activity in blood. In a search for new biomarkers of OP exposure, we treated mice with a biotinylated organophosphorus agent, FP-biotin. The biotinylated proteins in muscle were purified by binding to avidin-Sepharose, separated by gel electrophoresis, digested with trypsin, and identified from their fragmentation patterns on a quadrupole time-of-flight mass spectrometer. Albumin and ES1 carboxylesterase (EC 3.1.1.1) were found to be major targets of FP-biotin. These FP-biotinylated proteins were also identified in mouse plasma by comparing band patterns on nondenaturing gels stained for albumin and carboxylesterase activity, with band patterns on blots hybridized with Streptavidin Alexa-680. Two additional FP-biotin targets, AChE (EC 3.1.1.7) and BChE (EC 3.1.1.8), were identified in mouse plasma by finding that enzyme activity was inhibited 50-80%. Mouse plasma contained eight additional FP-biotinylated bands whose identity has not yet been determined. In vitro experiments with human plasma showed that chlorpyrifos oxon, echothiophate, malaoxon, paraoxon, methyl paraoxon, diazoxon, diisopropylfluorophosphate, and dichlorvos competed with FP-biotin for binding to human albumin. Though experiments with purified albumin have previously shown that albumin covalently binds OP, this is the first report of OP binding to albumin in a living animal. Carboxylesterase is not a biomarker in man because humans have no carboxylesterase in blood. It is concluded that OP bound to albumin could serve as a new biomarker of OP exposure in man.
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PMID:Albumin, a new biomarker of organophosphorus toxicant exposure, identified by mass spectrometry. 1552 94

The goal of this work was to identify the esterases in human plasma and to clarify common misconceptions. The method for identifying esterases was nondenaturing gradient gel electrophoresis stained for esterase activity. We report that human plasma contains four esterases: butyrylcholinesterase (EC 3.1.1.8), paraoxonase (EC 3.1.8.1), acetylcholinesterase (EC 3.1.1.7), and albumin. Butyrylcholinesterase (BChE), paraoxonase (PON1), and albumin are in high enough concentrations to contribute significantly to ester hydrolysis. However, only trace amounts of acetylcholinesterase (AChE) are present. Monomeric AChE is seen in wild-type as well as in silent BChE plasma. Albumin has esterase activity with alpha- and beta-naphthylacetate as well as with p-nitrophenyl acetate. Misconception #1 is that human plasma contains carboxylesterase. We demonstrate that human plasma contains no carboxylesterase (EC 3.1.1.1), in contrast to mouse, rat, rabbit, horse, cat, and tiger that have high amounts of plasma carboxylesterase. Misconception #2 is that lab animals have BChE but no AChE in their plasma. We demonstrate that mice, unlike humans, have substantial amounts of soluble AChE as well as BChE in their plasma. Plasma from AChE and BChE knockout mice allowed identification of AChE and BChE bands without the use of inhibitors. Human BChE is irreversibly inhibited by diisopropylfluorophosphate, echothiophate, and paraoxon, but mouse BChE spontaneously reactivates. Since human plasma contains no carboxylesterase, only BChE, PON1, and albumin esterases need to be considered when evaluating hydrolysis of an ester drug in human plasma.
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PMID:Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. 1621 67

Despite the widespread interest in malnutrition in the elderly, the utility of laboratory tests is limited. This is because their diagnostic significance can be impaired by undercurrent diseases, pre-analytical effects and unsatisfactory standardization. This survey summarizes the most important parameters of malnutrition. Thus, "nitrogen balance" is considered the golden standard of nutrition status, while the diagnostic significance of serum proteins depends on their biological half-time. Albumin is seen as the most reliable malnutrition marker, but cholinesterase and cholesterol-decrease must also be mentioned. The so-called "low-T3-phenomenon" which is caused by the production of "reverse T3", seems to be the unique parameter for the "catabolic" state of metabolism. Of special interest are also prognostic markers of mortality, such as orosomucoid. Cytokines, other signal peptides, trace elements and vitamins are from the diagnostic point of view of rather limited significance. In sum, the diagnosis and monitoring of malnutrition in the elderly represents an important challenge for laboratory medicine.
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PMID:[Limits and relevance of the laboratory diagnosis of malnutrition in the elderly]. 1682 28

Butyrylcholinesterase in human plasma and acetylcholinesterase in human red blood cells have aryl acylamidase activity toward o-nitroacetanilide, hydrolyzing the amide bond to produce o-nitroaniline and acetate. People with a genetic variant of butyrylcholinesterase that had no detectable activity with butyrylthiocholine, nevertheless had aryl acylamidase activity in their plasma. To determine the source of this aryl acylamidase activity we tested fatty acid free human albumin for activity. We found that albumin had aryl acylacylamidase activity and that this activity was inhibited by diisopropylfluorophosphate. Since the esterase activity of albumin is also inhibited by diisopropylfluorophosphate, and since it is known that diisopropylfluorophosphate covalently binds to Tyr 411 of human albumin, we conclude that the active site for aryl acylamidase activity of albumin is Tyr 411. Albumin accounts for about 10% of the aryl acylamidase activity in human plasma.
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PMID:Diisopropylfluorophosphate-sensitive aryl acylamidase activity of fatty acid free human serum albumin. 1682 79

The goal of this work is to identify novel serum proteins that are labeled with organophosphates (OPs) and to create a protocol for identification using mass spectroscopy. The use of OP-labeled proteins for identification of exposure is useful because such proteins will remain in circulation for weeks (Van Der Schans et al., 2004). Currently, both butyrylcholinesterase (BChE) and albumin have been shown to bind OPs in blood. Peeples et al. (2005) showed that albumin is labeled by OPs, specifically 6-Nbiotinylaminohexyl isopropyl phosphorofluoridate hemihydrate, in living mice. Albumin is the major protein in human serum, and its reaction with OPs tends to overwhelm the identification of other proteins. In vitro studies of human serum require removal of the serum albumin without depleting the less abundant proteins. Following this step, identifying the remaining proteins is simply a matter of labeling the proteins with an OP, separating the labeled from nonlabeled proteins, and using Q-trap mass spectrometry for identification.
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PMID:Markers of organophosphate exposure in human serum. 1719 43


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