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PubMed1992

The determination of tissue ethanolamine levels by reverse-phase high-performance liquid chromatography.

A rapid and sensitive procedure for the determination of ethanolamine levels in mammalian tissues is reported. Ethanolamine was extracted from the tissue with a chloroform/methanol mixture, followed by phase separation. The aqueous phase was subjected to charcoal chromatography and the eluant was derivatized with phenylisothiocyanate. The amount of phenylthiocarbamyl (PTC) ethanolamine in the tissue extract was determined by reverse-phase high-performance liquid chromatography. Quantitation of PTC ethanolamine was linear between 0.1-1.0 nmol. The pool sizes of ethanolamine in hamster heart, liver and kidney were found to be 1.07, 0.92 and 1.11 mumol/g wet weight, respectively. The sensitivity of the method would allow the determination of ethanolamine in very small tissue samples.

Animals↗

PubMed1992

Lipid metabolism in large T47D human breast cancer spheroids: 31P- and 13C-NMR studies of choline and ethanolamine uptake.

31P- and 13C-NMR were used to determine the kinetics of choline and ethanolamine incorporation in T47D clone 11 human breast cancer cells grown as large (300 microns) spheroids. Spheroids were perfused inside the spectrometer with 1,2-13C-labeled choline or ethanolamine (0.028 mM) and the buildup of labeled phosphorylcholine (PC) or phosphorylethanolamine (PE) was monitored. To analyze the NMR kinetic data, it was assumed that each signal represents a weighted average of signal from the proliferating and non-proliferating compartments of the large spheroid. The average ATP pool size was 4 +/- 1 fmol/cell compared to 8 +/- 1 fmol/cell in small (150 microns) proliferating spheroids (P less than 0.0002). The average PC pool size at steady state was reduced to 11 +/- 6 fmol/cell compared to 22 +/- 8 (P less than 0.007). This could be correlated with an overall reduction of choline uptake in the non-proliferating spheroid fraction. The rate of the enzyme choline kinase was 0.3 fmol/(cell h) compared to 1.0 fmol/(cell h) (P less than 0.0001) for proliferating cells. The rate constant of CTP:phosphocholine cytidyltransferase (0.05 h-1) was not significantly altered, but the rate of the enzyme was reduced from 1.3 to 0.2-0.5 fmol/(cell h). The pool size of PE in medium containing serum ethanolamine (1.7 microM) was approximately the same (15 fmol/cell) in small and large spheroids. In the presence of high ethanolamine (0.028 mM) the average PE level decreased slightly (11 fmol/cell) and the rate of the enzyme ethanolamine kinase in the non-proliferating fraction was 0.7 fmol/(cell h) versus 1.0 fmol/(cell h) in the proliferating cells (P less than 0.07). The rate constant of CTP:phosphoethanolamine cytidyltransferase (0.07 h-1) was not significantly altered but the corresponding reaction rate was reduced from 1.4 to 0.2-0.8 fmol/(cell h). The kinetics of choline incorporation did not alter in the presence of 0.028 mM ethanolamine.

Breast Neoplasms↗

PubMed1984

Incorporation of serine into Paramecium ethanolamine phospholipid and phosphonolipid head groups.

Ethanolamine phospholipid head groups in Paramecium were synthesized directly from ethanolamine. As in other cell types, radioactivity from ethanolamine failed to incorporate significantly into head groups of ethanolamine phosphonolipids, indicating that the phosphonolipids are not derived from their phospholipid analogues. Unlike other systems previously examined, radioactivity from serine is incorporated into both ethanolamine phospholipid and phosphonolipid head groups of glycerolipids and sphingolipids in this ciliate. These observations suggest that synthesis of ethanolamine phosphonolipids involves synthesis de novo of free phosphonoserine, which is then incorporated into lipids, and then lipid-bound phosphonoserine intermediates (glycerolipids or sphingolipids) undergo decarboxylation, forming lipidbound phosphonoethanolamine compounds.

Animals↗

PubMed2004

Glycosylphosphatidylinositol (GPI) proteins of Saccharomyces cerevisiae contain ethanolamine phosphate groups on the alpha1,4-linked mannose of the GPI anchor.

In humans and Saccharomyces cerevisiae the free glycosylphosphatidylinositol (GPI) lipid precursor contains several ethanolamine phosphate side chains, but these side chains had been found on the protein-bound GPI anchors only in humans, not yeast. Here we confirm that the ethanolamine phosphate side chain added by Mcd4p to the first mannose is a prerequisite for the addition of the third mannose to the GPI precursor lipid and demonstrate that, contrary to an earlier report, an ethanolamine phosphate can equally be found on the majority of yeast GPI protein anchors. Curiously, the stability of this substituent during preparation of anchors is much greater in gpi7Delta sec18 double mutants than in either single mutant or wild type cells, indicating that the lack of a substituent on the second mannose (caused by the deletion of GPI7) influences the stability of the one on the first mannose. The phosphodiester-linked substituent on the second mannose, probably a further ethanolamine phosphate, is added to GPI lipids by endoplasmic reticulum-derived microsomes in vitro but cannot be detected on GPI proteins of wild type cells and undergoes spontaneous hydrolysis in saline. Genetic manipulations to increase phosphatidylethanolamine levels in gpi7Delta cells by overexpression of PSD1 restore cell growth at 37 degrees C without restoring the addition of a substituent to Man2. The three putative ethanolamine-phosphate transferases Gpi13p, Gpi7p, and Mcd4p cannot replace each other even when overexpressed. Various models trying to explain how Gpi7p, a plasma membrane protein, directs the addition of ethanolamine phosphate to mannose 2 of the GPI core have been formulated and put to the test.

Animals↗

PubMedDate not supplied

A comparison of ethanolamine and potassium hydroxide as quantitative trapping agents for radiolabeled CO2 in metabolism studies.

The efficiency of ethanolamine and potassium hydroxide (KOH) as trapping agents for CO2 was determined using a flow of 500 mL/min through CO2 absorption towers containing trapping solutions. Radiolabeled 14CO2 was produced by acidification of suspensions containing Ba14CO3. Both 100% ethanolamine and 5M ethanolamine in 2-methoxyethanol were evaluated. With 200 mL of either solution, trapping efficiency of 14CO2 decreased when only 5% or less of the amount of ethanolamine available had reacted (22 mmoles of CO2 trapped). In contrast, use of 200 mL of 1M or 5M KOH was effective in retaining 88 mmoles of CO2. This is equivalent to the amount of CO2 produced by a rat over an 8-hr period. In summary, with flow rates commonly used in in vivo metabolism studies, the trapping efficiency of ethanolamine was far less than the theoretical efficiency. In these types of studies KOH would be a more suitable trapping agent or, if used, ethanolamine solutions must be changed frequently.

Carbon Dioxide↗

PubMed1984

Ethanolamine accumulation by photoreceptor cells of the rabbit retina.

The rabbit retina accumulates ethanolamine by an overall process that has a high affinity for ethanolamine. This process is different from the choline uptake, since ethanolamine accumulation was unaffected by high choline concentrations. Autoradiography identified the major site of high-affinity uptake as the perinuclear region of the photoreceptor cells. Ethanolamine accumulated by the high-affinity uptake was not used for neurotransmission by photoreceptor cells but was used to synthesize phosphatidylethanolamine. However, only a small percentage of the accumulated ethanolamine was converted into phospholipid. The rate of phosphorylation may contribute to control of phospholipid synthesis, since choline kinase activity is much greater than ethanolamine kinase activity in the rabbit retina.

Animals↗

PubMed1992

Autogenous regulation of ethanolamine utilization by a transcriptional activator of the eut operon in Salmonella typhimurium.

The genes required for use of ethanolamine as a carbon and nitrogen source are encoded by a single operon (eut) whose expression is induced by the simultaneous presence of both ethanolamine and cobalamin (vitamin B12). The action of B12 as an inducer of this operon reflects the fact that this cofactor is required by the degradative enzyme ethanolamine lyase (eutBC). The eutR gene encodes a protein that activates transcription of the eut operon in response to the simultaneous presence of B12 and ethanolamine. The eutR gene is expressed by a weak constitutive promoter activity (PII) and by the main regulated promoter (PI). Because it is encoded within the operon that it activates, the EutR protein controls its own production. Initial induction of the eut operon by ethanolamine plus B12 causes an increase in expression of the eutR gene; this increase acts as part of a positive feedback loop that is required for maximal operon expression. Because of this mode of regulation, constitutive regulatory mutations, described here, include mutations that generate new internal promoters and thereby increase the basal level of eutR gene expression. In mutants with an increased level of activator protein, each inducer (B12 or ethanolamine), presented singly, is sufficient for partial operon induction.

Bacterial Proteins↗

PubMed1975

Interaction between ethanolamine ammonia-lyase and methylcobalamin. Half-site reactivity with an adenosylcobalamin-dependent enzyme.

The adenosylcobalamin-dependent enzyme ethanolamine ammonia-lyase contains two active sites per molecule. The effects of methylcobalamin on the properties of this enzyme differ qualitatively depending on whether one or both of these sites is occupied by the cobamide. At 0.5 mol of methylcobalamin/mol of active sites, catalytic activity fell rapidly to approximately 30% of control levels, thereafter remaining constant for an hour. With the partially inhibited enzyme, Km values for ethanolamine and adenosylcobalamin were 5.5 muM and 1.6 muM, respectively, values that do not differ significantly from those of uninhibited enzyme. When the methylcobalamin per active site ratio was increased to 1, the decline in activity became progressive with time, eventually falling to levels much lower than seen at a cobamide per active site ratio of 0.5. Methylcobalamin also promotes the formation of a complex stable to gel filtration between ethanolamine and enzyme. Complex formation increased with increasing methylcobalamin per active site ratios up to a ratio of 0.7/1, at which point 0.5 mol of ethanol/mol of active sites was taken up. Ethanolamine uptake did not increase at higher methylcobalamin to active sites ratios. Methylcobalamin itself was taken up by enzyme, forming a complex containing 0.5 mol of methylcobalamin/mol of active sites that was stable to gel filtration. Measurement by the technique of Hummel and Dreyer ((1962) Biochim. Biophys. Acta 63, 530-532), however, showed one methylcobalamin binding site per active site. The formation of enzyme-ligand complexes stable to gel filtration was not affected by 5'-deoxyadenosine nor did 5'-deoxyadenosine by itself promote the formation of a stable complex between enzyme and ethanolamine. These observations were interpreted as evidence indicating half-site reactivity of ethanolamine ammonia-lyase with methylcobalamin. Comparison with previous results suggested that this half-site reactivity was an epiphenomenon not related to catalysis.

Ammonia-Lyases↗

PubMed1985

Purification and properties of an ethanolamine-serine base exchange enzyme of rat brain microsomes.

The activity of an ethanolamine and serine base exchange enzyme of rat brain microsomes was copurified to near homogeneity. The purification sequence involved detergent solubilization, Sepharose 4B column chromatography, phenyl-Sepharose 4B column chromatography, glycerol gradient sedimentation, and agarose-polyacrylamide gel electrophoresis under non-denaturing conditions. The ratio of the ethanolamine and serine base exchange activities remained almost constant during purification, and both enzyme activities were enriched 25-fold over the initial microsomal suspension. The final enzyme preparation which contained both enzyme activities showed a single protein band on sodium dodecyl sulfate-polyacrylamide gel, having an apparent molecular mass of about 100 kDa. Serine inhibited the ethanolamine incorporation by this preparation and ethanolamine inhibited the serine incorporation. The competitive nature of this inhibition was apparent from Lineweaver-Burk plots, suggesting that the enzyme catalyzes the incorporation of both ethanolamine and serine into their corresponding phospholipids. The Km and Ki values for ethanolamine were quite similar, being 0.02 and 0.025 mM, respectively. The Km and Ki values for serine were also quite similar being 0.11 and 0.12 mM, respectively. The pH optimum was the same at 7.0 with both substrates. The optimum Ca2+ concentration was 8 mM for serine incorporation.

Animals↗

PubMed1996

Protein kinase C inhibitors enhance the synergistic mitogenic effects of ethanolamine analogues and insulin in NIH 3T3 fibroblasts.

Monomethylethanolamine (1 mM) and dimethylethanolamine (1 mM) stimulated DNA synthesis 10- and 15-fold, respectively, in NIH 3T3 fibroblasts. In addition, simultaneous treatments with insulin (500 nM) and methylated ethanolamine analogues (1 mM or less) resulted in synergistic activation of DNA synthesis. The order of mitogenic potency of ethanolamine analogues was dimethylethanolamine > monomethylethanolamine > ethanolamine. Choline (1-5 mM) alone had no effect on DNA synthesis, but it increased the combined effects of lower concentrations of ethanolamine analogues and insulin. The synergistic effects of ethanolamine analogues, choline and insulin were considerably (1.7- to 1.9-fold) enhanced by GF 109203X (3 microM), a specific inhibitor of protein kinase C. The results suggest that ethanolamine analogues enhance insulin-induced DNA synthesis by a mechanism which is inhibited by the protein kinase C system.

3T3 Cells↗

PubMed1980

Regulation of aminophospholipid asymmetry in murine fibroblast plasma membranes by choline and ethanolamine analogues.

The regulation of the asymmetric distribution of aminophospholipids in mammalian cell plasma membranes is not understood at this time. One approach to determine the nature of such regulatory mechanisms is to attempt alteration of the plasma membrane phospholipid composition. Choline analogues such as N,N'-dimethylethanolamine and N-monomethylethanolamine lowered the quantity of phosphatidylethanolamine in the plasma membrane of LM fibroblasts grown in defined medium without serum. Ethanolamine supplementation increased the phosphatidylethanolamine content while ethanolamine analogues such as 2-amino-2-methyl-1-propanol, 2-amino-1-butanol, 1-aminopropanol, and 3-aminopropanol did not alter the aminophospholipid content significantly. The transverse distribution of aminophospholipids in the plasma membrane was determined by use of a chemical labelling reagent trinitrobenzenesulfonic acid. The percent phosphatidylethanolamine trinitrophenylated by trinitrobenzenesulfonate in the outer plasma membrane monolayer of LM cells supplemented with choline analogues was not altered. In contrast, ethanolamine analogue supplementation increased the percentage of aminophospholipid in the outer monolayer 2--3-fold. Ethanolamine analogue-containing phospholipids were distributed asymmetrically across the plasma membrane with 85 to 91% being located in the inner monolayer of the plasma membrane, a distribution similar to that of phosphatidylethanolamine. The fatty acyl composition of aminophospholipids in the outer monolayer was in all cases more saturated than in the corresponding phospholipids of the inner monolayer. However, choline analogues and especially the ethanolamine analogues reduced this difference. Thus, base analogues of choline and ethanolamine may alter the aminophospholipid asymmetry, the surface charge, and the acyl chain asymmetry of LM cell plasma membranes.

Animals↗

PubMed1980

Microbial metabolism of amino alcohols. Biosynthetic utilization of ethanolamine for lipid synthesis by bacteria.

1. Ten bacteria utilizing [2-14C]ethanol-2-amine as the sole or major source of nitrogen for growth on glycerol + salts medium incorporated radioactivity into a variety of bacterial substances. A high proportion was commonly found in lipid fractions, particularly in the case of Erwinia carotovora. 2. Detailed studies of [14C]ethanolamine incorporation into lipids by five bacteria, including E. carotovora, showed that all detectable lipids were labelled. Even where phosphatidylethanolamine was the major lipid labelled, radioactivity was predominantly in the fatty acid rather than the base moiety. The labelled fatty acids were identified in each case. 3. The addition of acetate to growth media decreased the incorporation of radioactivity from ethanolamine into both fatty acid and phosphatidyl-base fragments of lipids from all the bacteria except Mycobacterium smegmatis. Experiments with [3H]ethanolamine and [14C]acetate confirmed that unlabelled acetate decreased the incorporation of both radioactive isotopes into lipids, except in the case of M. smegmatis. 4. Enzyme studies suggested one of two metabolic routes between ethanolamine and acetyl-CoA for each of four bacteria. A role for ethanolamine O-phosphate was not obligatory for the incorporation of [14C]ethanolamine into phospholipids, but correlated with CoA-independent aldehyde dehydrogenase activity.

Acetates↗

PubMed1977

Dimethyl ethanolamine-induced asthma.

Progressively severe sneezing, rhinorrhea, cough, wheezing, and dyspnea developed in a spray-painter, apparently in relation to exposure to a particular spray paint. A monitoring of exposure at work revealed the development of symptoms and a decrease in peak flow rates. Subsequent challenges in the laboratory performed under conditions resembling occupational exposure resulted in dual asthmatic responses on exposure to the whole paint (98 per cent methyl methacrylate emulsion and 2 per cent dimethyl ethanolamine solution) and to dimethyl ethanolamine solution (2 per cent) alone. Water, methyl methacrylate emulsion, and 1,4 dioxane (0.6 per cent) used as a thinner in the dimethyl ethanolamine did not produce a response in the airways. Allergy skin tests with dimethyl ethanolamine and a mixture of dimethyl ethanolamine and human serum albumin were negative. To our knowledge, this is the first report of asthma and/or rhinitis induced specifically by dimethyl ethanolamine. The mechanism of the specific reactivity is not known.

Adult↗

PubMed1998

The effect of ethanolamine on acute carbon tetrachloride intoxication.

The effects of ethanolamine on injured liver were investigated by oral administration of ethanolamine to male ddY mice 24 h after carbon tetrachloride (CCl4) injection. The serum aminotransferase activities in mice with liver injury were reduced by ethanolamine treatment (10-30 mg/kg body weight). Drastically increased regenerative reaction of ethanolamine treated-CCl4 injured liver was also observed through an increase in 5-bromo-2'-deoxyuridine uptake. ATP concentration in liver tissue was recovered by administration of ethanolamine. These results suggest that oral administration of ethanolamine accelerates recovery from CCl4-induced liver injury.

Adenosine Triphosphate↗

PubMed2000

Effects of Ethanolamine as a nitrogen source on hydrogen production by Rhodobacter capsulatus.

Ethanolamine was examined as a nitrogen source in the production of hydrogen by Rhodobacter capsulatus ST-410, a hydrogenase-deficient mutant of the strain B-100. It was found that ethanolamine supports cell growth as the sole nitrogen source and permits a large amount of hydrogen evolution, detected at 138 micromol/ml-culture from 3.5 mM ethanolamine and 30 mM DL-malate. The amount corresponded to a stoichiometric yield of 77% and was close to that obtained from 7.0 mM L-glutamate and 30 mM DL-malate. The hydrogen evolution rate per unit biomass (cells) was higher than that with L-glutamate, and the cells grown with ethanolamine had higher nitrogenase activity than the cells grown with L-glutamate. In terms of bioconversion of cellulosic and hemicellulosic biomass to hydrogen, D-glucose, D-xylose, and D-cellobiose were tested as substrates. The results indicated that those sugars permit a large evolution of hydrogen through cultivation with ethanolamine as a nitrogen source. For instance, the cells grown with 3.5 mM ethanolamine evolved hydrogen of 289 micromol/ml-culture (80% yield) from 30 mM D-glucose under a controlled pH of 6.4 to 6.9.

Ethanolamine↗

PubMed1979

Glycerophospho-(N-acyl)-ethanolamine lipids in degenerating BHK cells.

The phospholipids, which accompany semilysobisphosphatidic acid from degenerating BHK cells, were identified as a mixture of glycerophospho-(N-acyl)-ethanolamine lipids. The identification was based on infrared spectroscopy, thin-layer chromatography and ethanolamine content of the intact lipids or their partial degradation products. Sequential treatments with mild acid and alkali revealed the presence of three different derivatives: the most abundant of these was the O-(1-alkenyl) ether derivative (plasmenyl-(N-acyl)-ethanolamine), which represented 55-60% of the total glycerophospho-(N-acyl)-ethanolamine lipids; the O-alkyl derivative (plasmanyl-(N-acyl)-ethanolamine) and the di-O-acyl derivative (phosphatidyl-(N-acyl)-ethanolamine) each represented about 20% of the total.

Chromatography, Paper↗

PubMed1966

Ethanolamine metabolism in plant tissues.

Ethanolamine is readily metabolized by oat, pea, wheat, apple and carrot tissue preparations. Ethanolamine-1,2 (14)C was incorporated into the lipid fraction, and (14)C activity was distributed in the organic acid, sugar, acid volatile, carbon dioxide and insoluble residue fractions. The distribution varied with the particular tissue. Incorporation into the lipid fraction occurred in tissue homogenates in the absence of ATP by a Ca(++) activated system similar to that reported for animal preparations. The initial step in ethanolamine oxidation involves an amine oxidase. Glycolaldehyde and glyoxylic acid are metabolic intermediates, the former in the conversion of ethanolamine to carbon dioxide. No evidence was obtained for the operation of an ethanolamine transaminase or for the involvement of phosphorylated intermediates in the conversion of ethanolamine to carbon dioxide.

Amino Alcohols↗

PubMed2002

Separate myocardial ethanolamine phosphotransferase activities responsible for plasmenylethanolamine and phosphatidylethanolamine synthesis.

Ethanolamine phosphotransferase (EPT) is a key enzyme responsible for the synthesis of ethanolamine glycerophospholipids. Plasmenylethanolamine is a predominant molecular subclass of ethanolamine glycerophospholipids in the heart. The present study was designed to identify the selective use of 1-O-alk-1'-enyl-2-acyl-sn-glycerol as a substrate for EPT as a mechanism responsible for the predominance of plasmenylethanolamine in the rabbit heart. EPT activity in rabbit myocardial membranes using 1,2-diacyl-sn-glycerol as substrate is activated by Mn2+, inhibited by dithiobisnitrobenzoic acid (DTNB) and is unaffected by Ca2+. In contrast, ethanolamine phosphotransferase activity using 1-O-alk-1'-enyl-2-acyl-sn-glycerol as substrate is inhibited by Mn2+ and Ca2+, but is activated by DTNB. Additionally, ethanolamine phosphotransferase activity using 1-O-alk-1'-enyl-2-acyl-sn-glycerol substrate was more sensitive to thermal denaturation compared with that of 1,2-diacyl-sn-glycerol. Taken together, these results suggest that separate ethanolamine phosphotransferase activities are present in heart membranes that are responsible for the synthesis of phosphatidylethanolamine and plasmenylethanolamine.

Animals↗