• Toxicological Research
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• 제6권1호
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• pp.109-119
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• 1990

Ro09-0198, a cyclic peptide isolated from culture filtrates of Streptoverticillium griseoverticillatum, induced lysis of erythrocytes. Ro-09-0198-induced hemolysis was temperature-dependent and the sensitivity of hemolysis differed greatly among animal species. Preincubation of the peptide with phosphatidylethanolamine reduced the hemolytic activity, whereas other phospholipids present in erythrocytes in nature had no effect. A study of the structural requirements on phosphatidylethanolamine necessary for interaction with the peptide indicates that Ro09-0198 recognizes strictly a particular chemical structure of phosphatidylethanolamine: dialkylphosphoethanolamine as well as 1-acylglycerophosphoethanolamine showed the same inhibitory effct on hemolysis induced by Ro09-0198 as diacylphosphatidyl-ethanolamine, whereas phosphoethanolamine gave no inhibitory effect. Neither phosphatidyl-N-monomethylethanolamine nor alkylphosphopropanolamine had an inhibitory effect. Proton resonances of the peptide were observed in dimethyl sulfoxide solution in the presence of 1-dodecanoyl-sn-glycerophosphoethanolamine. This peptide caused permeability increase and aggregation of liposomes containing phosphatidylethanolamine. A glycerol backbone and a primary amino group of phosphatidylethanolamine are necessary for interaction with Ro09-0198 to cause membrane damage. Ro09-0198 induced a selective permeability change on liposomes. Glucose and umbelliferyl phosphate were effluxed significantly, but sucrose was only slightly permeable and inulin could not be released. Platelet aggregation and serotonin release simultaneously induced by Ro09-0198. Addition of peptide to rat platelet, loaded with the fluorescent $Ca^{++}$ chelator quin-2, caused immediate rise in cytosolic free $Ca^{++}$ to liposomal membrane containing phosphatidylethanolamine was observed dose dependently.

• BMB Reports
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• 제31권2호
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• pp.170-176
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• 1998

Phosphatidylethanolamine N-methyltransferase (PEMT) is known to be a membrane-associated protein. However, cytosolic PEMT was detected when sufficient amounts of exogenous phospholipids were added in the incubation media. The methylation of phospholipids was measured by the incorporation of the $[^3H]-methyl$ group from S-adenosylmethionine and the methylated phospholipids were analyzed by thinlayer chromatography. The essence of the assay condition for the cytosolic enzyme was the inclusion of 200 ${\mu}g$ of each substrate, phosphatidylethanolamine (PE), phosphatidyl N-monomethylethanolamine (PME) and phosphatidyl N,N-dimethylethanolamine (PDE), in the reaction mixture of 100 ${\mu}l$. The subcellular fractionation of brain PEMT activities revealed that approximately 38.1 % for PME, 39.5% for PDE, and 22.4% for PC formation was present in the cytosolic fraction. The general properties of cytosolic PEMT were characterized and compared with those of neuronal nuclei PEMT.

• Bulletin of the Korean Chemical Society
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• 제20권6호
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• pp.683-688
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• 1999

In deuterium NMR spectra of phosphatidylethanolamine bilayers with an extremely high content of saturated fatty acids, each C1 deuteron of the glycerol backbone gave rise to a doublet. This suggests the presence of two backbone conformations, the exchange between which is slow on an NMR time scale. The origin of the two conformations has been investigated in this work using saturated 1,2-diacyl-sn-glycero-3-phosphoethanolamine specifically deuterated in the glycerol backbone. The results showed that the two conformations originate from different domains, which have different fatty acid compositions. The differential scanning calorimetry of the bilayers suggested that the size of the domain is not large enough to show an independent phase transition. Thus, the formation of microdomains in the phosphatidylethanolamine bilayers has been concluded. Conformational difference in different domains was shown to be restricted to the C1 position of the glycerol backbone. The microdomains of phosphatidylethanolamine were retained even in the presence of other phospholipids.

• 미생물학회지
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• 제22권3호
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• pp.151-156
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• 1984

When enterobacterium, Escherichia coli B was cultivated with normal media in the presence of $0.2{\sim}0.6%$ Palmitoylcarnitine and $0.05{\sim}0.2%$ Ginseng Saponin, maximum population growth of the bacteria was presented 71% and 31%, respectively. Such a result, in vitro test, was concluded from the result that both detergents stimulated $C^{14}$-glucose, $C^{14}$-alanine and $C^{14}$-phosphatidylethanolamine uptake into the membrane of cells. The pre-treatment of cells with different amounts of Palmitoylcarnitine from $0.005{\sim}0.05{\mu}$ moles represented a significant increase of uptake, 33% of $C^{14}$-glucose, 129% of $C^{14}$-alanine and 158% of phosphatidylethanolamine at the concentration of $0.05{\mu}$ moles of Palmitoylcarnitine. On the other hand, the result of $C^{-2}%$ Saponin treatment showed the maximum value of uptake, 17% of $C^{14}$-glucose and 112% of $C^{14}$-alanine. In case of $C^{14}$-phosphatidylethanolamine, the maximum uptake showed 25% of increase at the concentration of $C^{14}$% Saponin.

• 한국응용과학기술학회지
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• 제31권1호
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• pp.44-49
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• 2014

인지질(L-${\alpha}$-phosphatidylethanolamine, LAPE) 단분자층 LB막의 전기화학적 특성을 통하여 그 안정성을 순환전압전류법으로 조사하였다. LAPE 단분자층 LB막은 ITO glass에 LB법을 사용하여 제막하였다. 전기화학적특성은 0.5 N, 1.0 N, 1.5 N 및 2.0 N $KClO_4$ 용액에서 3 전극 시스템으로 순환전압전류법에 의해 측정하였다. 측정범위는 연속적으로 1650 mV로 산화시키고, 초기 전위인 -1350 mV로 환원시켰다. 주사속도는 각각 50, 100, 150, 200 및 250 mV/s로 설정하였다. 그 결과 LAPE LB막은 순환전압전류곡선으로부터 산화전류로 인한 비가역공정으로 나타났다. LAPE LB막은 전해질농도가 0.01 N, 0.05 N. 0.10 N, 0.15 N 과 0.20 N $KClO_4$ 용액에서 확산계수(D)는 각각 195, 15.9, 5.75, 1.38 및 $0.754cm^2s^{-1}{\times}10^{-9}$을 얻었다.

• Animal cells and systems
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• 제8권2호
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• pp.105-109
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• 2004

Aminoalcoholphosphotransferase catalyzes the synthesis of phosphatidylcholine and phosphatidylethanolamine from diacylglycerol plus a CDP-aminoalcohol such as CDP-choline or CDP-ethanolamine. Previously we suggested the presence of possible isoforms of this enzyme from Chinese cabbage roots and now report the cDNA cloning and expression analysis of AAPT3 encoding a third isoform of aminoalcoholphosphotransferase (AAPT3). AAPT3 contains an open reading frame of 1,176 bp coding for a protein of 392 amino acids. It shares 96 and 95% identity with Chinese cabbage AAPT1 and AAPT2, respectively, at the deduced amino acid level. The results from reverse transcriptase-polymerase chain reaction analysis indicate that expression of AAPT3 is up-regulated by low temperature as well as AAPT1 and AAPT2.

• Bulletin of the Korean Chemical Society
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• 제12권6호
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• pp.714-716
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• 1991

• 한국식품과학회지
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• 제40권6호
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• pp.611-620
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• 2008

달걀 노른자에 함유된 인지질 중 PC와 PE를 추출, 분리하고 이를 토코페롤을 제거한 TSCO에 0, 200, 500, 2,000 ppm의 농도로 단독으로, 또는 1,000 ppm씩 혼합하여 첨가한 후 $180^{\circ}C$에서 12시간 동안 가열하여 함유된 인지질의 함량변화와 TSCO의 갈색화 정도를 살펴보고, TSCO의 가열산화에 미치는 영향을 지방산 조성, 공액이중산값, 아니시딘값으로 평가하였다. TSCO에 첨가된 인지질은 가열 시작 후 2-3시간 내에 매우 빠르게 소실되었고, 가열 중 PE의 분해속도가 PC에 비해 높았다. PC와 PE가함께 첨가된 TSCO를 가열할때 PE는 PC의 분해를 억제하였다. TSCO는 가열 시간이 증가함에 따라 갈색화가 증가하였고, PC와 PE는 갈색화를 촉진하였으며 PE가 PC보다 큰 영향을 주었다. 가열 중 TSCO의 P/L, P/Ln, 공액이중산값, 아니시딘값은 증가하였으며, PC의 첨가는 이들 값을 낮추어 가열 카놀라유의 산화방지제 역할을 하였으나 PE는 큰 영향을 나타내지 않았으며, PC와 PE는 TSCO의 가열산화 억제에 있어서 antagonism이 관찰되었다.

• Journal of Applied Biological Chemistry
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• 제42권2호
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• pp.75-80
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• 1999

The effects of dietary n-3 fatty acids, ${\alpha}$-linolenic acid (18:3), eicosapentaenoic acid (EPA, 20:5), and docosahexaenoic acid (DHA, 22:6), on brain phospholipid content and fatty acid composition were compared in rats fed with a diet containing constant ratios of saturated fatty acid/monounsaturated fatty acid/polyunsaturated fatty acid (PUFA) and n-3/n-6. The dietary fat in each diet was added at the level of 10%. In each diet, n-3 PUFA comprised two-thirds of the PUFA and the remaining one-third was linoleic acid (18:2). Dietary fat containing linoleic acid as the sole source of PUFA was also given to the control group. The content of brain phospholipid in the three n-3 PUFA groups was significantly lower than that of the linoleic acid group. This reduction was greater in the EPA and DHA groups than in the ${\alpha}$-linolenic acid group. The decrease in phospholipid content in rats fed n-3 fatty acid-rich diets was largely due to the decrease in the phosphatidylethanolamine fraction. Each dietary n-3 PUFA was found to affect the fatty acid composition of brain phospholipids; the most pronounced alteration was observed in phosphatidylethanolamine fraction. Furthermore, the proportion of DHA in the phosphatidylethanolamine fraction tended to be higher in the DHA group than in other PUFA groups. In conclusion, dietary ${\alpha}$-linolenic acid, EPA and DHA can influence the phospholipid content, phospholipid subclass, and fatty acid composition in rat brain.

• Molecules and Cells
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• 제27권2호
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• pp.251-255
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• 2009

Sepsis is the leading cause of death in critically ill patients. Today, around 60% of all cases of sepsis are caused by Gram-negative bacteria. The cell wall component lipopolysaccharide (LPS) is the main initiator of the cascade of cellular reactions in Gram-negative infections. The core receptors for LPS are toll-like receptor 4 (TLR4), MD-2 and CD14. Attempts have been made to antagonize the toxic effect of endotoxin using monoclonal antibodies against CD14 and synthetic lipopolysaccharides but there is as yet no effective treatment for septic syndrome. Here, we describe an inhibitory effect of a phosphatidylethanolamine derivative, PE-DTPA (phosphatidylethanolamine diethylenetriaminepentaacetate) on LPS recognition. PE-DTPA bound strongly to CD14 ($K_d$, $9.52{\times}10^{-8}M$). It dose dependently inhibited LPS-mediated activation of human myeloid cells, mouse macrophage cells and human whole blood as measured by the production of tumor necrosis factor-${\alpha}$ (TNF-${\alpha}$) and nitric oxide, whereas other phospho-lipids including phosphatidylserine and phosphatidylethanolamine had little effect. PE-DTPA also inhibited transcription dependent on $NF-{\kappa}B$ activation when it was added together with LPS, and it rescued LPS-primed mice from septic death. These results suggest that PE-DTPA is a potent antagonist of LPS, and that it acts by competing for binding to CD14.