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At least 19 recordsLinked to original sources
PubMed1984

Ethanolamine glycerophospholipid formation by decarboxylation of serine glycerophospholipids in myelinating organ cultures of cerebellum.

Serine decarboxylation as a source of glycerophospholipid ethanolamine is known to occur in mammals. However, early investigators failed to demonstrate the pathway in brain. In the present study serine is shown to be decarboxylated to glycerophospholipid ethanolamine in myelinating organ cultures of rat cerebellum up to 32 days in vitro. The pattern of incorporation of L-[3-14C]serine into culture phospholipids strongly suggests a precursor-product relationship between serine glycerophospholipids (SGP) and ethanolamine glycerophospholipids (EGP), with serine label appearing in the ethanolamine moiety of EGP. The time course of labelling was similar for both acid-stable and acid-labile EGP. In contrast DL-[1-14C]serine failed to label EGP significantly due to the loss of serine carbon C1 on decarboxylation. Through the systematic hydrolysis of phospholipids from cerebellar cultures incubated with L-[3-14C], it was clear that in SGP, acid-stable EGP, and acid-labile EGP greater than to 70% of radiolabel resides in the base moiety of each of these molecular species. It is proposed that serine decarboxylation as a source of EGP ethanolamine may be important in the early stages of brain development.

Animals↗
PubMed1981

Oligodendroglial glycerophospholipid synthesis: incorporation of radioactive precursors into ethanolamine glycerophospholipids by calf oligodendroglia prepared by a Percoll procedure and maintained in suspension culture.

Oligodendroglia prepared from minced calf cerebral white matter by trypsinization at pH 7.4, screening, and isosmotic Percoll (polyvinylpyrolidone-coated silica gel) density gradient centrifugation survived in culture on polylysine-coated glass, extending processes and maintaining phenotypic characteristics of oligodendroglia. In the present study, ethanolamine glycerophospholipid (EGP) metabolism of the freshly isolated cells was examined during short-term suspension culture by dual label time course and substrate concentration dependence experiments with [2-3H]glycerol and either [1,2-14C]ethanolamine or L-[U-14C]serine. Rates of incorporation of 3H from the glycerol and of 14C from the ethanolamine into EGP were constant for 14 h. In medium containing 3 mM-[1,2-14C]ethanolamine and 4.8 mM-[2-3H]glycerol, rates of incorporation of 14C and 3H into diacyl glycerophosphoethanolamine (diacyl GPE) were similar. Under the same conditions, 3H specific activities of alkylacyl GPE and alkenylacyl GPE were much lower than 14C specific activities, likely as a result of the loss of tritium during synthesis of these forms of EGP via dihydroxyacetone phosphate. L-[U-14C]serine was incorporated into serine glycerophospholipid (SGP) by base exchange rather than de novo synthesis. 14C from L-[U-14C]serine also appeared in EGP after an initial lag period of several hours. Methylation of oligodendroglial EGP to choline glycerophospholipid (CGP) was not detected.

Animals↗
PubMed1985

Concurrent disappearance of N-acylethanolamine glycerophospholipids and phagolysosomes enriched in N-acylethanolamine glycerophospholipids as Dictyostelium discoideum cells aggregate.

As the cellular slime mold, Dictyostelium discoideum, undergoes development, a phospholipid fraction containing 80% N-acylethanolamine glycerophospholipids (NAEGPs) and 20% acylphosphatidylglycerol (APG) disappears during the aggregation stage. In this study, the subcellular distribution of that NAEGP phospholipid fraction and the precise time period of disappearance of the fraction were determined. The content of the NAEGP fraction was determined in aggregating cells at 2-h intervals from the beginning of the developmental phase through 14 h, when the cells were completely aggregated. The NAEGP fraction comprised about 8% of the phospholipids in amoebae just starting the development cycle and about 12% in cells between 2 and 6 h of development; then its level decreased until it could not be detected at 12 and 14 h of development. The mole percentage of the total lipid phosphate in the NAEGP fraction was determined in isolated subcellular organelles. The phagolysosomes were enriched in the NAEGP fraction 1.7-2-fold over the level found in the amoebae and about 8-fold over the level in fractions highly enriched in the plasma membrane, mitochondria or peroxisomes. The content of phagolysosomes was determined by electron microscopy of aggregating cells. The amoebae contained large amounts of phagolysosomes up to 6 h of development, and then they gradually disappeared between 6 and 12 h of development. This combination of quantitative phospholipid analysis, subcellular organelle isolation and electron microscopy has revealed that in D. discoideum amoebae, the phagolysosomes were selectively enriched in the NAEGP fraction and both the NAEGP-enriched phagolysosomes and the NAEGPs disappeared concurrently between 6 and 12 h of development.

Dictyostelium↗
PubMed2006

Hydrolysis of minor glycerophospholipids of plasma lipoproteins by human group IIA, V and X secretory phospholipases A2.

We investigated the hydrolysis of the minor glycerophospholipids of human HDL(3), total HDL and LDL using human group IIA, V and X secretory phospholipases A(2) (sPLA(2)s). For this purpose we employed the enzyme and substrate concentrations and incubation times optimized for hydrolysis of phosphatidylcholine (PtdCho), the major glycerophospholipid of plasma lipoproteins. In contrast to PtdCho, which was readily hydrolyzed by group V and X sPLA(2)s, and to a lesser extent by group IIA sPLA(2), the minor ethanolamine, inositol and serine glycerophospholipids exhibited marked resistance to hydrolysis by all three sPLA(2)s. Thus, when PtdCho was hydrolyzed about 80%, the ethanolamine and inositol glycerophospholipids reached a maximum of 40% hydrolysis. The hydrolysis of phosphatidylserine (PtdSer), which was examined to a more limited extent, showed similar resistance to group IIA, V and X sPLA(2)s, although the group V sPLA(2) attacked it more readily than group X sPLA(2) (52% versus 39% hydrolysis, respectively). Surprisingly, the group IIA sPLA(2) hydrolysis remained minimal at 10-15% for all minor glycerophospholipids, and was of the order seen for the PtdCho hydrolysis by group IIA sPLA(2) at the 4-h digestion time. All three enzymes attacked the oligo- and polyenoic species in proportion to their mole percentage in the lipoproteins, although there were exceptions. There was evidence of a more rapid destruction of the palmitoyl compared to the stearoyl arachidonoyl glycerophospholipids. Overall, the characteristics of hydrolysis of the molecular species of the lipoprotein-bound diradyl GroPEtn, GroPIns and GroPSer by group V and X sPLA(2)s differed significantly from those observed with lipoprotein-bound PtdCho. As a result, the acidic inositol and serine glycerophospholipids accumulated in the digestion residues of both LDL and HDL, and presumably increased the acidity of the residual particles. An accumulation of the ethanolamine glycerophospholipids in the sPLA(2) digestion residues also had not been previously reported. These results further emphasize the diversity in the enzymatic activity of the group IIA, V and X sPLA(2)s. Since these sPLA(2)s possess comparable tissue distribution, their combined activity may exacerbate their known proinflammatory and proatherosclerotic function.

Atherosclerosis↗
PubMed1986

Relative degradation of different arachidonoyl molecular species of choline glycerophospholipids in opsonized zymosan-stimulated rabbit alveolar macrophages.

The relative degradation of arachidonoyl molecular species of glycerophospholipids prelabeled with [3H]20:4 caused by opsonized zymosan was studied in rabbit alveolar macrophages using a recently developed high-performance liquid chromatographic method. The opsonized zymosan caused the release of [3H]20:4 only from choline glycerophospholipids, no significant changes being observed in the radioactivities of other glycerophospholipids and triacylglycerol. Choline glycerophospholipids were resolved into seven arachidonoyl molecular species, which differed as to the alkyl ether or acyl residue bound at the 1-position, by high-performance liquid chromatography. Arachidonate was predominantly located in the alkyl type having 16:0 at the 1-position which comprised more than half of the total arachidonoyl molecular species of choline glycerophospholipids. The radioactivities of all arachidonoyl molecular species of choline glycerophospholipids, except for the 18:2-20:4 and 18:1-20:4 species of diacylglycerophosphocholine, decreased to 80-85% of the control values as a result of the challenge with opsonized zymosan for 1 h. However, 50% of the released 20:4 came from the 16:0-20:4 species of alkylacylglycerophospholipids, which were the most predominant species of choline glycerophospholipids. The present results indicate that the 16:0-20:4 species of alkylacylglycerophosphocholine is a significant source of arachidonate and 1-O-alkyl-2-lysoglycerophosphocholine, the precursor of the platelet-activating factor, relative to other arachidonoyl species in activated alveolar macrophages.

Animals↗
PubMed2004

Cross talk between sphingolipids and glycerophospholipids in the establishment of plasma membrane asymmetry.

Glycerophospholipids and sphingolipids are distributed asymmetrically between the two leaflets of the lipid bilayer. Recent studies revealed that certain P-type ATPases and ATP-binding cassette (ABC) transporters are involved in the inward movement (flip) and outward movement (flop) of glycerophospholipids, respectively. In this study of phytosphingosine (PHS)-resistant yeast mutants, we isolated mutants for PDR5, an ABC transporter involved in drug efflux as well as in the flop of phosphatidylethanolamine. The pdr5 mutants exhibited an increase in the efflux of sphingoid long-chain bases (LCBs). Genetic analysis revealed that the PHS-resistant phenotypes exhibited by the pdr5 mutants were dependent on Rsb1p, a putative LCB-specific transporter/translocase. We found that the expression of Rsb1p was increased in the pdr5 mutants. We also demonstrated that expression of RSB1 is under the control of the transcriptional factor Pdr1p. Expression of Rsb1p also was enhanced in mutants for the genes involved in the flip of glycerophospholipids, including ROS3, DNF1, and DNF2. These results suggest that altered glycerophospholipid asymmetry induces the expression of Rsb1p. Conversely, overexpression of Rsb1p resulted in increased flip and decreased flop of fluorescence-labeled glycerophospholipids. Thus, there seems to be cross talk between sphingolipids and glycerophospholipids in maintaining the functional lipid asymmetry of the plasma membrane.

4-Chloro-7-nitrobenzofurazan↗
PubMed1995

Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and Neisseria gonorrhoeae: identification, characterization, and mutagenesis of a lysophosphatidic acid acyltransferase.

Lysophosphatidic acid (LPA) acyltransferases of Neisseria meningitidis and Neisseria gonorrhoeae were identified which share homology with other prokaryotic and eukaryotic LPA acyltransferases. In Escherichia coli, the conversion of LPA to phosphatidic acid, performed by the 1-acyl-sn-glycerol-3-phosphate acyltransferase PlsC, is a critical intermediate step in the biosynthesis of membrane glycerophospholipids. A Tn916-generated mutant of a serogroup B meningococcal strain was identified that exhibited increased amounts of capsular polysaccharide, as shown by colony immunoblots, and a threefold increase in the number of assembled pili. The single, truncated 3.8 kb Tn916 insertion in the meningococcal mutant was localized within a 771 bp open reading frame, The gonococcal equivalent of this gene was identified by transformation with the cloned meningococcal mutant gene. In N. gonorrhoeae, the mutation increased piliation fivefold. The insertions were found to be within a gene that was subsequently designated nlaA (neisserial LPA acyltransferase). The predicted neisserial LPA acyltransferases were homologous (>20% identity, >40% amino acid similarity) to the family of PlsC protein homologues. A cloned copy of the meningococcal nlaA gene complemented in trans a temperature-sensitive E. coli PlsCts- mutant. Tn916 and omega-cassette insertional inactivations of the neisserial nlaA genes altered the membrane glycerophospholipid compositions of both N. meningitidis and N. gonorrhoeae but were not lethal. Therefore, the pathogenic Neisseria spp. appear to be able to utilize alternative enzyme(s) to produce phosphatidic acid. This hypothesis is supported by the observation that, although the amounts of mature glycerophospholipids were altered in the meningococcal and the gonococcal nlaA mutants, glycerophospholipid synthesis was detectable at significant levels. In addition, acyltransferase enzymatic activity, while reduced in the gonococcal nlaA mutant, was increased in the meningococcal nlaA mutant. We postulate that the pathogenic Neisseria spp. are able to utilize alternate acyltransferases to produce glycerophospholipids in the absence of nlaA enzymatic activity. Implementation of these secondary enzymes results in alterations of glycerophospholipid composition that lead to pleiotropic effects on the cell surface components, including effects on capsule and piliation.

Acyltransferases↗
PubMed1985

Heterogeneity in the metabolism of the arachidonoyl molecular species of glycerophospholipids of rabbit alveolar macrophages. The interrelationship between metabolic activities and chemical structures of the arachidonoyl molecular species.

The relative incorporation of [3H]arachidonic acid (20:4) into individual molecular species containing 20:4 at the 2 position (18:1-20:4, 16:0-20:4 and 18:0-20:4 species) of diacyl and ether-linked glycerophosphocholine, glycerophosphoethanolamine and glycerophosphoinositol of rabbit alveolar macrophages has been measured by reversed-phase high-performance liquid chromatography (HPLC). The rate of incorporation of [3H]20:4 into the molecular species of glycerophospholipids was greatly influenced by their structures. The reversed-phase HPLC analysis allowed elucidation of the influence of structural differences, such as the nature of the polar head group, the fatty chain at the 1 position and the chemical form of the bond of the fatty chain attached at the 1 position on the uptake of [3H]20:4 by comparison of the specific radioactivities of arachidonoyl molecular species having the same structures, except that one of the three kinds of moiety was different. The specific radioactivities of the molecular species containing choline head groups were significantly higher than those containing ethanolamine and inositol moieties. The specific radioactivities of diacyl molecular species were considerably higher than those of ether-linked molecular species. The nature of the fatty chain attached at the 1 position also influenced the uptake of [3H]20:4 into glycerophospholipids. The arachidonoyl molecular species containing 18:1 at the 1 position were preferentially labelled with [3H]20:4 as compared to the corresponding 16:0-20:4 and 18:0-20:4 species either of diacyl or ether-linked glycerophospholipids. The present results suggest that the acyltransferase involved in the incorporation of 20:4 into glycerophospholipids has selectivity for the structures of glycerophospholipids and the order of selectivity of this enzyme for the arachidonoyl molecular species, deduced in the present experiments, was as follows: choline head group greater than ethanolamine and inositol groups, acyl bond greater than ether and vinyl ether bonds, 18:1 fatty chain greater than 16:0 and 18:0 fatty chains at the 1 position. Comparison of the metabolic activities of all major arachidonoyl molecular species of glycerophospholipids having a single structure is reported here for the first time.

Animals↗
PubMed2000

Glycerophospholipids in brain: their metabolism, incorporation into membranes, functions, and involvement in neurological disorders.

Neural membranes contain several classes of glycerophospholipids which turnover at different rates with respect to their structure and localization in different cells and membranes. The glycerophospholipid composition of neural membranes greatly alters their functional efficacy. The length of glycerophospholipid acyl chain and the degree of saturation are important determinants of many membrane characteristics including the formation of lateral domains that are rich in polyunsaturated fatty acids. Receptor-mediated degradation of glycerophospholipids by phospholipases A(l), A(2), C, and D results in generation of second messengers such as arachidonic acid, eicosanoids, platelet activating factor and diacylglycerol. Thus, neural membrane phospholipids are a reservoir for second messengers. They are also involved in apoptosis, modulation of activities of transporters, and membrane-bound enzymes. Marked alterations in neural membrane glycerophospholipid composition have been reported to occur in neurological disorders. These alterations result in changes in membrane fluidity and permeability. These processes along with the accumulation of lipid peroxides and compromised energy metabolism may be responsible for the neurodegeneration observed in neurological disorders.

Animals↗
PubMed1982

Studies on molecular species of choline and ethanolamine glycerophospholipids obtained from rat brain myelin and synaptosomes by gas-liquid chromatography mass spectrometry.

By converting to t-butyldimethylsilyl derivatives, molecular species of ethanolamine glycerophospholipid including both 1,2-diacyl and 1-alk-1'-enyl-2-acyl (plasmalogen) types were able to be analysed by a gas chromatography mass spectrometry selected ion monitoring technique. The samples analysed were ethanolamine glycerophospholipid and also choline glycerophospholipid obtained from myelin and synaptosomes of rat brain, both of which are characteristic subcellular organella of the nervous system. Main molecular species of ethanolamine glycerophospholipid were as follows: in myelin as 1,2-diacyl type, 36:1 (mainly 18:0/18:1), and as 1-alk-1'-enyl-2-acyl type, 34:2 (mainly vinyl 16:0/18:1), 36:2 (mainly vinyl 18:0/18:1) and 36:3 (mainly vinyl 18:1/18:1), whereas in synaptosomes as 1,2-diacyl type 36:1 (mainly 18:0/18:1), 38:4 (mainly 18:0/20:4) and 40:6 (18:0/22:6), and as 1-alk-1'-enyl-2-acyl type 34:2 (mainly vinyl 16:0/18:1), 36:2 (mainly vinyl 18:0/18:1), and 36:3 (mainly vinyl 18:1/18:1). The molecular species of choline glycerophospholipid consisted almost entirely of 1,2-diacyl type and they were in myelin 34:1 (mainly 16:0/18:1), 36:1 (mainly 18:0/18:1) and 36:2 (mainly 18:1/18:1), whereas in synaptosomes 32:0 (mainly 16:0/16:0), 34:0 (16:0/18:0), 34:1 (mainly 16:0/18:1) and 36:1 (mainly 18:0/18:1). In myelin as 1-alkyl-2-acyl type, 34:1 (1-hexadectl-2-octadecenoyl) was present at about 7%.

Animals↗
PubMed1979

Choline and ethanolamine glycerophospholipid synthesis in isolated synaptosomes of rat brain.

Substantial activities of cholinephosphotransferase (EC 2.7.8.2) and ethanolaminephosphotransferase (EC 2.7.8.1) were found with lysed synaptosomes but not with intact synaptosomes isolated from adult rat brains. Synaptosomal and non-synaptosomal microsomal transferases were similar in kinetic properties. Substantial activities of synaptosomal transferases have not been described previously. Part of the glycerophospholipids in synaptosomal membranes may be synthesized in the nerve ending in addition to the glycerophospholipids supplied by axonal transport. The synthesis of the alkylacyl type of choline and ethanolamine glycerophospholipids was moderately inhibited by 1 mM ATP and 1 microM cyclic AMP. This synthesis was also inhibited by more than 50% by 1 mM norepinephrine and to a lesser extent by 5 mM hydroxytryptamine and 1 mM acetylcholine. Cyclic AMP may mediate the effects of biogenic amines. The relative synthesis of different glycerophospholipid classes and the relative proportion of alkylacyl type (plasmalogen precursors) and diacyl type of glycerophospholipids may be influenced by the levels of adenine nucleotides and/or biogenic amines. Elevated cyclic AMP levels will decrease the synthesis of plasmalogen precursors.

Adenine Nucleotides↗
PubMed1992

Glycerophospholipid metabolism: back to the future.

It has become customary to regard the various glycerophospholipids as quite similar, and the acyl groups are considered to have little influence on the behaviour of the lipids in membranes or metabolism. Nevertheless, a number of recent observations by the authors and others indicate a high degree of metabolic compartmentation and substrate specificity with regard to the acyl substituents (acyl specificity) of glycerophospholipid metabolising enzymes in intact cells. 1. [32P]Orthophosphate and [3H]glycerol are incorporated into phosphatidylcholine (PC) and phosphatidylethanolamine (PE) of platelets and Swiss 3T3 fibroblasts with a [32P]/[3H]-ratio several fold lower than in glycerol-3-phosphate, phosphatidic acid (PA) and phosphatidylinositol (PI), suggesting distinct metabolic separation (probably by cellular compartmentation) of the glycerol and choline (or ethanolamine) branches of de novo phospholipid biosynthesis. 2. In fibroblasts the [32P]/[3H]-ratio varied 50-fold among the molecular species of PC, PE, PI and PA, which indicates that the enzymes involved in these conversions have some degree of acyl specificity. 3. In vitro assays for lipid-converting enzymes employ detergents, which affect acyl specificity of the enzymes (lipid kinases) both by their chemical nature and concentrations. 4. Thrombin stimulation of platelets causes formation of a multitude of diacylglycerol (DAG) molecular species, but only one major molecular species of PA is formed indicating that the DAG kinase may have distinct acyl specificity in the intact cell. 5. However, this specificity could also result from the net reactions of DAG kinase(s) and PA phosphohydrolase(s), which would constitute an ATP-utilising, paired regulation of the molecular species of PA and the inositol lipids on one hand, and PC, PE phosphatidylserine and triacylglycerol on the other. These findings indicate a high complexity of glycerophospholipid metabolism and a distinct acyl specificity in intact cells that are not apparent from studies in vitro. A major challenge for future research in this area is to bridge the apparent discrepancy between in vivo and in vitro observations regarding glycerophospholipid metabolism, an endeavour that will require more knowledge about the physical chemistry of naturally occurring molecular species than is available today. The most prevailing appreciation of glycerophospholipids among biological scientists to-day is that they can be distinguished functionally, topographically and metabolically only by their head groups and that they form the bilayer in biological membranes. Most of us know that the fatty acid in the sn-2 position is unsaturated and have been indoctrinated that the higher the degree of unsaturation, the greater the fluidity of the membrane.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed2002

Comparison of the oxidizability of various glycerophospholipids in bilayers by the oxygen uptake method.

The aims of this study were twofold: develop a convenient and rapid procedure for assessing the oxidizability of small quantities of glycerophospholipids in bilayers by the oxygen uptake method, and determine and compare the oxidizability of various glycerophospholipids in bilayers. Our purpose was to elucidate phospholipid oxidation characteristics in membranes. The quantitative autoxidation kinetics of dilinoleoyl phosphatidylcholine (DLPC) (18:2/18:2) was studied in large unilamellar vesicles (LUV) in aqueous dispersions with water-soluble initiator--2,2'-azobis(2-amidinopropane) dihydrochloride--and inhibitor 2-carboxy-2,5,7,8-tetramethyl-6-chromanol. The kinetic data indicated a high efficiency of free radical production, resulting in shortening of measuring time; the very low kinetic chain length, particularly in the induction period, suggested the possibility of including large errors in the kinetics data. Nevertheless, the autoxidation of DLPC obeyed the classic rate law: Rp = kp[LH]Ri(1/2)/(2kt)(1/2) (where Rp = rate of oxygen consumption, kp = rate constant for chain propagation, [LH] = substrate concentration; Ri(1/2) = square root of rate of chain initiation, and 2kt = rate constant for chain termination) in a mixed bilayer system with saturated dimyristoyl PC (14:0/14:0), which provided precise and reproducible data. Therefore, the system was used to assess the relative oxidizability of each glycerophospholipid DLPC (18:2/18:2), dilinolenoyl PC (18:3/18:3),1-palmitoyl-2-linoleoyl PC (16:0/18:2), 1-palmitoyl-2-arachidonoyl PC (16:0/20:4), 1-palmitoyl-2-docosahexaenoyl PC (16:0/22:6), and dilinoleoyl PE (18:2/18:2) in bilayers. The results suggested that the oxidizability of glycerophospholipid in bilayers is substantially influenced by the number of intramolecular oxidizable acyl chains and the content of bis-allylic hydrogen in a structured environment, and showed deviation of the rate law for autoxidation in PC and PE mixed LUV, which possibly was due to non-homogeneous phospholipid distribution in vesicles.

Chromatography, Thin Layer↗
PubMed1989

Molecular species of glycerophospholipids and sphingomyelins of human plasma: comparison to red blood cells.

In addition to diacyl glycerophosphocholine and sphingomyelin, human plasma also contains small amounts of other glycerophospholipids, which may have special metabolic function. The structure and origin of these minor plasma lipids has not been determined. Knowledge of the detailed composition of the phospholipids of red blood cells (Myher et al., Lipids 24, 1989) permits evaluation of one of the possible sources. This study reports the detailed analyses of plasma glycerophospholipids made in parallel to those of the erythrocyte lipids obtained from the same blood using HPLC and GLC methods. The proportions of the major phospholipid classes in the plasma and erythrocytes were similar to published values, including the essential absence of diradyl glycerophosphoserine from plasma. Plasma diradyl glycerophosphocholine contained 93.0% diacyl, 3.4% alkylkacyl and 3.6% alkenylacyl, whereas the diradyl glycerophosphoethanolamine consisted of 71.8% alkenylacyl, 19.9% diacyl and 8.3% alkylacyl subclasses. The diradyl glycerophosphoinositol was 100% diacyl. The content of the minor subclasses of plasma diradyl glycerophosphocholine is similar to that of the red cells, but the ether content of the diradyl glycerophosphoethanolamine is higher in plasma than in cells. The lipid ether subclasses of plasma glycerophospholipids also contained a higher proportion of the C20, C22 and C24 alkyl and alkenyl chains than those of the cells. Furthermore, the C16 and C18-containing species in diradyl glycerophosphoethanolamine subclasses varied with the nature of the polyunsaturated acid, whereas in diradyl glycerophosphocholine subclasses the polyunsaturated acids were combined with the C16 and C18 acids in equal proportions. The significant differences in the molecular species of glycerophospholipids and sphingomyelin between plasma and red cells would appear to limit any direct transfer or equilibration of their lipid components.

Erythrocytes↗
PubMed1980

Triacylglycerols and glycerophospholipids in ovaries from maturing and superovulated immature rats.

The concentration and composition of triacylglycerols and glycerophospholipids in the rat ovary were measured during the development of follicles to corpora lutea. Changes occurring during normal development, as the rats aged from 20 to 41 days, were compared with those following treatment of 20-day-old rats with gonadotrophin to stimulate superovulation. In the ovaries of immature superovulated rats, where many follicles developed into corpora lutea in synchrony, the glycerophospholipids increased in concentration throughout growth and luteinization. At the same time the total amount of triacylglycerol rose 10-fold but only increased in concentration during the 24 h after administration of pregnant mare's serum gonadotrophin. In both classes of lipid the proportion of polyunsaturated fatty acids rose throughout. Six days after administration of gonadotrophin 20% of the fatty acid in glycerophospholipid was arachidonic acid (20:4), while the amount of 22:5 acid had risen from 3 to 17% in the triacylglycerols. During normal aging, changes in the developing follicles were masked by the number of other cell types present. In the whole ovary the glycerophospholipids did not change between 20 and 41 days, but the triacylglycerol concentration rose. However, there was a marked similarity between the concentrations of both lipid classes in corpora lutea dissected out of the 41-day-old ovary and those of the superovulated rats. The changes in proportion of the polyunsaturated fatty acids were also the same during normal and stimulated development of the corpora lutea. In the day-41 corpus luteum the phospholipid contained 22% arachidonic acid (20:4), and 20% of the fatty acids in the triacylglycerol was 22:5. The changes in composition of fatty acids suggests that when a follicle begins to develop there is transfer of polyunsaturated fatty acids from cholesterol esters in the interstitial tissue to the triacylglycerols.

Animals↗
PubMed1991

Suppression of ethanolamine-containing glycerophospholipid synthesis in HL-60 cells during retinoic acid-induced differentiation.

Synthesis and degradation of glycerophospholipids in HL-60 cells and retinoic acid (RA)-treated HL-60 cells were examined. The synthesis of each subclass of ethanolamine-containing glycerophospholipids was extremely suppressed in RA-treated HL-60 cells, while that of other glycerophospholipids was not seriously affected. A pulse-chase experiment revealed that about 88% of 1,2-diacyl and 28% of 1-alkenyl-2-acyl glycerophosphoethanolamine were degraded during 4 days in RA-treated HL-60 cells. These characteristics of metabolism observed in RA-treated HL-60 cells might be responsible for the change of subclass composition of ethanolamine-containing glycerophospholipids in HL-60 cells during differentiation to granulocytes.

Cell Differentiation↗