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PubMed1990

Sodium fluoride unmasks the accumulation of lysophosphatidylcholine in intact pancreatic islet cells.

When intact but dispersed neonatal islet cells, prelabelled with [14C-Me]choline, were stimulated with a calcium ionophore, ionomycin alone elicited only small rises in lysophosphatidylcholine; in contrast, pretreatment for 20 min with sodium fluoride (20mM) unmasked a consistent accumulation of lysophospholipid (to 155% of control at 1 min, 162% at 5 min and 212% at 10 min). Fluoride was shown to inhibit (by 40-50%) the reacylation of exogenous acyl- or alkyl-linked lysophosphatidylcholines by a delayed and indirect effect, whereas, in contrast, 12-O-tetradecanoylphorbol-13-acetate or dioctanoylglycerol actually augmented acylation. Thus, increased production of lysophosphatidylcholine in intact islets is obscured by rapid removal mechanisms, one of which might involve protein kinase C (or diglycerides directly). The use of sodium fluoride partially obviates this clearance, but this finding may necessitate a re-interpretation of claims that G protein agonists such as fluoride directly activate phospholipase A2 in some cells.

Acylation↗

PubMed1983

Bradykinin-stimulated differential incorporation of arachidonic acid into lipids of kidney cortex and medulla.

We investigated bradykinin-induced changes in the turnover of arachidonate in renal lipids of the perfused rabbit kidney. Upon hormone stimulation, this cellular system undergoes only transient dynamic changes in arachidonic acid metabolism; no loss of bradykinin effect on arachidonate release and prostaglandin generation is shown upon repeated hormone administrations during 8-9 hr of perfusion. Ureter-obstructed rabbit kidneys were perfused for 5-6 hr and then saline or bradykinin in saline was administered, followed after 10 sec by pulse labelling with [14C]arachidonate. The pattern of distribution of [14C]arachidonate in lipid fractions of the cortex showed that bradykinin caused a 2 to 2.5-fold increase in the relative incorporation of arachidonic acid into phosphatidylinositol (PI), phosphatidic acid (PA), diglyceride (DG) and triglyceride (TG) fractions and a concomitant decrease in its incorporation into phosphatidylcholine (PC) and phosphatidylethanolamine (PE). In contrast, in the medulla hormone administration caused a marked increase of arachidonate incorporation into PI and PC, and a decrease in incorporation into PE, PA, DG and TG. This differential arachidonate labelling of cortical vs medullary lipids following bradykinin stimulation suggests that the hormone activates different lipolytic processes in cortex and medulla, and promotes hydrolysis of arachidonic acid from different phospholipid pools.

Animals↗

PubMed1983

Phospholipase A2 inhibitors. Differential inhibition of fatty acid acylation into kidney lipids by mepacrine and p-bromophenacyl bromide.

Mepacrine and p-bromophenacyl bromide, in addition to their inhibitory effect on lipolysis, are also potent inhibitors of fatty acid acylation into renal medullary lipids. Significant qualitative and quantitative differences in the inhibition by the two drugs were seen. p-Bromophenacyl bromide exerted a non-selective effect inhibiting the incorporation of saturated and unsaturated fatty acids into all phospholipid classes and triacylglycerols. In contrast, mepacrine selectively inhibited the incorporation of both saturated and unsaturated acids into phosphatidylcholine, phosphatidylethanolamine and triglycerides, and concurrently markedly enhanced their incorporation into phosphatidylinositol. Quantitative analysis of these mepacrine effects, together with the known inhibitory effects of this compound on phospholipase A2 and phosphatidylinositol-specific phospholipase C, suggests that mepacrine also inhibits phosphatidic acid phosphatase, thereby shunting the flux of phosphatidic acid away from diglyceride formation and into synthesis of phosphatidylinositol.

Acetophenones↗

PubMed1993

Association between leukotriene B4-induced phospholipase D activation and degranulation of human neutrophils.

We have explored the role of phospholipase D (PLD) activation in leukotriene B4 (LTB4)-induced Ca2+ mobilization and degranulation of human neutrophils. Stimulation of [3H]alkyl-acyl-phosphatidylcholine-labeled neutrophils with LTB4 resulted in a rapid accumulation of [3H]alkyl-phosphatidic acid (PA) as well as a somewhat slower accumulation of [3H]alkyl-diglyceride (DG). In the presence of ethanol, PLD catalyzed a transphosphatidylation reaction in which LTB4 increased [3H]alkyl-phosphatidylethanol formation and simultaneously decreased LTB4-induced PA and DG accumulation. This pattern of lipid metabolism is consistent with the conclusion that LTB4 stimulates PLD activity in human neutrophils. Additional studies in which the extracellular and intracellular concentrations of Ca2+ were varied indicated that maximal LTB4-induced PLD activation was dependent upon Ca2+ and potentiated by inhibitors of protein kinase C. The time-course and concentration-response curves for LTB4-induced PLD activation were different from those for LTB4-induced Ca2+ mobilization, as measured by fura-2 fluorescence. On the other hand, the concentration-response curve for LTB4-induced PLD activation was similar to that for LTB4-induced degranulation. Preincubation of the cells with ethanol inhibited LTB4-induced PA and DG accumulation, as well as degranulation, suggesting that one or both of these metabolites were important for this response. In contrast, ethanol had no effect on LTB4-induced Ca2+ mobilization. Propranolol, an inhibitor of phosphatidate phosphohydrolase, abolished DG accumulation in response to LTB4 but had no effect on degranulation, suggesting that PA is more important than DG as a mediator of degranulation. Taken collectively, these data indicate that LTB4-induced activation of PLD in human neutrophils is mediated by a Ca(2+)-dependent mechanism, but not by protein kinase C. In addition, PLD activation in these cells may induce degranulation, but not Ca2+ mobilization.

Alkaloids↗

PubMed1988

Comparison of the effects of carbon tetrachloride and of 2,3,7,8-tetrachlorodibenzo-p-dioxin on the disposition of linoleic acid in rat liver in vitro.

Both 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) and carbon tetrachloride (CCl4) have conspicuous effects on lipid metabolism in rat liver. Although it is generally accepted that CCl4 administration leads to hepatic lipid peroxidation in vivo, conflicting reports from different laboratories make it unclear whether or not lipid peroxidation is involved in the mechanism of toxicity of TCDD. The present study involved pretreating F344 rats with CCl4 or TCDD, then at predetermined times thereafter, giving [U-14C]linoleic acid. A variety of compound classes were monitored in extracts of liver taken 30 min after the label was given. A previously unreported effect of CCl4 was a conspicuous increase in turnover of 1,2-diglycerides. That CCl4 did cause lipid peroxidation was evident from the presence of allylic hydroxyacids not seen in vehicle-treated controls, greatly increased radioactivity in protein-bound material, and decreased levels of arachidonate without decreased synthesis from linolate. Where effects of TCDD pretreatment could be seen, they were much less than the corresponding effects of CCl4. No allylic hydroxyacids were detected in livers of TCDD-treated rats. The concentration of arachidonate was not reduced, and elongation of linolate was not stimulated, indicating that TCDD did not cause extensive-but-repaired peroxidation. It is concluded that while TCDD may slightly increase hepatic lipid peroxidation in rats in vivo, the extent of such stimulation appears to be too slight to account for the toxicity of TCDD.

Aldehydes↗

PubMed1993

The relationship between the effect of biphenylcarboxylic acid analogs on glyceride synthesis and conformation.

The inhibition of biphenylcarboxylic acid analogs on glyceride synthesis was studied in association with conformation of the chemicals. Chemicals used were benzoic acid substituted with phenyl, benzoyl and phenoxy groups, phenylphenyloxyacetic acid and p-phenylacetic acid. Twist angles were calculated by a molecular orbital method. Following oral administration of p-phenylbenzoic acid to the rats for 7 days, the decrease of the triglyceride synthesized from [14C]oleic acid was observed in the adipose tissue. The in vitro inhibitions on the formation of fatty acyl-CoA thioester were examined from the influence on the hippuric acid formation from [14C]benzoic acid using the rat liver slices. In the homologous series, high inhibition was observed in para and meta substituents. None, or low inhibitions of ortho-substituted chemicals were related to the steric hindrance of the phenyl ring against carboxyl groups. This hinderance was associated with conformation and with the geometrical relationship between substituted phenyl rings and carbon atoms of carboxylic acid. In the in vitro inhibition on overall formation of diglyceride and triglyceride from [14C]glycerol, o-phenylbenzoic acid showing no inhibition on hippuric acid formation did not show inhibition. However, other ortho-substituted chemicals showed higher inhibition in comparison with the inhibition on hippuric acid formation. The inhibition of para- and meta-substituted chemicals were higher than the corresponding values of ortho substituted compounds.

Animals↗

PubMed1975

ORD and CD studies of saturated glycerides.

A convenient method for transforming 3-acyl-sn-glycerols into 1-acyl-2,3-diacyl'-sn-glycerols, antipodes of 1,2-diacyl'=3-acyl-sn-glycerols, of relatively high optical purity, via the 1,2-dimesyl-3-acyl-sn-glycerols has been worked out. ORD and CD curves of optically active triglycerides and also some mono- and diglycerides have been studied in detail. The curo 200 nm or below. A Cotton effect from the n yeilds ets* transtition of the ester chromophore was observed at 215-220 nm, which was negative for triglyceritical rotations could be observed in triglycerides with very small differences in chain length, such as 1,2-dilauroyl-3-myristoyl-sn-glycerol.

Circular Dichroism↗

PubMed1988

Isolation and structural characterization of a new non-phosphorylated lipoamino acid from Mycobacterium phlei.

A new non-phosphorylated lipoamino acid was extracted from Mycobacterium phlei, strain IST. It is particularly sensitive to alkaline hydrolysis, and contains a lysine residue joined to a 1,2-diglyceride via an ester linkage. The FAB-positive mass spectrum shows the presence of various molecular species of which the most abundant contains a palmitic and a tuberculostearic acid residue. An analogue of this lipid was synthesized, 1,2-dipalmitoyl 3-lysyl glycerol. Both its chromatographic behavior (TLC), and the decomposition pathways of the MH+ ions, studied by FAB MS and MIKE spectroscopy, were identical to the natural product.

Amino Acids↗

PubMed1991

Regio- and stereoselective enzymatic esterification of glycerol and its derivatives.

A methodology for regio- and stereoselective preparation of acyl glycerol derivatives is presented. It offers easy access to specific 1,2-, 1,3-diglycerides and triglycerides as well as alkyl glycerol esters, phospholipids and glycolipids. These compounds are prepared by esterification of the corresponding glycerol derivatives such as 2-monoglycerides, alkyl glycerols, glyceryl glycosides, glyceryl phosphate esters, or unsubstituted glycerol. The regio- and stereoselectivity in the esterification is achieved by using fatty acid anhydrides and an enzymatic catalyst, 1,3-specific lipase. NMR methods for determining the regio- and stereoselectivity of esterification are discussed.

Esterification↗

PubMed1994

Synthesis and antiviral activity of 3'-azido-3'-deoxythymidine triphosphate distearoylglycerol: a novel phospholipid conjugate of the anti-HIV agent AZT.

Phospholipid conjugates of 3'-azido-3'-deoxythymidine (AZT) show activity against the human immunodeficiency virus (HIV) in vitro. In a previous report (K.Y. Hostetler, L.M. Stuhmiller, B.H.M. Lenting, H. van den Bosch and D.D. Richman (1991), J. Biol. Chem. 265, 6112-6117) the syntheses and anti-HIV activities of AZT mono- and diphosphate diglyceride have been described. We now report on the synthesis, characterization and biological activity of 3'-azido-3'-deoxythymidine triphosphate distearoylglycerol (AZTTP-DSG). The compound was prepared by the condensation of AZT diphosphate with distearoylphosphatidic acid morpholidate in anhydrous pyridine at room temperature and purified by means of high-performance liquid chromatography using a silica column. Characterization was performed with 31P-NMR and IR analyses and determination of the fatty acid, phosphorus and nucleoside content of the product. AZTTP-DSG inhibited HIV-1 replication in both CEM and HT4-6C cells at a level intermediate in potency between its mono- and diphosphate analogs. The IC50 values of AZTTP-DSG were 0.33 and 0.79 microM in these two cell lines, respectively. In addition, AZTTP-DSG was less toxic to CEM cells in vitro than the other AZT liponucleotides and reduced viable cell numbers in this cell type by 50% at 1000 microM. Initial studies on the metabolism of AZTTP-DSG revealed that both AZT and AZT monophosphate were liberated from the lipid pro-drug by a rat liver mitochondrial enzyme preparation. These phospholipid derivatives of AZT nucleotides represent pro-drugs for the intracellular delivery of phosphorylated antiviral nucleoside analogs.

Antiviral Agents↗

PubMed1976

Stereospecific distribution of fatty acids in human plasma triglycerides.

Because of a biological difference between both primary hydroxylgroups of glycerol there are three distinct hydroxylgroups esterified with fatty acids in triglycerides. The distribution of fatty acids in the three distinct positions of triglycerides can be investigated by a combination of partial hydrolysis of triglycerides by pancreatic lipase, phosphorylation of the diglycerides formed and the stereospecific action of phospholipase A on phosphatides. Plasma triglycerides from normal and hyperlipemic humans are analysed. Human plasma triglycerides are highly asymmetric. The 1-position contains more than twice as much palmitic acid as the 3-position. Statistically significant differences are found between normal and hyperlipemic humans for palmitic and linoleic acid at the 2-position, and for oleic and linoleic acid at the 3-position.

Chromatography, Gas↗

PubMed1978

An enzymic determination for serum phospholipid.

A new colorimetric determination for serum phospholipid is described. Firstly, serum phospholipid is incubated with phospholipase C from Bacillus cereus, and then the released diglyceride and triglyceride are hydrolyzed completely to fatty acid and glycerol by lipoprotein lipase from Pseudomonas fluorescens. Secondly, the glycerol produced is enzymatically determined by glycerol dehydrogenase in the presence of NAD+, using phenazine methosulfate-nitro blue tetrazolium as color reagents. The absorbance at 570 nm is recorded. The amount of the glycerol from phospholipid is calculated by subtracting the amount of glycerol from triglyceride from the amount of total glycerol. The present method requires only 20 microliter of serum and a 40 min incubation and is highly reproducible. The results obtained show good correlation with those obtained by a chemical method (correlation coefficient, 0.925) or the phospholipase D-choline oxidase method (correlation coefficient, 0.936). These results strongly suggest that the proposed method can be utilized as a routine clinical test.

Glycerol↗

PubMed1980

Studies of selected enzymes of phospholipid metabolism in the dystrophic human muscle.

Proceeding from deviations of the phospholipid pattern in the muscle in progressive muscular dystrophy, the activities of a number of enzymes of phospholipid metabolism in the normal and dystrophic human muscle were measured. Twelve cases of the Duchenne type and four of the Becker-Kiener type were studied. The activities of CDP-choline:diglyceride-P-cholinetransferase, of CDP-choline:ceramide-P-cholinetransferase and of phosphatidylcholine degradation were determined in normal and dystrophic human muscle. A significant difference in enzyme activities between normal and dystrophic muscle could not be established. The activities of a phosphatidylethanolaminemethyltransferase and a transfer of P-choline directly from phosphatidylcholine to sphingomyelin could be excluded for normal human muscle. The significance of these results for the integration of phospholipid findings in ideas about pathogenesis of progressive muscular dystrophy is discussed.

Adolescent↗

PubMed1985

Phosphatidic acid phosphatase activity in subcellular fractions of normal and dystrophic human muscle.

Biopsy samples from normal and dystrophic human muscle (Duchenne type) were fractionated by differential centrifugation and microsomes, mitochondria and cytosol were assayed for phosphatidic acid phosphatase (EC 3.1.3.4) and marker enzymes of mitochondria and cytosol. The activity of phosphatidic acid phosphatase was significantly lower in microsomes and higher in cytosol and mitochondria of dystrophic muscle than in the corresponding subcellular fractions of normal muscle. The results support an explanation of earlier findings that there is reduced G3P incorporation into diglycerides and phosphatidylcholine and a qualitative and quantitative change in the amount of phosphatidylcholine in dystrophic microsomes. The possible reasons for the reduction in the activity of only microsomal PA-P-ase were discussed.

Animals↗

PubMed1987

Hydrolysis of phosphatidate by human placental alkaline phosphatase.

Highly purified alkaline phosphatase of human placenta catalyzed the hydrolysis of phosphatidate with quantitative formation of almost stoichiometric amounts of diglyceride and inorganic phosphate. In the presence of sodium deoxycholate, the activity was maximal at pH 8.8. The activity was strongly inhibited by L-phenylalanine but scarcely affected by NaF. These results show that alkaline phosphatase hydrolyzes phosphatidate under different conditions from those for activity of phosphatidate phosphohydrolase.

Alkaline Phosphatase↗

PubMed1988

Composition and surface properties of the bronchial lipids in adult patients with cystic fibrosis.

Bronchial secretions from seven patients with cystic fibrosis (CF) were aspirated by fibreoptic bronchoscopy and analysed for lipid composition. The total lipid fraction was also used to measure dynamic surface tension. Pooled samples from 'normal' patients, healthy volunteers, patients with chronic bronchitis, and individual samples from two patients with bronchiectasis were used as controls. Increased bronchial inflammation and infection correlated with a decrease of the phospholipid fraction, and an increase of the cholesterol, diglyceride and triglyceride fractions. When individual phospholipids were analysed, patients with clinically severe CF showed a markedly decreased phosphatidylcholine fraction, whereas the phosphatidylinositol fraction was significantly higher in CF patients than in controls (p less than 0.05). Minimum surface tension was higher in CF patients compared to patients with chronic bronchitis (p less than 0.05). This might be related to earlier reported specific changes in the pattern of fatty acids of the CF bronchial phospholipids.

Adult↗

PubMed1989

A G-protein mediates secretagogue-induced gap junctional channel closure in pancreatic acinar cells.

Using the double whole-cell patch-clamp technique, we determined that dialysis of cell pairs by GTP[S] potentiated electrical uncoupling induced by extracellular addition of carbamylcholine (CCh). An inhibitor of diglyceride lipase, RHC 80267, further potentiated CCh/GTP[S]-induced junctional channel closure, probably by accumulation of diacylglycerol. Moreover, the protein kinase C inhibitor polymyxin B completely blocked uncoupling elicited by CCh/GTP[S]. These results provide the first evidence suggesting that gap junction channel closure by cholinergic stimulation is mediated by a G-protein, which acts by increasing phosphatidylinositol biphosphate breakdown and protein kinase C activity.

Animals↗

PubMed1983

Determination of locust vitellogenin by radioimmunoassay with [3H]Propionyl-vitellogenin.

A simple procedure for radiolabeling of locust vitellogenin is described. This procedure involves coupling of [3H]propionyl succinimidate to purified vitellogenin with high yield and specific activity. Using this radiolabeled analog, a specific and sensitive radioimmunoassay was developed for determining locust vitellogenin content, with a lower detection limit of 1 ng. [3H]Propionyl-vitellogenin binds completely to rabbit anti-vitellogenin (locust) and can be completely competed out by locust vitellogenin. The structural similarity of locust vitellogenin with that of locust egg vitellin, male locust lipophorin (a diglyceride-carrying lipoprotein), Xenopus laevis vitellogenin, and chicken egg yolk lipovitellin was examined with this RIA procedure. Comparable binding competition was obtained with locust vitellin only. Male locust lipophorin, Xenopus vitellogenin, and chicken lipovitellin did not inhibit vitellogenin binding at concentrations 1000-fold greater than that of locust vitellogenin. The use of this RIA in determination of vitellogenin synthesis in vivo and in vitro, using isolated fat body preparations, is described.

Animals↗