Synthesis and Characterization of 1- And 2-Monoglyceryl Ethers of Anteiso Fatty Alcohols, and Reinvestigation of Benzylidene Glycerol Synthesis

Serdarevich, B.; Carroll, K. K.

doi:10.1139/o66-092

Cited by 15 publications

(12 citation statements)

References 10 publications

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“…The precipitate was collected by filtration and washed successively with 50% ice-cold aqueous methanol, absolute ethanol 3 times, ethyl acetate 2 times, and diethyl ether 3 times. Yield was 3.86 g (95% To prepare 2-hexadecylglycerol-1,3-bisphosphate, 2-hexadecylglycerol was first prepared from 1-bromohexadecane and 1,3-benzylidene glycerol according to the procedure of Serdarevich and Carroll (50) except that the alkylation reaction was carried out in NaH/dimethylformamide as described above. The product migrated as a single spot on TLC (R F 0.14, benzene/diethyl ether/acetic acid, 25 Hexadecyl phosphate was prepared by phosphorylation of hexadecyl alcohol with excess phosphoryltriimidazole as described previously (51) and crystallized as the monosodium salt from ethanol/water.…”

Section: Methodsmentioning

confidence: 99%

Arachidonoyl-diacylglycerol Kinase SPECIFIC IN VITRO INHIBITION BY POLYPHOSPHOINOSITIDES SUGGESTS A MECHANISM FOR REGULATION OF PHOSPHATIDYLINOSITOL BIOSYNTHESIS

Walsh

Suen

Glomset

1995

Journal of Biological Chemistry

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We previously described the purification of a membrane-bound diacylglycerol kinase highly selective for sn-1-acyl-2-arachidonoyl diacylglycerols (Walsh, J. P., Suen, R., Lemaitre, R. N., and Glomset, J. A. (1994) J. Biol. Chem. 269, 21155-21164). This enzyme appears to be responsible for the rapid clearance of the arachidonaterich pool of diacylglycerols generated during stimulusinduced phosphoinositide turnover. We have now shown phosphatidylinositol 4,5-bisphosphate to be a potent and specific inhibitor of arachidonoyl-diacylglycerol kinase. Kinetic analyses indicated a K i for phosphatidylinositol 4,5-bisphosphate of 0.04 mol %. Phosphatidic acid also was an inhibitor with a K i of 0.7 mol %. Other phospholipids had only small effects at these concentrations. A series of multiply phosphorylated lipid analogs also inhibited the enzyme, indicating that the head group phosphomonoesters are the primary determinants of the polyphosphoinositide effect. However, these compounds were not as potent as phosphatidylinositol 4,5-bisphosphate, indicating some specificity for the polyphosphoinositide additional to its total charge. Five other diacylglycerol kinases were activated to varying degrees by phosphatidylinositol 4,5-bisphosphate and phosphatidic acid, suggesting that inhibition by acidic lipids may be specific for the arachidonoyl-DAG kinase isoform. Given the presumed role of arachidonoyl-diacylglycerol kinase in the phosphoinositide cycle, this inhibition may represent a mechanism for polyphosphoinositides to regulate their own synthesis.Diacylglycerol kinases catalyze the ATP-dependent phosphorylation of sn-1,2-diacylglycerol (DAG) 1 to phosphatidic acid (PA) (1-3). As such, they are widely regarded as attenuators of the DAG signaling and protein kinase C activation that occur during stimulus-induced PI turnover (4). The recent identification of a specific DAG kinase essential for PI-mediated invertebrate visual transduction is a striking confirmation of the involvement of DAG kinases in the PI cycle (5). It has recently become evident that DAG kinases are a diverse family of isoenzymes (2). The first of these to be purified and cloned was an 82.6-kDa isoform expressed predominantly in brain and thymus (6, 7). Several homologs of this enzyme also have been cloned, each of which has its own highly specific pattern of expression in cells and tissues (8 -12). Additional DAG kinases, which appear distinct from the cloned isoforms described above, also have been reported (13-21). However, detailed enzymologic data on these are not available at this time. Our laboratory has described and purified a membranebound DAG kinase highly selective for DAG molecular species containing arachidonate as the sn-2 fatty acyl moiety (21-24). This activity can be distinguished from other DAG kinases by a variety of enzymologic properties in addition to its substrate specificity (21-24). Arachidonoyl-DAG kinase activity varies widely between different tissues, but it is detectable in all cells and tissues we have examined (21-24). G...

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Section: Methodsmentioning

confidence: 99%

Arachidonoyl-diacylglycerol Kinase SPECIFIC IN VITRO INHIBITION BY POLYPHOSPHOINOSITIDES SUGGESTS A MECHANISM FOR REGULATION OF PHOSPHATIDYLINOSITOL BIOSYNTHESIS

Walsh

Suen

Glomset

1995

Journal of Biological Chemistry

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“…143,185 The spectra at higher fields (Ͼ350 MHz), on the other hand, were much more informative and in CDCl 3 displayed all the protons in the glycerol moiety as well as those on the ␣-carbon atom of the fatty chain. 31,138 The spectra showed that in dilute CDCl 3 solution(ca.…”

Section: Propertiesmentioning

confidence: 99%

“…[141][142][143] This procedure was useful for preparing dialkenyl and mixed alkyl-alkenyl glycerol ethers and was satisfactory in some instances for racemic ethers, but we have found it unsatisfactory for preparing monoalkyl glyceryl ethers directly without avoiding racemization. ␣-Alkyl thioglyceryl ethers, on the other hand, were obtained in very high yields by boiling unprotected thioglycerol with alkyl bromides or iodides in the presence of potassium hydroxide in 95% ethanol (or methanol with a crystal of iodine), 138 or with the alkyl tosylate in the presence of triethylamine in ethanol.…”

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confidence: 96%

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Glyceryl-ether monooxygenase [EC 1.14.16.5]. A microsomal enzyme of ether lipid metabolism

Taguchi¹,

Armarego²

1998

Med. Res. Rev.

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“…The free hydroxyl group in position 1 of glycerol is reacted with a fatty acid or fatty alcohol derivative, and subsequent removal of the blocking group by boric acid or hydrochloric acid leaves 1-monoglyeeride or 1-monoglyceryl ether (3,4). The free hydroxyl group in position 1 of glycerol is reacted with a fatty acid or fatty alcohol derivative, and subsequent removal of the blocking group by boric acid or hydrochloric acid leaves 1-monoglyeeride or 1-monoglyceryl ether (3,4).…”

Section: Isopropylidcne Glycerolmentioning

confidence: 99%

Glyceride isomerizations in lipid chemistry

Serdarevich

1967

J Americ Oil Chem Soc

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144

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Isomerization of isopropy]idene glycerol ketals and benzylidene glycerol acetals was studied, and isomerization equilibria were established. Reaction of benzaldehyde with glycerol gave four benzylidene glycerol isomers, which were separated by column chromatography and characterized by NMR spectroscopy and other methods.Isomerization of 1-and 2-monoglycerides and of 1,2-and 1,3-diglyeerides, and their separation by column chromatography, are described. Mechanisms of isomerization in mono-and diglycerides and factors which affect them are discussed.Isomerization of 1-and 2-glycerophosphates and of cyclic glycerophosphates by acid and base was also studied. Hydrolysis products of L-3glyeerylphosphorylcholine and 2-glycerylphosphorylcholine were separated by column chromatography and characterized by periodic acid oxidation, optical rotation, and NMR spectroscopy. No isomerization of unhydrolyzed L-3glycerylphosphoryleholine and 2-glyccrylphosphorylcholine was observed. Evidence indicated that acid-catalyzed hydrolyses of phosphoglyeerides are under thermodynamic control whereas most base-catalyzed hydrolyses are under kinetic control.

show abstract

Synthesis and Characterization of 1- And 2-Monoglyceryl Ethers of Anteiso Fatty Alcohols, and Reinvestigation of Benzylidene Glycerol Synthesis

Cited by 15 publications

References 10 publications

Arachidonoyl-diacylglycerol Kinase SPECIFIC IN VITRO INHIBITION BY POLYPHOSPHOINOSITIDES SUGGESTS A MECHANISM FOR REGULATION OF PHOSPHATIDYLINOSITOL BIOSYNTHESIS

Arachidonoyl-diacylglycerol Kinase SPECIFIC IN VITRO INHIBITION BY POLYPHOSPHOINOSITIDES SUGGESTS A MECHANISM FOR REGULATION OF PHOSPHATIDYLINOSITOL BIOSYNTHESIS

Glyceryl-ether monooxygenase [EC 1.14.16.5]. A microsomal enzyme of ether lipid metabolism

Glyceride isomerizations in lipid chemistry

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