Glyceride isomerizations in lipid chemistry

Serdarevich, B.

doi:10.1007/bf02666775

Cited by 144 publications

(65 citation statements)

References 78 publications

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“…Preparations of 1,3-diC8 of greater than 99% purity showed considerably more activity (up to 70% of that seen with diC8) unless they were subjected to HPLC purification immediately prior to use. Facile acyl group migration between the 2 and 3 positions (27) makes it likely that the activity of nonpurified preparations resulted from acyl group migration and formation of a small amount of 1,2-diC8. The structures of acyl2Gro analogues synthesized to test the importance of the oxygen ester carbonyls are shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols.

Ganong¹,

Loomis²,

Hannun³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

234

102

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The specificity of protein kinase C activation by sn-1,2-diacylglycerols and analogues was investigated by using a Triton X-100 mixed micellar assay [Hannun, Y. A., Loomis, C. R. & Bell, R. M. (1985) J. Biol. Chem. 260, 10039-10043]. Analogues containing acyl or alkyl chains eight carbons in length were synthesized because sn-1,2-dioctanoylglycerol is an effective cell-permeant activator of protein kinase C. These analogues were tested as activators and antagonists of rat brain protein kinase C to determine the exact structural features important for activity. The analogues established that activation of protein kinase C by diacylglycerols is highly specific. Several analogues established that both carbonyl moieties of the oxygen esters are required for maximal activity and that the 3-hydroxyl moiety is also required. None of the analogues were antagonists. These data, combined with previous investigations, permitted formulation of a model of protein kinase C activation. A three-point attachment of sn-1,2-diacylglycerol to the surface-bound protein kinase C-phosphatidylserine-Ca21 complex is envisioned to cause activation. Direct ligation of diacylglycerol to Ca2+ is proposed to be an essential step in the mechanism of activation of protein kinase C.

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Section: Resultsmentioning

confidence: 99%

Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols.

Ganong¹,

Loomis²,

Hannun³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

234

102

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“…1). These isomers will undergo acyl migration to form equilibrium at a ratio of 3-4:7-6 between 1,2-and 1,3-DAG (Takano and Itabashi 2002) often in the presence of an acid, alkali, or heat (Sedarevich 1967). 1,3-DAG is more thermodynamically stable because of the steric effect of the molecule.…”

Section: Physicochemical Propertiesmentioning

confidence: 99%

Diacylglycerol Oil—Properties, Processes and Products: A Review

Tan

Long

et al. 2008

Food Bioprocess Technol

158

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Diacylglycerol (DAG) oil has beneficial effects on obesity and weight-related disorders. A survey of literature has shown the effects of DAG on the reduction in the accumulation of body fat in both animals and humans. The physiological effect of DAG is believed to be attributed to its metabolic pathway, which is different from triacylglycerol (TAG) metabolism. Physicochemical properties, such as melting and smoke points and polymorphic forms, of DAG are also distinct from TAG. Various patented processes for DAG oil production from several reaction routes are discussed. A review of patent literature of commercial products based on DAG oils and fats is also provided.

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“…( )compound that originates from the non-enzymatic isomer-Ž ization of 2-arachidonylglycerol Serdarevich, 1967;Mechoulam et al, 1995;Bisogno et al, 1997;Stella et al, . Ž .…”

Section: Production Of Other Fatty Acid Ethanolamidesmentioning

confidence: 99%

Receptor-dependent formation of endogenous cannabinoids in cortical neurons

Stella

Piomelli

2001

European Journal of Pharmacology

224

167

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Ž. We investigated the transduction mechanisms mediating formation of the endogenous cannabinoid endocannabinoid lipids, Ž . anandamide arachidonylethanolamide and 2-arachidonylglycerol, in primary cultures of rat cortical neurons. Unstimulated neurons contained 0.3 " 0.1 pmol of anandamide and 16.5 " 3.3 pmol of 2-arachidonylglycerol per mg of protein, as determined by gas 2q Ž . chromatographyrmass spectrometry. Ca entry into the neurons via activated glutamate N-methyl-D-aspartate NMDA receptors increased 2-arachidonylglycerol levels approximately three times, but had no effect on anandamide levels. By contrast, anandamide formation was stimulated five times by simultaneous activation of NMDA and acetylcholine receptors. Alone, acetylcholine receptor activation had no effect on anandamide or 2-arachidonylglycerol levels. The formation of fatty acid ethanolamides that do not activate cannabinoid receptors, including palmitylethanolamide and oleylethanolamide, was stimulated by coactivation of NMDA and acetylcholine receptors. Pharmacological experiments suggest that the cholinergic contribution to anandamide formation was mediated Ž . by a7 nicotinic receptors antagonized by methyllycaconitine , whereas the contribution to palmitylethanolamide and oleylethanolamide Ž . formation was mediated by muscarinic receptors antagonized by atropine . These findings indicate that cortical neurons produce anandamide and 2-arachidonylglycerol in a receptor-dependent manner, and that brain neurons may generate different endocannabinoid lipids depending on their complement of neurotransmitter receptors. q

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Glyceride isomerizations in lipid chemistry

Cited by 144 publications

References 78 publications

Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols.

Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols.

Diacylglycerol Oil—Properties, Processes and Products: A Review

Receptor-dependent formation of endogenous cannabinoids in cortical neurons

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