scholarly journals Relationship between lipid saturation and lipid-protein interaction in liver mitochondria modified by catalytic hydrogenation with reference to cardiolipin molecular species

1990 ◽  
Vol 265 (1) ◽  
pp. 79-85 ◽  
Author(s):  
M Schlame ◽  
L Horvàth ◽  
L Vìgh
Keyword(s):  
Double Bond ◽  
Stearic Acid ◽  
Liver Mitochondria ◽  
Solvation Shell ◽  
Fatty Acid Analysis ◽  
Structural Requirement ◽  
Hydrophobic Moiety ◽  
Membrane Compartment ◽  
Lipid Protein Interaction ◽  
Tight Association

Lipid acyl double bonds in isolated mitochondrial membranes were gradually reduced by palladium-complex-catalysed hydrogenation, and the resulting saturation was monitored by fatty acid analysis of phosphatidylcholine, phosphatidylethanolamine and cardiolipin. The courses of hydrogenation of these phospholipids suggested that cardiolipin is in a membrane compartment which is less accessible to the applied catalyst. Native cardiolipin and its hydrogenation products were further characterized by analysis of their molecular diacylglycerol species. A decrease in the double bond content was accompanied by an increased amount of motionally restricted lipids at the hydrophobic interface of proteins as measured by two different spin-labelled lipids (C-14 positional isomers of spin-labelled stearic acid and phosphatidylcholine analogues). The protein-immobilized fraction of spin-labelled stearic acid increased in parallel with the hydrogenation of cardiolipin rather than of phosphatidylcholine or phosphatidylethanolamine. These data are interpreted in terms of a tight association of cardiolipin with membrane proteins, which becomes looser upon double bond reduction leading to the replacement of cardiolipin by spin-labelled stearic acid in the solvation shell. Thus the hydrophobic moiety of cardiolipin, characterized by double-unsaturated C18-C18 diacylglycerol species, seems to be an important structural requirement for the high protein affinity of this compound.

ChemInform Abstract: Highly Chemo-, Regio-, and Stereoselective Introduction of a cis-Double Bond into a Thia-Analogue of Stearic Acid.

ChemInform ◽  
1987 ◽  
Vol 18 (32) ◽  
Author(s):  
P. H. BUIST ◽  
H. G. DALLMANN ◽  
R. T. RYMERSON ◽  
P. M. SEIGEL
Keyword(s):  
Double Bond ◽  
Stearic Acid

FATTY ACID COMPOSITION OF PHOSPHATIDYL ETHANOL-AMINE AND PHOSPHATIDYL SERINE FROM DOG BILE

1964 ◽  
Vol 42 (3) ◽  
pp. 309-316 ◽  
Author(s):  
U. K. Misra ◽  
D. A. Turner
Keyword(s):  
Fatty Acids ◽  
Arachidonic Acid ◽  
Fatty Acid ◽  
Linoleic Acid ◽  
Stearic Acid ◽  
Palmitic Acid ◽  
Linolenic Acid ◽  
Phosphatidyl Ethanolamine ◽  
Phosphatidyl Serine ◽  
Fatty Acid Analysis

Phosphatidyl ethanolamine and phosphatidyl serine extracted from dog bile have been separated by means of ammonium silicate column chromatography. Concentration of phosphatidyl serine in dog bile is about seven times higher than phosphatidyl ethanolamine. Fatty acid analysis by gas chromatography showed that phosphatidyl ethanolamine contains about 26% palmitic acid, 18% stearic acid, 11% linoleic acid, 2% linolenic acid, 9% arachidonic acid, 3% C22:5 fatty acid, and 6% C22:6 fatty acid. The concentrations of these fatty acids observed in phosphatidyl serine are different; palmitic acid represents about 43%, stearic acid 9%, linoleic acid 24%, linolenic acid a trace amount, and arachidonic acid 5%; C22:5 and C22:6 fatty acids are absent.

scholarly journals Leaky β-Oxidation of atrans-Fatty Acid

2004 ◽  
Vol 279 (50) ◽  
pp. 52160-52167 ◽  
Author(s):  
Wenfeng Yu ◽  
Xiquan Liang ◽  
Regina E. Ensenauer ◽  
Jerry Vockley ◽  
Lawrence Sweetman ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fatty Acid ◽  
Double Bond ◽  
Octadecenoic Acid ◽  
Liver Mitochondria ◽  
Gas Chromatography Mass Spectrometry ◽  
Rat Liver Mitochondria ◽  
Mitochondrial Matrix ◽  
Chain Acyl ◽  
Long Chain

The degradation of elaidic acid (9-trans-octadecenoic acid), oleic acid, and stearic acid by rat mitochondria was studied to determine whether the presence of atransdouble bond in place of acisdouble bond or no double bond affects β-oxidation. Rat mitochondria from liver or heart effectively degraded the coenzyme A derivatives of all three fatty acids. However, with elaidoyl-CoA as a substrate, a major metabolite accumulated in the mitochondrial matrix. This metabolite was isolated and identified as 5-trans-tetradecenoyl-CoA. In contrast, little or none of the corresponding metabolites were detected with oleoyl-CoA or stearoyl-CoA as substrates. A kinetic study of long-chain acyl-CoA dehydrogenase (LCAD) and very long-chain acyl-CoA dehydrogenase revealed that 5-trans-tetradecenoyl-CoA is a poorer substrate of LCAD than is 5-cis-tetradecenoyl-CoA, while both unsaturated acyl-CoAs are poor substrates of very long-chain acyl-CoA dehydrogenase when compared with myristoyl-CoA. Tetradecenoic acid and tetradecenoylcarnitine were detected by gas chromatography/mass spectrometry and tandem mass spectrometry, respectively, when rat liver mitochondria were incubated with elaidoyl-CoA but not when oleoyl-CoA was the substrate. These observations support the conclusion that 5-trans-tetradecenoyl-CoA accumulates in the mitochondrial matrix, because it is less efficiently dehydrogenated by LCAD than is itscisisomer and that the accumulation of this β-oxidation intermediate facilitates its hydrolysis and conversion to 5-trans-tetradecenoylcarnitine thereby permitting a partially degraded fatty acid to escape from mitochondria. Analysis of this compromised but functional process provides insight into the operation of β-oxidation in intact mitochondria.

scholarly journals Metabolism of pent-4-enoate in rat heart. Reduction of the double bond

1981 ◽  
Vol 194 (2) ◽  
pp. 427-432 ◽  
Author(s):  
J K Hiltunen ◽  
E J Davis
Keyword(s):  
Double Bond ◽  
Rat Heart ◽  
No Reduction ◽  
Tricarboxylic Acid Cycle ◽  
Liver Mitochondria ◽  
Tricarboxylic Acid ◽  
Beta Oxidation ◽  
Initial Oxidation ◽  
Acid Cycle ◽  
Tricarboxylic Acid Cycle Intermediates

1. Soluble extracts from rat heart and liver mitochondria were used to evaluate the early steps in the conversion of pent-4-enoyl-CoA into tricarboxylic acid-cycle intermediates. Hitherto the unresolved problem was the reduction of the double bond of pent-4-enoate. 2. Soluble extracts from heart mitochondria reduced pent-4-enoyl-CoA and penta-2,4-dienoyl-CoA in the presence of NADPH at rates (nmol/min per mg of protein) of 0.9 +/- 0.1 and 132 +/- 8 and from the liver mitochondria at the rates of 1.9 +/- 0.2 and 52 +/- 6 respectively. No reduction of acryloyl-CoA was found. 3. We show that primarily the double bond in position 4, not in position 2, of penta-2,4-dienoyl-CoA is reduced. 4. It is concluded that the principal metabolic pathway of penta-4-enoate is reduction of the double bond in position 4 after an initial oxidation of penta-2,4-dienoyl-CoA. The pent-2-enoyl-CoA thus formed can be further metabolized by the usual enzymes of beta-oxidation, and by the further metabolism of propionyl-CoA to tricarboxylic acid-cycle intermediates.

Synthesis of biologically active spin-labelled radioactive cytidine diphosphodiglyceride, a novel probe for biological membranes

1976 ◽  
Vol 54 (6) ◽  
pp. 553-560 ◽  
Author(s):  
L. Stuhne-Sekalec ◽  
N. Z. Stanacev
Keyword(s):  
Stearic Acid ◽  
Biological Membranes ◽  
Chemical Conversion ◽  
Liver Mitochondria ◽  
Biologically Active ◽  
Rat Liver Mitochondria ◽  
Inner Mitochondrial Membrane ◽  
Isolation And Purification ◽  
Enzymatic Acylation ◽  
Mitochondrial Biosynthesis

A versatile synthesis of spin-labelled radioactive cytidine diphospho-sn-1,2-diacylglycerol (CDP-diglyceride) has been developed based on the combination of the enzymatic acylation of radioactive sn-glycero-3-phosphate with 12-doxyl stearic acid and the chemical conversion of the thus obtained spin-labelled radioactive phosphatidic acid with cytidine monophosphomorpholidate into spin-labelled radioactive CDP-diglyceride. The method for the isolation and purification of the latter compound was described. This obtained CDP-[2-3H]diglyceride contained 10% of fatty acids of paramagnetic nature, presumably present as a covalently bound 12-doxyl stearic acid esters. The biological activity was tested by using the synthesized compound as a substrate in the mitochondrial biosynthesis of phosphatidylglycerol. It was found that spin-labelled CDP-[2-3H]diglyceride prepared as described can be converted in the presence of sn-[2-14C]-glycero-3-phosphate into a spin-labelled [2-3H, 2′-14C]phosphatidylglycerol with isolated rat liver mitochondria, establishing therefore that the site of its utilization is identical with the site of phosphatidylglycerol synthesis in isolated mitochondria, i.e. inner mitochondrial membrane. Results described demonstrate that the synthesized spin-labelled CDP-diglyceride can be used as a specific probe for the spin- and radioactive covalent labelling of polyglycerophosphatides of mitochondrial membranes. Some implications and further possibilities in the study of biological membranes using the spin-labelled radioactive CDP-diglyceride are discussed.

Model Vulcanization of EPDM Compounds—Part I: Structure Determination of Vulcanization Products from Ethylidene Norbornane

1984 ◽  
Vol 57 (2) ◽  
pp. 265-274 ◽  
Author(s):  
J. H. M. van den Berg ◽  
J. W. Beulen ◽  
E. F. J. Duynstee ◽  
H. L. Nelissen
Keyword(s):  
Zinc Oxide ◽  
Double Bond ◽  
Stearic Acid ◽  
Structure Determination ◽  
Epdm Rubber

Abstract Vulcanization of ENBH (C9H14), a model for ENB containing EPDM rubber, with a system consisting of zinc oxide, stearic acid, sulfur, TMTD, and MBT at 140°C for 1 h yields slightly more than 30 different crosslinked products C9H13-Sn-C9H13 where n=2,3,4, and 5. In all of the products, the original ENBH structure is maintained (no shift of the double bond) and attachment of the sulfur bridge occurs only at the two allylic positions 3 and 9. Monosulfides (n=1) are probably also formed but no structures could be determined. Only small amounts of the MBT-Sn-C9H13 coupling products and noncrosslinked cyclic sulfides are formed.

Highly chemo-, regio-, and stereoselective introduction of a cis-double bond into a thia-analogue of stearic acid

1987 ◽  
Vol 28 (8) ◽  
pp. 857-860 ◽  
Author(s):  
Peter H. Buist ◽  
H.Garry Dallmann ◽  
Robert T. Rymerson ◽  
Peter M. Seigel
Keyword(s):  
Double Bond ◽  
Stearic Acid

scholarly journals The metabolism of tetradecylthiopropionic acid, a 4-thia stearic acid, in the rat. In vivo and in vitro studies

1992 ◽  
Vol 286 (3) ◽  
pp. 879-887 ◽  
Author(s):  
E Hvattum ◽  
S Skrede ◽  
J Bremer ◽  
M Solbakken
Keyword(s):  
Stearic Acid ◽  
Rat Hepatocytes ◽  
Liver Mitochondria ◽  
Oxidation Products ◽  
Rat Liver Mitochondria ◽  
Beta Oxidation ◽  
Isolated Rat Hepatocytes ◽  
Semialdehyde Dehydrogenase

The metabolism of [1-14C]tetradecylthiopropionic acid (TTP), a 4-thia stearic acid, and its sulphoxide, [1-14C]texadecylsulphoxypropionic acid (TTP-SO), has been studied in intact rats, in isolated rat hepatocytes, and in rat liver mitochondria. Two pathways of oxidation (beta-oxidation and omega-oxidation) have been demonstrated. TTP is incorporated, in vivo, into tissue triacylglycerol and phospholipids, it is oxidized to CO2, and it is excreted in urine, mainly as carboxypropylsulphoxypropionic acid and a little as carboxymethylsulphoxypropionic acid. TTP-SO is metabolized, in vivo, more rapidly to the same two omega-oxidation products. In hepatocytes TTP is incorporated into triacylglycerol and phospholipids even more rapidly than stearic acid. It is recovered mainly in the 1-position of phosphatidylcholine. Some is oxidized to CO2 and acid-soluble products. TTP-SO is mainly omega-oxidized to the same metabolites as are found in urine. A small fraction is incorporated into phospholipids or oxidized to CO2. In isolated mitochondria [1-14C]TTP is converted into 14CO2, radioactive malonic semialdehyde, and addition products of malonic semialdehyde. In the presence of phenylhydrazine, malonic semialdehyde phenylhydrazone is the dominating product. In soluble extracts of mitochondria [1-14C]malonic semialdehyde is oxidized directly to 14CO2 in the presence of CoA and NAD+, probably by the (methyl)malonic acid semialdehyde dehydrogenase (EC 1.2.1.27).

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