Disease relevance of Arachidonyl-coa

• Synthesis of arachidonoyl CoA and docosahexaenoyl CoA in homogenates and microsomes from cerebrum, cerebellum, and brain stem and in synaptic plasma membranes from cerebrum of control rats and rats undergoing bicuculline-induced status epilepticus were studied [1].
• Of the acyl-CoA molecular species only the concentration of arachidonoyl-CoA was increased at 3 min and 15 min after decapitation, by 3-4 fold compared with microwaved brain [2].
• Triacsin C was found to inhibit the action of arachidonoyl-CoA synthetase and the nonspecific enzyme in sonicates of HSDM1C1 mouse fibrosarcoma cells [3].
• Hypoxia had no significant effect on the level of AA radioactivity in diacylglycerol (DAG) as compared to control but significantly enhanced the level of arachidonoyl-CoA (AA-CoA) radioactivity [4].
• The increase in arachidonoyl-CoA after decapitation indicates that reincorporation of arachidonic acid into membrane phospholipids is possible during ischemia, likely at the expense of docosahexaenoic acid [2].

Psychiatry related information on Arachidonyl-coa

• As chronic administration of valproic acid in bipolar disorder achieves whole-brain levels of 1.0 to 1.5 mM, inhibition of arachidonoyl-CoA formation can occur at brain concentrations that are therapeutically relevant to this disease [5].

High impact information on Arachidonyl-coa

• Herein, we demonstrate the highly selective iPLA2beta-catalyzed hydrolysis of saturated long-chain fatty acyl-CoAs (palmitoyl-CoA approximately myristoyl-CoA >> stearoyl-CoA >> oleoyl-CoA approximately = arachidonoyl-CoA) present either as monomers in solution or guests in host membrane bilayers [6].
• Homogenates also contained acyl-CoA:1-radyl-2-lyso-sn-glycero-3-phosphocholine acyltransferase activity, which transferred acyl chains from oleoyl-, linoleoyl-, or linolenoyl-CoA to both 1-alkyl and 1-acyl acceptors, but preferred the 1-acyl acceptor when arachidonoyl-CoA was used [7].
• Cholesterol arachidonate was formed upon incubation of phenylmethanesulfonyl fluoride-modified LCAT with arachidonyl-CoA [8].
• Arachidonoyl-CoA synthetase. Separation from nonspecific acyl-CoA synthetase and distribution in various cells and tissues [9].
• To further substantiate that the two acyl-CoA synthetases are distinct proteins, we solubilized enzyme from a mutant cell line lacking arachidonoyl-CoA synthetase and from the parent cell line from which it was derived [9].

Chemical compound and disease context of Arachidonyl-coa

• The relatively lower selectivity for arachidonoyl-CoA as compared with oleoyl-CoA of the 1-acyl-glycerophosphocholine acyltransferase system is consistent with the decrease in polyenoic fatty acid content at the 2-position of the hepatoma phospholipids [10].

Biological context of Arachidonyl-coa

• Thus, arachidonoyl-CoA synthetase is required for arachidonate homeostasis in HSDM1C1 cells [11].
• Despite its ability to block AA acylation almost completely, H2O2 did not directly inhibit arachidonoyl CoA synthetase or arachidonoyl CoA:lysophosphatide acyltransferase, which catalyze AA incorporation into phospholipids [12].
• We have examined the fatty acid substrate specificity of arachidonoyl-CoA synthetase from human platelet membranes [13].
• H2O2 inhibited the arachidonoyl-CoA synthetase with an IC50 of 3.3 mmol/l without affecting the lysophospholipid acyltransferase [14].
• These data indicate that the HETEs and other 20 carbon fatty acid substrates probably compete for activity of a specific arachidonyl-CoA synthetase, which is the first and rate-limiting step for esterification of arachidonic acid by many human cells [15].

Anatomical context of Arachidonyl-coa

• Platelet membranes catalyze formation of 2.9 nmol of arachidonoyl-CoA/min/10(9) platelets and 2.5 nmol of 8,11,14-eicosatrienoyl-CoA/min/10(9) platelets [16].
• Arachidonoyl-CoA synthetase is widely distributed and is present in significantly lower concentrations than nonspecific acyl-CoA synthetase only in adipose tissue and liver [9].
• The enzyme from pig heart microsomes displayed optimal activity at pH 6.0 and the preference for arachidonyl-CoA as the acyl donor [17].
• Synthesis of labeled arachidonoyl-CoA from [1-14C]arachidonate was decreased by about 50% by 25 microM hydroperoxy fatty acids both in synaptosomes and in the microsomal fraction [18].
• We have therefore investigated the effectiveness of THC and merthiolate in inhibiting the acylation of lysophosphatidylcholine, lysophosphatidylethanolamine, lysophosphatidylserine, lysophosphatidylinositol (LPI) and lysophosphatidic acid (LPA) in guinea pig liver microsomes using oleoyl-CoA and arachidonoyl-CoA as acyl donors [19].

Associations of Arachidonyl-coa with other chemical compounds

• These preparations were chromatographed on hydroxylapatite, and the mutant showed an absence of the peak identified as arachidonoyl-CoA synthetase in the parent while retaining the peak of nonspecific acyl-CoA synthetase activity [9].
• Examination of enzymes involved in CoA-dependent acylation revealed a low activity of both arachidonoyl-CoA synthetase and arachidonoyl-CoA: lyso-PAF arachidonoyltransferase [20].
• Acyltransferase displayed an approximately threefold preference for arachidonyl-CoA over palmitoyl-CoA, whereas the acylation rate of different lysophospholipids was in the order lysophosphatidylinositol > 1-palmitoyl lysophosphatidylcholine > 1-oleoyl lysophosphatidylcholine >> lysophosphatidylserine > lysophosphatidylethanolamine [21].
• Linoleoyl-CoA, linolenoyl-CoA and arachidonoyl-CoA were much less effective as acyl donors [22].
• Comparison between condensation and overall chain elongation of arachidoyl-CoA and arachidonoyl-CoA in swine cerebral microsomes [23].

Gene context of Arachidonyl-coa

• UDPGT activity was inhibited by arachidonoyl-CoA [24].
• Expressions of the brain-specific LACS family increased in the PC12 cells undergoing neurite outgrowth by nerve growth factor. mLACS preferentially catalyzed the formation of arachidonoyl-CoA more than palmitoyl-CoA or oleoyl-CoA in PC12 cells [25].
• Binding assays with arachidonyl-CoA revealed that replacement of a conserved R residue (R150A in ACBP1 and R284A in ACBP3), disrupted binding [26].
• This immunochemical study demonstrates that palmitoyl-CoA ligase does not share immunological determinants with acyl-CoA ligases in peaks B or C, thus demonstrating that palmitoyl-CoA ligase (peak A) is different from the arachidonoyl-CoA and lignoceroyl-CoA ligase activities in peaks B or C [27].
• Importantly, however, the triacsin concentration and length of pre-incubation with the enzymes could be adjusted to almost completely inhibit (greater than 80%) the nonspecific long chain acyl CoA-synthetase, with less than 20% inhibition of arachidonoyl-CoA synthetase [3].

References