scispace - formally typeset
Search or ask a question
Topic

Acyl-CoA

About: Acyl-CoA is a research topic. Over the lifetime, 527 publications have been published within this topic receiving 25134 citations. The topic is also known as: Acyl Coenzyme A.


Papers
More filters
Journal ArticleDOI
TL;DR: It is highlighted that altering fatty acid and TG metabolism within enterocytes has the capacity to alter systemic delivery of dietary fat and may serve as an effective target for preventing and treating metabolic diseases such as hepatic steatosis.

19 citations

Journal ArticleDOI
01 Aug 2000-Lipids
TL;DR: Dietary ethyl linoleate and ethyl 19,19,20,20-d4-1,2-13C-11,14-eicosadienoate were about equally effective as precursors of esterified arachidonate, suggesting that a small amount of the substrate may have been metabolized by the sequential use of δ8 and δ5 desaturases.
Abstract: Several experimental approaches were used to determine whether rat liver and testes express an acyl-CoA-dependent δ8 desaturase. When [1-14C]5, 11, 14-eicosatrienoic acid was injected via the tail vein, or directly into testes, it was incorporated into liver and testes phospholipids, but it was not metabolized to other labeled fatty acids. When [1-14C]11, 14-eicosadienoic acid was injected, via the tail vein or directly into testes, or incubated with microsomes from both tissues, it was only metabolized to 5,11, 14-eicosatrienoic acid. When ethyl 5,5,11,11,14,14-d6-5,11,14-eicosatrienoate was fed to rats maintained on a diet devoid of fat, it primarily replaced esteri-fied 5,8,11-eicosatrienoic acid, but not arachidonic acid. No labeled linoleate or arachidonate were detected. Dietary ethyl linoleate and ethyl 19,19,20,20-d4-1,2-13C-11,14-eicosadienoate were about equally effective as precursors of esterified arachidonate. The doubly labeled 11,14-eicosadienoate was metabolized primarily by conversion to 17,17,18,18-d4-9,12-ocatdeca-dienoic acid, followed by its conversion to yield esterified arachidonate, with a mass four units greater than endogenous arachidonate. In addition, the doubly labeled substrate gave rise to a small amount of arachidonate, six mass units greater than endogenous arachidonate. No evidence was obtained, with the radiolabeled substrates, for the presence of a δ8 desaturase. However, the presence of an ion, six mass units greater than endogenous arachidonate when doubly labeled 11, 14-eicosa-dienoate was fed, suggests that a small amount of the substrate may have been metabolized by the sequential use of δ8 and δ5 desaturases.

19 citations

Journal ArticleDOI
TL;DR: Results from these in vitro studies strongly suggest that acyl-CoA thioester derivatives are chemically reactive and are able to bind covalently to tissue proteins in vitro, and, therefore, may contribute significantly to covalent adduct formation of profen drugs in vivo.
Abstract: In this study, we investigated the possible involvement of acyl-CoA, reactive intermediary metabolites of 2-arylpropionic acids (profens), in protein adduct formation in rat liver homogenate and in human serum albumin (HSA) in buffer. (RS)-[1-14C]-2-Phenylpropionic acid (14C-2-PPA, 1 mM) was incubated with rat liver homogenate (1.5 mg/ml) in the presence of cofactors of acyl-CoA formation (Mg2+, ATP, and CoA). Aliquots of the incubation mixture were analyzed for covalent binding and acyl-CoA formation over a 3-h period. High-performance liquid chromatographic analysis of the products from such incubations showed the presence of 2-phenylpropionyl-S-acyl-CoA (2-PPA-CoA), which was confirmed by coelution with authentic 2-PPA-CoA, as well as by mass spectrometry. In the same incubations, 2-PPA was shown to bind covalently to hepatic proteins in a time- and ATP-dependent fashion. Inhibition of 2-PPA-CoA formation by acyl-CoA synthetase inhibitors, such as palmitic acid, lauric acid, octanoic acid, and ibuprofen, markedly decreased the extent of covalent binding of 2-PPA to hepatic proteins. Results from these in vitro studies strongly suggest that acyl-CoA thioester derivatives are chemically reactive and are able to bind covalently to tissue proteins in vitro, and, therefore, may contribute significantly to covalent adduct formation of profen drugs in vivo.

19 citations

Journal ArticleDOI
TL;DR: The synthesis of lipids from radioactive fatty acids in developing sunflower seeds has been examined in this article, where Lauric, palmitic, stearic and oleic acids were used.

19 citations

Journal ArticleDOI
TL;DR: ACSL1-mediated metabolic trapping of exogenous LCFA accelerates LCFA uptake rates, albeit to a lesser extent in females, which distinctly affects LCFA trafficking to acyl intermediates but not triglyceride storage or mitochondrial oxidation and is affected by female sex hormones.

19 citations


Network Information
Related Topics (5)
Protein subunit
33.2K papers, 1.7M citations
83% related
Amino acid
124.9K papers, 4M citations
82% related
Binding site
48.1K papers, 2.5M citations
82% related
Cholesterol
44.6K papers, 1.9M citations
81% related
Protein kinase A
68.4K papers, 3.9M citations
81% related
Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20232
202212
20218
20205
20193
20185