Unknown

Dataset Information

0

Inhibition of long chain fatty acyl-CoA synthetase (ACSL) and ischemia reperfusion injury.

ABSTRACT: Various triacsin C analogs, containing different alkenyl chains and carboxylic acid bioisoteres including 4-aminobenzoic acid, isothiazolidine dioxide, hydroxylamine, hydroxytriazene, and oxadiazolidine dione, were synthesized and their inhibitions of long chain fatty acyl-CoA synthetase (ACSL) were examined. Two methods, a cell-based assay of ACSL activity and an in situ [(14)C]-palmitate incorporation into extractable lipids were used to study the inhibition. Using an in vivo leukocyte recruitment inhibition protocol, the translocation of one or more cell adhesion molecules from the cytoplasm to the plasma membrane on either the endothelium or leukocyte or both was inhibited by inhibitors 1, 9, and triacsin C. The results suggest that inhibition of ACSL may attenuate the vascular inflammatory component associated with ischemia reperfusion injury and lead to a decrease of infarct expansion.

SUBMITTER: Prior AM 

PROVIDER: S-EPMC3963287 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Inhibition of long chain fatty acyl-CoA synthetase (ACSL) and ischemia reperfusion injury.

Prior Allan M AM   Zhang Man M   Blakeman Nina N   Datta Palika P   Pham Hung H   Chen Qian Q   Young Lindon H LH   Weis Margaret T MT   Hua Duy H DH  

Bioorganic & medicinal chemistry letters 20140113 4

Various triacsin C analogs, containing different alkenyl chains and carboxylic acid bioisoteres including 4-aminobenzoic acid, isothiazolidine dioxide, hydroxylamine, hydroxytriazene, and oxadiazolidine dione, were synthesized and their inhibitions of long chain fatty acyl-CoA synthetase (ACSL) were examined. Two methods, a cell-based assay of ACSL activity and an in situ [(14)C]-palmitate incorporation into extractable lipids were used to study the inhibition. Using an in vivo leukocyte recruit  ...[more]

Similar Datasets

Unknown Diversity and history of the long-chain acyl-CoA synthetase (Acsl) gene family in vertebrates.
| S-EPMC3890633 | biostudies-literature
Unknown Ontogeny of mRNA expression and activity of long-chain acyl-CoA synthetase (ACSL) isoforms in Mus musculus heart.
| S-EPMC1797059 | biostudies-literature
Unknown Enhancement of E. coli acyl-CoA synthetase FadD activity on medium chain fatty acids.
| S-EPMC4493641 | biostudies-literature
Unknown Long-chain acyl-CoA synthetase isoforms differ in preferences for eicosanoid species and long-chain fatty acids.
| S-EPMC5408607 | biostudies-literature
Unknown FATP2 is a hepatic fatty acid transporter and peroxisomal very long-chain acyl-CoA synthetase.
| S-EPMC2944282 | biostudies-literature
Unknown Hepatic long-chain acyl-CoA synthetase 5 mediates fatty acid channeling between anabolic and catabolic pathways.
| S-EPMC2952567 | biostudies-literature
Unknown Long-Chain Acyl-CoA Synthetase 4-Mediated Fatty Acid Metabolism Sustains Androgen Receptor Pathway-Independent Prostate Cancer.
| S-EPMC7785683 | biostudies-literature
Unknown Long-chain fatty acyl-CoA synthetase 1 promotes prostate cancer progression by elevation of lipogenesis and fatty acid beta-oxidation.
| S-EPMC8842993 | biostudies-literature
Unknown Long-chain acyl-CoA synthetases and fatty acid channeling.
| S-EPMC2846691 | biostudies-literature
Unknown Inhibition of Acyl-CoA Synthetase Long Chain Isozymes Decreases Multiple Myeloma Cell Proliferation and Causes Mitochondrial Dysfunction.
| S-EPMC10979990 | biostudies-literature