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Article
Inhibition of Long Chain Fatty Ccyl-CoA Synthetase (ACSL) and Ischemia Reperfusion Injury
Bioorganic & Medicinal Chemistry Letters
  • Allan M. Prior
  • Man Zhang
  • Nina Blakeman
  • Palika Datta
  • Hung Pham, Philadelphia College of Osteopathic Medicine
  • Qian Chen, Philadelphia College of Osteopathic Medicine
  • Lindon H. Young, Philadelphia College of Osteopathic Medicine
  • Margaret T. Weis
  • Duy H. Hua
Document Type
Article
Publication Date
2-15-2014
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.
PubMed ID
24480468
Comments

This article was published in Bioorganic & Medicinal Chemistry Letters, Volume 24, Issue 4, February 15, 2014, Pages 1057-1061.

The published version is available at http://dx.doi.org/10.1016/j.bmcl.2014.01.016

Copyright © 2014 Elsevier B.V.

Citation Information
Allan M. Prior, Man Zhang, Nina Blakeman, Palika Datta, et al.. "Inhibition of Long Chain Fatty Ccyl-CoA Synthetase (ACSL) and Ischemia Reperfusion Injury" Bioorganic & Medicinal Chemistry Letters Vol. 24 Iss. 4 (2014) p. 1057 - 1061
Available at: http://works.bepress.com/qian_chen/21/