Triacsin C was originally isolated from a Streptomyces aureofaciens culture. The compound is an inhibitor of long fatty acid acyl-CoA synthetase (ACSL) in intact cells and the nonspecific ACSL in cell sonicates (IC50=3.6-8.7 μM). Triacsin C has been shown to inhibit de novo synthesis of triacylglycerol, diacylglycerol, cholesterol esters, and phospholipids. The inhibitory effect of Triacsin C prevents degranulation by human neutrophils through superoxide anion generation inhibition, thus inhibiting neutrophil activity. Triacsin C has been classified as a hypotensive vasodilator which may act by increasing methacholine-induced NO synthesis. The compound has also been reported to inhibit β-cells by abolishing L-type Ca2+ CP (L-type Ca2+) channel modulation.
