76343-93-6

Actin disruption is used to study cell functions in vitro (e.g., migration, endocytosis) and in vivo (e.g., tumor cell invasion). Latrunculin A is a bioactive 2-thiazolidinone macrolide derived from sponges that sequesters G-actin and prevents F-actin assembly. It binds monomeric actin with 1:1 stoichiometry and can be used to block actin polymerization both in vitro (K_d = 0.2 μM) and in cells (0.5 μM, 30 min).{ Latrunculin A (1-10 μM) causes depolymerization of tumor cell cytoskeleton within ten minutes. Overnight treatment of cells with latrunculin A (10 μM) strongly suppresses actin synthesis. Prolonged cell treatment blocks dexamethasone-induced changes in actin cytoskeleton with no effect on cell viability.

Latrunculin A has been used as medium supplementation for A549 cells to determine the internalization mechanism of CAV9 in A549 human lung carcinoma cells.

Latrunculin A, Latrunculia magnifica is a stabilizer of monomeric G-actin and polymerization inhibitor.

ChEBI: A bicyclic macrolide natural product consisting of a 16-membered bicyclic lactone attached to the rare 2-thiazolidinone moiety. It is obtained from the Red Sea sponge Latrunculia magnifica and from the Fiji Islands sponge Cacospongia myc fijiensis. Latrunculin A inhibits actin polymerisation, microfilament organsation and microfilament-mediated processes.

Latrunculin A, a toxin extracted from the red sea sponge Latrunculia magnifica. It participates in vitro in the morphological alteration of the polymerization of pure actin. It forms a complex by binding with the nucleotide cleft of actin for actin filaments elongation.

Latrunculin A inhibits actin polymerization by a different mechanism than cytochalasins. Latrunculin A disrupts microfilament-mediated processes.

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1) Coue et al. (1987), Inhibition of actin polymerization by latrunculin; FEBS Lett., 213 316 2) Spector et al. (1989), Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth; Cell Motil. Cytoskeleton, 13 127 3) Wang et al. (2005), Differential effects of latrunculin-A on myofibrils in cultures of skeletal muscle cells: Insights into mechanisms of myofibrillogenesis; Cell Motil. Cytoskeleton, 62 35 4) Reggiori et al. (2005), The actin cytoskeleton is required for selective types of autophagy, but not for non-specific autophagy, in the yeast Saccharomyces cerevisiae; Mol. Biol. Cell, 16 5843 5) Asadi et al. (2016) A Genetic Screen for Fission Yeast Gene Deletion Mutants Exhibiting Hypersensitivity to Latrunculin A; G3 Genes Genomes Genetics, 6 3399 [Focus Citation]