1-Oleoyl-2-acetyl-sn-glycerol

1-Oleoyl-2-acetyl-sn-glycerol is a synthetic activator of protein kinase C (PKC) [1].

PKC is a member of protein kinase enzymes which are involved in regulating the functions of other proteins via the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins. PKC plays a key role in intracellular signal transduction of Ca²⁺-dependent effects [2].

In the clonal GH₃ line of anterior pituitary cells, 1-oleoyl-2-acetyl-sn-glycerol at 4 ~ 60 μM reversibly reduced Ca²⁺ currents produced by test potentials to 10 mV, with IC50 value ~ 25 μM. 1-Oleoyl-2-acetyl-sn-glycerol at above concentrations also inhibited Ca²⁺ currents in chick embryo dorsal root ganglion cells and clonal AtT-20 pituitary cells [1]. In isolated rat parietal cells, 10^-7 ~ 10^-5 mol/l 1-oleoyl-2-acetyl-sn-glycerol reduced the submaximal and maximal H⁺ production response to 10^-5 or 10^-4 mol/l carbachol [2]. In human podocytes expressing transient receptor potential canonical-6 (TRPC6) channels, 100 μM 1-oleoyl-2-acetyl-sn-glycerol markedly increased intracellular Ca²⁺ levels of the cells via TRPC6 channels [3].

References:

[1]. Marchetti C, Brown AM. Protein kinase activator 1-oleoyl-2-acetyl-sn-glycerol inhibits two types of calcium currents in GH3 cells. American Journal of Physiology, 1988, 254(1 Pt 1): C206-C210.

[2]. Schepp W, Brosch E, Tatge C, et al. Cholinergic stimulation of isolated rat parietal cells: role of calcium, calmodulin and protein kinase C. Clinical Physiology and Biochemistry, 1989, 7(3-4): 137-148.

[3]. Ambrus L, Oláh A, Oláh T, et al. Inhibition of TRPC6 by protein kinase C isoforms in cultured human podocytes. Journal of Cellular and Molecular Medicine, 2015, 19(12): 2771-2779.