FEBS Letters · 1986 · 107 citations · 12 references
Life SciencesBiochemistryCell BiologyCell SignalingMolecular PharmacologySignal TransductionBiological MembranesCell Signaling NetworksDrug-receptor InteractionsLipid SignalingAnion BalanceCalcium Release From Intracellular StoresDrug - Membrane InteractionsInositol Lipid SignalingInositol Phosphate SignalingInositol Triphosphate SignalingInositol Trisphosphate SignalingPhospholipid Signaling
Neomycin, an antibiotic previously thought to interact specifically with inositol-containing phospholipids, was found to inhibit IP3-mediated Ca2+ release from the intracellular stores of permeabilized insulinoma and liver cells. This inhibition could be relieved by increasing the IP3 concentration. Radiolabelled IP3 was found to bind tightly to columns prepared from neomycin covalently attached to glass beads. ATP was also bound by these columns. It is concluded that neomycin acts in biological systems as a weak anion exchanger and is therefore unsuitable for use as a specific tool to study the role of inositol phospholipids in intracellular signalling.
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