Interaction of guanidinium compounds and K+ channel modulators with imidazoline binding sites in rabbit kidney.

Several guanidinium compounds were tested for their ability to inhibit the binding of [3H]idazoxan to the I2 subtype of the imidazoline site on rabbit kidney basolateral membranes. Phenformin, a biguanide, was the most potent with an IC50 of 50 +/- 3 microM. Various K+ channel modulators were also evaluated for inhibition of [3H]idazoxan binding.

Induction of intracellular acyl-CoA:cholesterol acyltransferase activity in glioblastoma cells by lidocaine.

The perturbation of cellular cholesteryl ester biosynthesis in glioblastoma C-6 cells by lidocaine was investigated. Lidocaine specifically inhibited the incorporation of radioactive oleic acid into cellular cholesteryl ester but had no significant effect on the incorporation of oleic acid into phosphatidylcholine. Oxygenated cholesterol-enhanced cholesteryl ester formation was less sensitive to lidocaine inhibition.