Ganglioside GM(1) biphasically regulates the activity of protein kinase C by the effects on the structure of the lipid bilayer.

Addition of a small amount of ganglioside GM(1) to phosphatidylserine (PS) liposomes, a gradual increase of protein kinase C (PKC) activity was recorded up to about 2 mol% GM(1) where the maximal enzyme activity was obtained. Then the activity of PKC began to decline and even turned to be inhibited with the further increase of GM(1) content. It was also indicated that GM(1)/PS binary liposomes had the highest membrane fluidity and very low spatial density of lipid headgroups which was demonstrated in the MC-540 studies due to the interposition of GM(1) when the liposomes contained about 2 mol% GM(1). Besides, the liposomes containing about 2 mol% GM(1) provided a more hydrophobic environment for PKC than the liposomes containing less or more GM(1) which was indicated in the Acrylodan experiments. These factors commonly induced PKC to be stimulated maximally. Whether at the lower or higher GM(1) content, the membrane structure was not the most suitable to support the activity of PKC, which declined as a consequence.