[Binding of colchiceine to isolated gangliosides and ganglioside-containing membranes (author's transl)].

The binding of the alkaloid colchicine and its metabolite colchiceine to different membranes and gangliosides has been investigated. In contrast to colchicine, colchiceine binds to erythrocyte ghosts, plasma membranes of rat liver and heart muscle, and synaptosomes of rat brain. The binding properties of isolated gangliosides are analogous to those of the membranes investigated. On a molar basis the binding capacities of the gangliosides GT1, GD1a and GM1 for colchiceine are 7:4:1, respectively. The binding of alkaloid to ganglioside structures is diminished in the presence of EDTA and after pretreatment with neuraminidase, suggesting a specific, Ca2 -dependent interaction of colchiceine with gangliosides. The results are discussed with respect to the different biological activities of colchicine and its metabolite colchiceine.