Binding of laminin to brain gangliosides and inhibition of laminin-neuron interaction by the gangliosides.
Binding of laminin to glycolipids of neuronal membranes was studied with a thin-layer chromatography overlay assay. The major brain ganglioside GD1A was the main binding component, when chromatograms containing the same molar amount of the different brain gangliosides and the brain sulfatide were incubated with laminin at physiological ionic strength. The possible role of laminin binding to brain gangliosides in laminin-neuron interactions was studied with adhesion assays. It was found that binding of rat brain neurons to laminin is blocked by 10-40 microM brain gangliosides but not by sulfatide. The inhibition by the gangliosides is suggested to be due to competition with the cell surface interaction sites of laminin and not to binding of the gangliosides to the cells. Our findings support the idea that the adhesive and neurite-promoting effect of laminin is dependent on its interaction with gangliosides at the neuronal cell surfaces.
D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002448:Cell Adhesion / Q000187:drug effects; D002855:Chromatography, Thin Layer; D003864:Depression, Chemical; D005732:Gangliosides / Q000378:metabolism* / Q000494:pharmacology / Q000502:physiology; D006017:Glycolipids / Q000378:metabolism; D007797:Laminin / Q000378:metabolism* / Q000502:physiology; D009474:Neurons / Q000166:cytology / Q000187:drug effects*; D011485:Protein Binding; D051381:Rats; D013552:Swine
D005732:Gangliosides; D006017:Glycolipids; D007797:Laminin