Bioactive ganglioside-mediated carbohydrate recognition in coupling with ecto-protein phosphorylation

Recent studies, including ours, on bioactive gangliosides revealed that certain gangliosides have an interesting ability to modulate a variety of cell functions. For instance, we demonstrated that a tetrasialoganglioside, GQ1b, promotes neurite outgrowth when added in nanomolar concentrations to cells from two human neuroblastoma cell lines. Also, phosphorylation of several cell surface proteins was observed on addition of ATP. Several lines of evidence indicated that this phosphorylation is probably catalysed by a novel cell surface membrane-bound protein kinase which is specifically activated by a particular ganglioside (Gg). Because of its location on the cell surface we proposed calling this type of kinase(s) ecto-Gg kinase. A procedure to inhibit the phosphorylation of the cell surface protein resulted in suppression of the GQ1b-dependent promotion of neuritogenesis, strongly suggesting that these two cellular events are intricately coupled. Other evidence also indicated that the GQ1b-dependent neuritogenesis is mediated through a receptor-coupled process of the cell surface membrane. Thus, it is likely that this represents a new type of biosignal transduction that is mediated through cell surface carbohydrate recognition (ecto biosignal transduction system).