Journal of Biological Chemistry · 1990 · 884 citations · 69 references
Life SciencesBiochemistryCell BiologyCell SignalingMolecular Cell BiologySignal TransductionCell Adhesion ReceptorsCell-surface GlycansCell-surface ReceptorsGlycan RecognitionGlycan-protein InteractionsLipid GlycosylationCell Surface GlycoproteinsCell Surface SpecializationsCell-surface Glycan RecognitionGlycosphingolipid InteractionsLectin InteractionsLectin RecognitionLectin-glycan RecognitionTransmembrane Proteins
Glycosphingolipids (GSLs), or their modified catabolites, at the cell surface modulate transmembrane signal transduction by influencing protein kinases associated with growth factor receptors and protein kinase C. On the other hand, the same or different GSLs at the cell surface interact in highly specific fashion with other GSLs or with binding proteins, possibly at the surface of adjacent interacting cells or in the extracellular matrix. The GSL-GSL interaction apparently provides the basis for a specific cell recognition system independent of the fibronectin/integrin or surface lectin systems, occurring earlier during a cell recognition event.
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