Modified ganglioside as a possible modulator of transmembrane signaling mechanism through growth factor receptors: a preliminary note.
Two types of modified GM3 strongly alter EGF-dependent phosphorylation of the EGF receptor in opposite directions, i.e., de-N-acetyl-GM3 (amino-GM3; NeuNH2 alpha 2----3Gal beta 1----4Glc beta 1----1 Ceramide) strongly promotes tyrosine phosphorylation of the EGF receptor of A431 cells, while lyso-GM3 (NeuNAc alpha 2----3Gal beta 1----4 Glc beta----1 Sphingosine) as well as GM3 inhibit tyrosine phosphorylation of the EGF receptor in the same cells under the same conditions. A hypothesis is proposed that de-N-acylation of gangliosides, in either the sialic acid or ceramide moiety, is a crucial event in triggering a positive or negative transmembrane signal.
D000107:Acetylation; D002460:Cell Line; D002462:Cell Membrane / Q000502:physiology; D004815:Epidermal Growth Factor / Q000502:physiology*; D066246:ErbB Receptors / Q000502:physiology*; D005679:G(M3) Ganglioside / Q000502:physiology*; D005732:Gangliosides / Q000502:physiology*; D006801:Humans; D066298:In Vitro Techniques; D011092:Polyethylene Glycols / Q000494:pharmacology; D011505:Protein-Tyrosine Kinases / Q000502:physiology*; D013329:Structure-Activity Relationship
D005679:G(M3) Ganglioside; D005732:Gangliosides; D011092:Polyethylene Glycols; D004815:Epidermal Growth Factor; D066246:ErbB Receptors; D011505:Protein-Tyrosine Kinases