Quantitative analysis of EGFR affinity to immobilized glycolipids by surface plasmon resonance.
EGF-induced activation of EGFR tyrosine kinase is known to be inhibited by ganglioside GM3, its dimer, and other mimetics. However, details of the interaction, such as kinetic properties, have not yet been clarified. The direct interaction is now defined by the surface plasmon resonance (SPR) technique. To determine the affinity of EGFR for lyso-GM3 or lyso-GM3 mimetic, these glycolipid ligands were covalently immobilized onto a sensor chip, and binding affinities were investigated. Results of these studies confirmed the direct interaction of lyso-GM3 or its mimetic with EGFR. A strong interaction between EGFR and lyso-GM3 or its mimetic was indicated by increased binding of EGFR to glycolipid-immobilized surface, in an EGFR dose-dependent manner.
Haga
Yoshimi
Y
Institute of Industrial Science, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo 153-8505, Japan.
Hakomori
Sen-itiroh
SI
Hatanaka
Kenichi
K
D040761:Biomimetic Materials / Q000378:metabolism; D002240:Carbohydrate Sequence; D066246:ErbB Receptors / Q000378:metabolism*; D005679:G(M3) Ganglioside / Q000031:analogs & derivatives / Q000378:metabolism; D006017:Glycolipids / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D007700:Kinetics; D029901:Maackia / Q000378:metabolism; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000378:metabolism; D011485:Protein Binding; D020349:Surface Plasmon Resonance; D013499:Surface Properties
D005679:G(M3) Ganglioside; D006017:Glycolipids; D037121:Plant Lectins; C056605:lyso-G(M3) ganglioside; D066246:ErbB Receptors