Post-translational processing of the epidermal growth factor receptor. Glycosylation-dependent acquisition of ligand-binding capacity.
The post-translational processing of the epidermal growth factor receptor in human A431 epidermoid carcinoma cells has been investigated. By employing the affinity matrix epidermal growth factor Affi-Gel in conjunction with immunoprecipitation, it has been demonstrated that core oligosaccharide addition is essential for the acquisition of epidermal growth factor-binding activity. Furthermore, the initial 160-kDa translation product was observed to undergo a processing step by which ligand-binding activity was acquired with a half-time of approximately 30 min while exhibiting no apparent change in mobility on sodium dodecyl sulfate-polyacrylamide gels. This was shown not to involve the conversion of high-mannose chains to complex chains which have been capped with fucose and sialic acid. Possible explanations for this activation in terms of translocation of intermediates and/or formation of disulfide bonds are discussed.
Slieker
L J
LJ
Lane
M D
MD
D050260:Carbohydrate Metabolism; D002294:Carcinoma, Squamous Cell / Q000378:metabolism; D002460:Cell Line; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004815:Epidermal Growth Factor / Q000378:metabolism; D066246:ErbB Receptors; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D011499:Protein Processing, Post-Translational; D011956:Receptors, Cell Surface / Q000096:biosynthesis*; D014415:Tunicamycin / Q000494:pharmacology
D011956:Receptors, Cell Surface; D014415:Tunicamycin; D004815:Epidermal Growth Factor; D066246:ErbB Receptors