Graduate Thesis Or Dissertation
 

Purification and identification of a 100 kDa protein, which is tyrosine-phosphorylated by EGF stimulation in SFME cell

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  • Serum-free mouse embryo (SFME) cells, which were derived from 16-day-old Balb/c mouse embryo brain, grow in absence of serum without losing genomic normality or proliferative potential, and require epidermal growth factor (EGF) for normal growth. EGF is a well studied mitogen that binds to a specific receptor on the cell surface membrane to activate the proliferative signal transduction pathways. The activated receptor is a tyrosine specific protein kinase, and tyrosine phosphorylation is one of the important mediators of EGF receptor (EGFR) signal transduction. Using anti-phosphotyrosine Western immunoblotting, we detected a 100 kDa protein which is tyrosine-phosphorylated in response to EGF in SFME cells. This protein is constitutively phosphorylated in an SFME cell line which expresses the neu oncogene. The neu oncogene encodes an analog protein of EGFR which does not require a ligand for activation, and neu-transformed SFME cells are tumorgenic in mice.This protein, p100 was not a fragment of EGFR, and was not antigenically related to other signal transduction phosphoproteins of about 100 kDa. We attempted to purify p100 from neu SFME tumor cells for amino acid sequencing.
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