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. / Graduation date: 1997
| Identifer | oai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/34207 |
| Date | 01 May 1997 |
| Creators | Murayama, Kaoru |
| Contributors | Barnes, David W. |
| Source Sets | Oregon State University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
Page generated in 0.001 seconds