Nm. Law et Sa. Rosenzweig, NEURONAL INSULIN-RECEPTORS IN Y79 RETINOBLASTOMA CELLS, Biochemical and biophysical research communications, 210(1), 1995, pp. 58-66
Immunoblot analysis of Y79 cell membrane proteins indicated that Y79 i
nsulin receptors (InsRs) alpha subunits had a mass of 115 kDa. Biosynt
hetic studies revealed a typical transit time for InsR delivery to the
Golgi (similar to 2h) and receptor processing. However, neither the p
roreceptor nor the mature receptor exhibited endoglycosidase H-resista
nce, consistent with a lack of N-linked glycan processing. Insulin sti
mulated a rapid and transient tyrosine phosphorylation of receptor bet
a subunits (95 kDa) and of IRS-1 in intact Y79 cells, whereas in vitro
studies with enriched membrane glycoproteins resulted in the autophos
phorylation of both InsR (95 kDa) and IGF-1-R (98k Da) beta subunits.
These studies provide the first biochemical dissection of InsR structu
re and function in retinoblastoma cells. (C) 1995 Academic Press, Inc.