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J. Biol. Chem., Vol. 259, Issue 11, 6818-6825, Jun, 1984
EG Bremer, S Hakomori, DF Bowen-Pope, E Raines and R Ross
Glycosphingolipids added exogenously in cell culture are slowly
incorporated into plasma membranes, inhibit cell growth, and modify growth
behavior ( Laine , R. A., and Hakomori, S. (1973) Biochem. Biophys. Res.
Commun. 54, 1039-1045; Keenan , T. W., Schmid, E., Franke , W. W., and
Wiegandt , H. (1975) Exp. Cell Res. 92, 259-270). With the availability of
purified growth factors and serum-free culture conditions in recent years,
we have been able to examine this phenomenon in mouse Swiss 3T3 cells in
greater detail with the following results. 1) Cell growth (cell number
increase) in serum-free medium was specifically inhibited by the presence
of GM1 and to a lesser extent by GM3, but not by NeuAcnLc4 , although the
gangliosides were incorporated equally well into cell membranes. GM3
inhibited both platelet-derived growth factor (PDGF)- and epidermal growth
factor- stimulated mitogenesis determined by thymidine incorporation, while
GM1 could only inhibit PDGF-stimulated mitogenesis. NeuAcnLc4 had no effect
on mitogen-stimulated thymidine incorporation. 2) The concentration-
dependent binding of 125I-PDGF binding to cells indicated that cells whose
growth was inhibited by GM1 or GM3 showed an increased affinity for PDGF as
compared to cells grown without addition of ganglioside, while the total
number of receptors stayed the same. Addition of ganglioside did not affect
the binding of 125I-EGF. 3) No direct interaction was observed between
gangliosides and growth factors as evidenced by the lack of competition by
ganglioside-containing liposomes for cellular binding of 125I growth
factors. 4) GM1 and GM3, but neither NeuAcnLc4 nor Gb4 , inhibited the
PDGF-stimulated tyrosine phosphorylation by membrane preparations of a
170,000 molecular weight protein, which is probably the PDGF receptor.
Thus, the level of gangliosides GM1 and GM3 in membranes may modulate PDGF
receptor function by affecting the degree of tyrosine phosphorylation and
may alter the affinity of the receptor for PDGF.
Ganglioside-mediated modulation of cell growth, growth factor binding, and receptor phosphorylation
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