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J Biol Chem, Vol. 273, Issue 18, 11164-11172, May 1, 1998
d
ocha,
From the Department of Biochemistry, The Institute for Cancer
Research, The Norwegian Radium Hospital, Montebello,
0310 Oslo, Norway
Acidic fibroblast growth factor (aFGF) is a
potent mitogen. It acts through activation of specific cell surface
receptors leading to intracellular tyrosine phosphorylation cascades,
but several reports also indicate that aFGF enters cells and that it
has an intracellular function as well. The aFGF(K132E) mutant binds to
and activates fibroblast growth factor receptors equally strongly as
the wild-type, but it is a poor mitogen. We demonstrate that
aFGF(K132E) enters NIH 3T3 cells and is transported to the nuclear
fraction like wild-type aFGF. A fusion protein of aFGF(K132E) and
diphtheria toxin A-fragment (aFGF(K132E)-DT-A) and a similar fusion
protein containing wild-type aFGF (aFGF-DT-A) were reconstituted with
diphtheria toxin B-fragment. Both fusion proteins were translocated to
the cytosol by the diphtheria toxin pathway and subsequently recovered
from the nuclear fraction. Whereas translocation of aFGF-DT-A
stimulated DNA synthesis in U2OSDR1 cells lacking functional fibroblast
growth factor receptors, aFGF(K132E)-DT-A did not. The mutation
disrupts a protein kinase C phosphorylation site in the growth factor
making it unable to be phosphorylated. The data indicate that a defect
in the intracellular action of aFGF(K132E) is the reason for its
strongly reduced mitogenicity, possibly due to inability to be
phosphorylated.
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