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J Biol Chem, Vol. 274, Issue 25, 18081-18086, June 18, 1999
d
ocha, and
From the Department of Biochemistry at The Institute for Cancer
Research, The Norwegian Radium Hospital, Montebello, 0310 Oslo, Norway
Acidic fibroblast growth factor (aFGF) contains a
phosphorylation site recognized by protein kinase C. A non-mitogenic
mutant growth factor is devoid of this phosphorylation site. We have changed amino acids in and close to the phosphorylation site and studied the consequences of this for binding of the growth factor to
high affinity receptors as well as to heparin. We have also studied the
ability of the mutants to stimulate DNA synthesis and cell
proliferation as well as phosphorylation of mitogen-activated protein
kinase and the ability of the growth factor mutants to be transported
to the nucleus. The results indicate that while the mutations strongly
affect the ability of the growth factor to bind to heparin, they do not
affect much the binding to the specific FGF receptors, activation of
mitogen-activated protein kinase or transport of the growth factor to
the nucleus. The mutations affect to various extents the ability of the
growth factor to stimulate DNA synthesis and to induce cell
multiplication. We find that phosphorylation of aFGF is not required
for mitogenic activity. The data suggest that altered interaction of
the growth factor with a cellular component different from the
receptor, possibly a component in the nucleus, is the reason for the
different mitogenicity of the different growth factor mutants.
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