Summary
We have recently reported that fibrinogen and fibrin bind to fibroblast growth factor-2
(FGF-2) and potentiate its ability to stimulate proliferation of endothelial cells.
In the present report, we have investigated the potential of fibrinogen and fibrin
to protect FGF-2 from proteolytic degradation. FGF-2 was incubated with trypsin or
chymotrypsin in the presence or absence of fibrinogen or fibrin and proteolysis of
FGF-2 was assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)
and Western blotting. In the absence of fibrinogen there was progressive tryptic degradation
of FGF-2, but in the presence of fibrinogen, FGF-2 was completely protected from trypsin
with no evidence of degradation. The degree of protection was maximum at a molar ratio
of FGF-2 to fibrinogen 1:2. Fibrinogen afforded similar protection from degradation
by chymotrypsin. Polymerized fibrin provided partial protection of FGF-2 from tryptic
degradation, with intact FGF-2 present for up to 360 min. Fibrin provided nearly complete
protection from chymotrypsin. These observations indicate that binding of FGF-2 to
fibrinogen or fibrin provides protection from proteolytic degradation, and this may
modulate its cell proliferative activity.
Key words
Fibrinogen - FGF-2 - trypsin - proteolysis