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Blood, 1 June 2001, Vol. 97, No. 11, pp. 3450-3457
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Differential regulation of the fibroblast growth factor
(FGF) family by  2-macroglobulin: evidence
for selective modulation of FGF-2-induced
angiogenesis
Iain R. Asplin,
Sean M. Wu,
Smitha Mathew,
Gourab Bhattacharjee, and
Salvatore V. Pizzo
From the Department of Pathology, Duke University
Medical Center, Durham, NC.
The fibroblast growth factor (FGF) family has an important role in
processes such as angiogenesis, wound healing, and development in which
precise control of proteinase activity is important. The human plasma
proteinase inhibitor  2-macroglobulin (2M)
regulates cellular growth by binding and modulating the activity of
many cytokines and growth factors. These studies investigate the
ability of native and activated 2M (2M*)
to bind to members of the FGF family. Both 2M and
2M* bind specifically and saturably to FGF-1, -2, -4, and -6, although the binding to 2M* is of significantly higher affinity. Neither 2M nor 2M* bind
to FGF-5, -7, -9, or -10. FGF-2 was chosen for more extensive study in
view of its important role in angiogenesis. It was demonstrated that
FGF-2 binds to the previously identified TGF- binding site. The
2M* inhibits FGF-2-dependent fetal bovine heart
endothelial cell proliferation in a dose-dependent manner.
Unexpectedly, 2M* does not affect FGF-2-induced
vascular tubule formation on Matrigel basement membrane matrix or
collagen gels. Further studies demonstrate that FGF-2 partitions
between fluid-phase 2M* and solid-phase Matrigel or collagen. These studies suggest that the ability of 2M*
to modulate the activity of FGF-2 is dependent on an interplay with
extracellular matrix components.
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