Platelet-derived growth factor (PDGF) [1,2] is a potent mitogen for cells of
mesenchymal origin, including smooth muscle cells and glial cells. PDGF
consists of two different but closely related chains (A and B chains) which
assemble to form disulfide linked homo- or heterodimers (A-A, B-B, an A-B).
Alternate splicing of the A chain transcript can give rise to two different
forms that differ only in their C-terminal extremity. The transforming protein
of simian sarcoma virus (SSV), encoded by the v-sis oncogene, is derived from
the B chain of PDGF.
PDGF is structurally related to a number of other growth factors which also
form disulfide-linked homo- or heterodimers:
Vascular endothelial growth factor (VEGF), also known as vascular
permeability factor (VPF) [3], a growth factor active in angiogenesis and
endothelial cell growth. The genome of the orf poxvirus encodes an homolog
of VEGF [4].
Vascular endothelial growth factor B (VEGF-B), also active in angiogenesis
and endothelial cell growth [5].
Vascular endothelial growth factor B (VEGF-C), also active in angiogenesis
and endothelial cell growth [6].
Placenta growth factor (PlGF) [7], which is also active in agiogenesis.
As a signature pattern for this family of growth factors, we selected a region
that include four of the eight cysteines conserved in the sequences of these
proteins. In PDGF, these cysteines are known to be involved in intra- and
inter-chain disulfide bonds [8]. We also developed a profile that spans the
eight conserved cysteines.
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