描述：
The plateletderived growth factor (PDGF) family consists of proteins derived from four
genes (PDGF-A, -B, -C, and -D) that form four disulfidelinked homodimers (PDGF-AA, -BB,
-CC, and -DD) and one heterodimer (PDGF-AB) .These proteins regulate diverse cellular
functions by binding to and inducing the homoor heterodimerization of two receptor
tyrosine kinases (PDGF Rα and Rβ). Within the PDGF family, PDGF-C and PDGF-D constitute
a subgroup that shares similar structural organization.Both proteins are secreted as inactive
homodimeric latent growth factors. Each monomer has two distinct protein domains: an
Nterminal CUB domain; and a C-terminal PDGF/VEGF homology domain that shares 27 - 35% sequence identity with the corresponding regions of other PDGF family members. An
80-90 amino acid residue hinge region connects the two domains. Sequential removal of
the CUB domains in the homodimeric latent growth factor by extracellular proteolytic
cleavage at the hinge region is required to release the bioactive PDGF/VEGF homology
domain. Twelve cysteine residues are found within the PDGF/VEGF homology domain of
PDGF-C, including the characteristic eight invariant cysteine residues involved in inter-and
intra-chains disulfidebonds needed for the formation of the cysteineknot structure. Bioactive
PDGF-CC binds with highaffinity to PDGF Rα but not PDGF Rβand activates PDGF Rα
homodimerization. PDGF-CC has also been shown to activate PDGF Rαβ heterodimers.
PDGF-CC is expressed in multiple embryonic and adult cell types and tissues. During
embryonic development, PDGFCC is involved in ductal morphogenesis. PDGF-CC is a potent
angiogenic factor that stimulates vessel growth in the mouse cornea pocket assay and in the
CAM assay. It stimulates coronary artery smooth muscle cell proliferation and may play an
important role in cardiovascular development and function. PDGF-CC is also expressed in many
tumors and tumor cell lines and has a causative role in tumorigenesis. Mature human and
mouse PDGF-C share 93.7% amino acid sequence identity.
原厂资料：
The plateletderived growth factor (PDGF) family consists of proteins derived from four
genes (PDGF-A, -B, -C, and -D) that form four disulfidelinked homodimers (PDGF-AA, -BB,
-CC, and -DD) and one heterodimer (PDGF-AB) .These proteins regulate diverse cellular
functions by binding to and inducing the homoor heterodimerization of two receptor
tyrosine kinases (PDGF Rα and Rβ). Within the PDGF family, PDGF-C and PDGF-D constitute
a subgroup that shares similar structural organization.Both proteins are secreted as inactive
homodimeric latent growth factors. Each monomer has two distinct protein domains: an
Nterminal CUB domain; and a C-terminal PDGF/VEGF homology domain that shares 27 - 35% sequence identity with the corresponding regions of other PDGF family members. An
80-90 amino acid residue hinge region connects the two domains. Sequential removal of
the CUB domains in the homodimeric latent growth factor by extracellular proteolytic
cleavage at the hinge region is required to release the bioactive PDGF/VEGF homology
domain. Twelve cysteine residues are found within the PDGF/VEGF homology domain of
PDGF-C, including the characteristic eight invariant cysteine residues involved in inter-and
intra-chains disulfidebonds needed for the formation of the cysteineknot structure. Bioactive
PDGF-CC binds with highaffinity to PDGF Rα but not PDGF Rβand activates PDGF Rα
homodimerization. PDGF-CC has also been shown to activate PDGF Rαβ heterodimers.
PDGF-CC is expressed in multiple embryonic and adult cell types and tissues. During
embryonic development, PDGFCC is involved in ductal morphogenesis. PDGF-CC is a potent
angiogenic factor that stimulates vessel growth in the mouse cornea pocket assay and in the
CAM assay. It stimulates coronary artery smooth muscle cell proliferation and may play an
important role in cardiovascular development and function. PDGF-CC is also expressed in many
tumors and tumor cell lines and has a causative role in tumorigenesis. Mature human and
mouse PDGF-C share 93.7% amino acid sequence identity.
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