描述：
The plateletderived growth factor (PDGF) family consists of proteins derived from four genes
(PDGF-A, -B, -C, and -D) that form four disulfide-linked 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 N-terminal 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 interand intra-chains disulfidebonds needed for the formation
of the cysteineknot structure. Bioactive PDGF-CC binds with high-affinity to PDGF Rα,but not
PDGF Rβ and 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, PDGF-CC 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 disulfide-linked 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 N-terminal 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 interand intra-chains disulfidebonds needed for the formation
of the cysteineknot structure. Bioactive PDGF-CC binds with high-affinity to PDGF Rα,but not
PDGF Rβ and 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, PDGF-CC 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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