描述:
The plateletderived growth factor (PDGF) family consists of four disulfidelinked
homodimers and one heterodimer (PDGFAB). These proteins regulate diverse
cellular functions through interactions with PDGF Rα and Rβ. Mature PDGF-DD
associates with PDGF Rβ and triggers signaling through PDGF Rβ homodimers
and PDGF Rα/β heterodimers. The human PDGF-DD cDNA encodes a 370 amino
acid (aa) precursor that includes a 23 aa signal sequence, one CUB domain, and
one PDGF/VEGF domain. The PDGF/VEGF domain shares 27 35% aa sequence identity
with the corresponding regions of other PDGF family members. Human PDGF-DD shares
87% aa sequence identity with mouse and rat PDGF-DD. PDGF-DD is secreted as a 100
kDa latent homodimer which is activated by proteolysis to release a 35 kDa bioactive
protein containing the PDGF/VEGF homology domain. A splice variant of PDGF-DD has
a 6 aa deletion near the Nterminus. A 72 aa deletion within the PDGF/VEGF domain
generates an inactive protein in mouse but has not been detected in human. PDGF-DD
is widely expressed in embryonic and adult tissues ,and PDGF Rβ is expressed in a generally
complementary pattern. PDGF-DD functions as a growth factor for renal artery smooth
muscle cells and lens epithelial cells, and as a macrophage chemoattractant. PDGF-DD is
overexpressed in and contributes to several disease states, including renal and hepatic
fibrosis, mesangial proliferative glomerulopathy, pulmonary lymphoid infiltration, and
many cancers. PDGF-DD functions in both paracrine and autocrine manners.
原厂资料:
The plateletderived growth factor (PDGF) family consists of four disulfidelinked
homodimers and one heterodimer (PDGFAB). These proteins regulate diverse
cellular functions through interactions with PDGF Rα and Rβ. Mature PDGF-DD
associates with PDGF Rβ and triggers signaling through PDGF Rβ homodimers
and PDGF Rα/β heterodimers. The human PDGF-DD cDNA encodes a 370 amino
acid (aa) precursor that includes a 23 aa signal sequence, one CUB domain, and
one PDGF/VEGF domain. The PDGF/VEGF domain shares 27 35% aa sequence identity
with the corresponding regions of other PDGF family members. Human PDGF-DD shares
87% aa sequence identity with mouse and rat PDGF-DD. PDGF-DD is secreted as a 100
kDa latent homodimer which is activated by proteolysis to release a 35 kDa bioactive
protein containing the PDGF/VEGF homology domain. A splice variant of PDGF-DD has
a 6 aa deletion near the Nterminus. A 72 aa deletion within the PDGF/VEGF domain
generates an inactive protein in mouse but has not been detected in human. PDGF-DD
is widely expressed in embryonic and adult tissues ,and PDGF Rβ is expressed in a generally
complementary pattern. PDGF-DD functions as a growth factor for renal artery smooth
muscle cells and lens epithelial cells, and as a macrophage chemoattractant. PDGF-DD is
overexpressed in and contributes to several disease states, including renal and hepatic
fibrosis, mesangial proliferative glomerulopathy, pulmonary lymphoid infiltration, and
many cancers. PDGF-DD functions in both paracrine and autocrine manners.