PDGF-DD
PDGF-DD is the proteolytically activated homodimer of the PDGF-D chain and acts chiefly through PDGFR-beta, with lower activity at PDGFR-alpha/beta heterodimers. Native PDGF-D is secreted latent and must be cleaved within its CUB domain, for example by tissue plasminogen activator, to release the active growth factor. Mature PDGF-DD stimulates mesenchymal cell proliferation and migration, promotes angiogenesis, and is overexpressed in several carcinomas where it recruits stroma and supports invasion. Because it bypasses the latent-state requirement, recombinant PDGF-DD is the preferred reagent for probing PDGFR-beta signaling, pericyte biology, and tumor microenvironment crosstalk in vitro.
