{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Huang W"],"funding":["NCI NIH HHS"],"pagination":["4527-35"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3482867"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(42)"],"pubmed_abstract":["Although increasing evidence suggests a critical role for platelet-derived growth factor (PDGF) receptor β (β-PDGFR) signaling in prostate cancer (PCa) progression, the precise roles of β-PDGFR and PDGF isoform-specific cell signaling have not been delineated. Recently, we identified the PDGF-D isoform as a ligand for β-PDGFR in PCa and showed that PDGF-D is activated by serine protease-mediated proteolytic removal of the CUB domain in a two-step process, yielding first a hemidimer (HD) and then a growth factor domain dimer. Herein, we demonstrate that the expression of PDGF-D in human PCa LNCaP cells leads to enhanced bone tumor growth and bone responses in immunodeficient mice. Histopathological analyses of bone tumors generated by PDGF-D-expressing LNCaP cells (LNCaP-PDGF-D) revealed os"],"journal":["Oncogene"],"pubmed_title":["A novel function for platelet-derived growth factor D: induction of osteoclastic differentiation for intraosseous tumor growth."],"pmcid":["PMC3482867"],"funding_grant_id":["CA123362","CA64139","R01 CA064139","R01 CA123362","T32-CA009531","R29 CA064139","R01 CA137280","T32 CA009531","R01CA137280"],"pubmed_authors":["Fridman Y","Saliganan A","Cher ML","Wiesner C","Huang W","Bonfil RD","Ustach CV","Kim HR","Conley-LaComb MK"],"additional_accession":[]},"is_claimable":false,"name":"A novel function for platelet-derived growth factor D: induction of osteoclastic differentiation for intraosseous tumor growth.","description":"Although increasing evidence suggests a critical role for platelet-derived growth factor (PDGF) receptor β (β-PDGFR) signaling in prostate cancer (PCa) progression, the precise roles of β-PDGFR and PDGF isoform-specific cell signaling have not been delineated. Recently, we identified the PDGF-D isoform as a ligand for β-PDGFR in PCa and showed that PDGF-D is activated by serine protease-mediated proteolytic removal of the CUB domain in a two-step process, yielding first a hemidimer (HD) and then a growth factor domain dimer. Herein, we demonstrate that the expression of PDGF-D in human PCa LNCaP cells leads to enhanced bone tumor growth and bone responses in immunodeficient mice. Histopathological analyses of bone tumors generated by PDGF-D-expressing LNCaP cells (LNCaP-PDGF-D) revealed os","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Oct","modification":"2025-07-06T03:05:45.696Z","creation":"2025-07-06T03:05:45.696Z"},"accession":"S-EPMC3482867","cross_references":{"pubmed":["22158043"],"doi":["10.1038/onc.2011.573"]}}