{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kim MY"],"funding":["National Research Foundation of Korea"],"pagination":["7044"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6504882"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(1)"],"pubmed_abstract":["c-Fms is the macrophage colony-stimulating factor (M-CSF) receptor, and intracellular signalling via the M-CSF/c-Fms axis mediates both innate immunity and bone remodelling. M-CSF-induced transient proteolytic degradation of c-Fms modulates various biological functions, and protein kinase C (PKC) signalling is activated during this proteolytic process via an unknown mechanism. Notably, the role of specific PKC isoforms involved in c-Fms degradation during osteoclast differentiation is not known. Here, we observed that inactivation of PKCδ by the biochemical inhibitor rottlerin, a cell permeable peptide inhibitor, and short hairpin (sh) RNA suppresses osteoclast differentiation triggered by treatment with M-CSF and receptor activator of NF-κB ligand. Interestingly, inhibition of PKCδ by eit"],"journal":["Scientific reports"],"pubmed_title":["Specific targeting of PKCδ suppresses osteoclast differentiation by accelerating proteolysis of membrane-bound macrophage colony-stimulating factor receptor."],"pmcid":["PMC6504882"],"funding_grant_id":["Nos. 2016R1A2B2012108 and 2015R1A5A2009124"],"pubmed_authors":["Shin HI","Jeong D","Kim MY","Lee K"],"additional_accession":[]},"is_claimable":false,"name":"Specific targeting of PKCδ suppresses osteoclast differentiation by accelerating proteolysis of membrane-bound macrophage colony-stimulating factor receptor.","description":"c-Fms is the macrophage colony-stimulating factor (M-CSF) receptor, and intracellular signalling via the M-CSF/c-Fms axis mediates both innate immunity and bone remodelling. M-CSF-induced transient proteolytic degradation of c-Fms modulates various biological functions, and protein kinase C (PKC) signalling is activated during this proteolytic process via an unknown mechanism. Notably, the role of specific PKC isoforms involved in c-Fms degradation during osteoclast differentiation is not known. Here, we observed that inactivation of PKCδ by the biochemical inhibitor rottlerin, a cell permeable peptide inhibitor, and short hairpin (sh) RNA suppresses osteoclast differentiation triggered by treatment with M-CSF and receptor activator of NF-κB ligand. Interestingly, inhibition of PKCδ by eit","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 May","modification":"2025-04-22T09:23:30.191Z","creation":"2019-06-06T23:28:30Z"},"accession":"S-EPMC6504882","cross_references":{"pubmed":["31065073"],"doi":["10.1038/s41598-019-43501-2"]}}