{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kuroyanagi G"],"funding":["Government of Japan Ministry of Education Culture Sports Science and Technology","National Center for Geriatrics and Gerontology"],"pagination":["495"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9134601"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(1)"],"pubmed_abstract":["Background
Heat shock protein (HSP) 90 functions as a molecular chaperone and is constitutively expressed and induced in response to stress in many cell types. We have previously demonstrated that transforming growth factor-β (TGF-β), the most abundant cytokine in bone cells, induces the expression of HSP27 through Smad2, p44/p42 mitogen-activated protein kinase (MAPK), p38 MAPK, and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in mouse osteoblastic MC3T3-E1 cells. This study investigated the effects of HSP90 on the TGF-β-induced HSP27 expression and the underlying mechanism in mouse osteoblastic MC3T3-E1 cells.Methods
Clonal osteoblastic MC3T3-E1 cells were treated with the HSP90 inhibitors and then stimulated with TGF-β. HSP27 expression and the phos"],"journal":["BMC musculoskeletal disorders"],"pubmed_title":["Upregulation of TGF-β-induced HSP27 by HSP90 inhibitors in osteoblasts."],"pmcid":["PMC9134601"],"funding_grant_id":["19K18471","15K10487 and 17K11002","28-9 and 29-12"],"pubmed_authors":["Sakai G","Kawabata T","Kuroyanagi G","Kim W","Tachi J","Tokuda H","Matsushima-Nishiwaki R","Hioki T","Fujita K","Iida H","Kozawa O","Otsuka T"],"additional_accession":[]},"is_claimable":false,"name":"Upregulation of TGF-β-induced HSP27 by HSP90 inhibitors in osteoblasts.","description":"Background
Heat shock protein (HSP) 90 functions as a molecular chaperone and is constitutively expressed and induced in response to stress in many cell types. We have previously demonstrated that transforming growth factor-β (TGF-β), the most abundant cytokine in bone cells, induces the expression of HSP27 through Smad2, p44/p42 mitogen-activated protein kinase (MAPK), p38 MAPK, and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in mouse osteoblastic MC3T3-E1 cells. This study investigated the effects of HSP90 on the TGF-β-induced HSP27 expression and the underlying mechanism in mouse osteoblastic MC3T3-E1 cells.Methods
Clonal osteoblastic MC3T3-E1 cells were treated with the HSP90 inhibitors and then stimulated with TGF-β. HSP27 expression and the phos","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2025-04-26T02:38:54.065Z","creation":"2025-02-19T02:16:21.138Z"},"accession":"S-EPMC9134601","cross_references":{"pubmed":["35619094"],"doi":["10.1186/s12891-022-05419-1"]}}