<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kuroyanagi G</submitter><funding>Government of Japan Ministry of Education Culture Sports Science and Technology</funding><funding>National Center for Geriatrics and Gerontology</funding><pagination>495</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9134601</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>23(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>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.&lt;h4>Methods&lt;/h4>Clonal osteoblastic MC3T3-E1 cells were treated with the HSP90 inhibitors and then stimulated with TGF-β. HSP27 expression and the phos</pubmed_abstract><journal>BMC musculoskeletal disorders</journal><pubmed_title>Upregulation of TGF-β-induced HSP27 by HSP90 inhibitors in osteoblasts.</pubmed_title><pmcid>PMC9134601</pmcid><funding_grant_id>19K18471</funding_grant_id><funding_grant_id>15K10487 and 17K11002</funding_grant_id><funding_grant_id>28-9 and 29-12</funding_grant_id><pubmed_authors>Sakai G</pubmed_authors><pubmed_authors>Kawabata T</pubmed_authors><pubmed_authors>Kuroyanagi G</pubmed_authors><pubmed_authors>Kim W</pubmed_authors><pubmed_authors>Tachi J</pubmed_authors><pubmed_authors>Tokuda H</pubmed_authors><pubmed_authors>Matsushima-Nishiwaki R</pubmed_authors><pubmed_authors>Hioki T</pubmed_authors><pubmed_authors>Fujita K</pubmed_authors><pubmed_authors>Iida H</pubmed_authors><pubmed_authors>Kozawa O</pubmed_authors><pubmed_authors>Otsuka T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Upregulation of TGF-β-induced HSP27 by HSP90 inhibitors in osteoblasts.</name><description>&lt;h4>Background&lt;/h4>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.&lt;h4>Methods&lt;/h4>Clonal osteoblastic MC3T3-E1 cells were treated with the HSP90 inhibitors and then stimulated with TGF-β. HSP27 expression and the phos</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 May</publication><modification>2025-04-26T02:38:54.065Z</modification><creation>2025-02-19T02:16:21.138Z</creation></dates><accession>S-EPMC9134601</accession><cross_references><pubmed>35619094</pubmed><doi>10.1186/s12891-022-05419-1</doi></cross_references></HashMap>