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Upregulation of TGF-β-induced HSP27 by HSP90 inhibitors in osteoblasts.

BMC musculoskeletal disorders | 2022

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.

Pubmed ID: 35619094 RIS Download

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Associated grants

  • Agency: Government of Japan Ministry of Education Culture Sports Science and Technology,
    Id: 19K18471
  • Agency: Government of Japan Ministry of Education Culture Sports Science and Technology,
    Id: 15K10487 and 17K11002
  • Agency: National Center for Geriatrics and Gerontology,
    Id: 28-9 and 29-12

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MC3T3-E1 (tool)

RRID:CVCL_0409

Cell line MC3T3-E1 is a Spontaneously immortalized cell line with a species of origin Mus musculus

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