Upregulation of TGF-β-induced HSP27 by HSP90 inhibitors in osteoblasts
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 ex...
Main Authors: | Gen Kuroyanagi, Haruhiko Tokuda, Kazuhiko Fujita, Tetsu Kawabata, Go Sakai, Woo Kim, Tomoyuki Hioki, Junko Tachi, Rie Matsushima-Nishiwaki, Takanobu Otsuka, Hiroki Iida, Osamu Kozawa |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2022-05-01
|
Series: | BMC Musculoskeletal Disorders |
Subjects: | |
Online Access: | https://doi.org/10.1186/s12891-022-05419-1 |
Similar Items
-
The Distinct Assignments for Hsp90α and Hsp90β: More Than Skin Deep
by: Cheng Chang, et al.
Published: (2023-01-01) -
Cytosolic Hsp90 Isoform-Specific Functions and Clinical Significance
by: Samarpan Maiti, et al.
Published: (2022-08-01) -
Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection
by: Anna Lubkowska, et al.
Published: (2021-08-01) -
The Chaperone System in Tumors of the Vocal Cords: Quantity and Distribution Changes of Hsp10, Hsp27, Hsp60, and Hsp90 during Carcinogenesis
by: Alessandro Pitruzzella, et al.
Published: (2024-01-01) -
Kajian Heat Shock Protein 90 (HSP90) dalam Pencarian Kandidat Penghambatnya melalui Ekplorasi Bahan Alam Indonesia
by: Rehmadanta Sitepu
Published: (2019-03-01)