Role of low-molecular-weight heat shock protein and the molecular mechanism in bone metabolism

2014 Fiscal Year Final Research Report

• Project/Area Number: 24592273
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Orthopaedic surgery
• Research Institution: Nagoya City University
• Principal Investigator: FUKUOKA Muneyoshi 名古屋市立大学, 医学(系)研究科(研究院), 講師 (80285204)
• Co-Investigator(Kenkyū-buntansha): MIZUTANI Jun 名古屋市立大学, 大学院医学研究科, 講師 (70326156) ; OTSUKA Takanobu 名古屋市立大学, 大学院医学研究科, 教授 (10185316) ; KOZAWA Osamu 岐阜大学, 大学院医学研究科, 教授 (90225417)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 骨芽細胞 / HSP27 / 骨代謝 / 骨粗鬆症 / オステオカルシン / eIF4E / 翻訳

Outline of Final Research Achievements

Heat shock proteins (HSPs) are induced by a variety of physiological and environmental stresses, such as heat. As molecular chaperones, HSPs facilitate the refolding of unfolded proteins. However, the details behind the HSP27-mediated effects on osteoblasts remain to be clarified. In the present study, in order to investigate the exact mechanism of HSP27 and its phosphorylation in osteoblasts, we explored the molecular targets of HSP27 using osteoblast-like MC3T3-E1 cells. Our results strongly suggest that the phosphorylation status of HSP27 play a role in switching its binding to eIF4E, resulting in regulation of the translation initiation process in osteoblasts.

Free Research Field

骨代謝