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HSP70 Inhibitor Suppresses IGF-I-Stimulated Migration of Osteoblasts Through p44/p42 MAP Kinase

HSP70 Inhibitor Suppresses IGF-I-Stimulated Migration of Osteoblasts Through p44/p42 MAP Kinase

Tetsu Kawabata, Haruhiko Tokuda, Go Sakai, Kazuhiko Fujita, Rie Matsushima-Nishiwaki, Gen Kuroyanagi, Takanobu Otsuka, Osamu Kozawa

Biomedicines. 2018 Nov 21;6(4):109.

PMID: 30469446

Abstract:

Heat shock protein 70 (HSP70) is a ubiquitously expressed molecular chaperone in a variety of cells including osteoblasts. We previously showed that insulin-like growth factor-I (IGF-I) elicits migration of osteoblast-like MC3T3-E1 cells through the activation of phosphatidylinositol 3-kinase/Akt and p44/p42 mitogen-activated protein (MAP) kinase. In the present study, we investigated the effects of HSP70 inhibitors on the IGF-I-elicited migration of these cells and the mechanism involved. The IGF-I-stimulated osteoblast migration evaluated by a wound-healing assay and by a transwell cell migration was significantly reduced by VER-155008 and YM-08, which are both HSP70 inhibitors. VER-155008 markedly suppressed the IGF-I-induced phosphorylation of p44/p42 MAP kinase without affecting that of Akt. In conclusion, our results strongly suggest that the HSP70 inhibitor reduces the IGF-I-elicited migration of osteoblasts via the p44/p42 MAP kinase.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP812647884	YM-08		812647-88-4	Price

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