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Updated: Oct 2, 2026

Osteoclast Derivation from Mouse Bone Marrow
Published on: November 6, 2014
Regulation of aromatase activity in bone-derived cells: possible role of mitogen-activated protein kinase
M Shozu1, H Sumitani, K Murakami
1Department of Obstetrics and Gynecology, School of Medicine, Kanazawa University, 13-1 Takara-machi, 920-0934, Kanazawa, Japan. shozu@med.kanazawa-u.ac.jp
Abstract:
Fetal human osteoblast-like cells and the THP-1 cell line that differentiates into macrophage/osteoblast-like cells in the presence of Vitamin D3 and which possesses high aromatase activity, constitute a useful model with which to study the regulation of aromatase in bone. We showed that dexamethasone (DEX)-induced aromatase activity in the THP-1 cell line is completely suppressed by forskolin and by dibutyryl cAMP. We therefore investigated the contribution of mitogen-activated protein kinase (MAPK) to the regulation of aromatase, because cAMP inhibits MAPK in many cells. We examined the role of MAPK on aromatase activity using PD98059, a selective inhibitor of MEK-1. PD98059 (100 microM) reduced DEX+interleukin (IL)-1beta-induced aromatase activity in human osteoblast-like cells by more than 90%, whereas 50% of the aromatase mRNA concentration was retained compared with the control incubated with DEX+IL-1beta. PD98059 (50 microM) reduced the activity of aromatase in THP-1 cells by 80% without significantly affecting the mRNA level. These results indicated that MAPK plays an important role in aromatase activation at the post-transcriptional level.
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