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Molecular and Cellular Biochemistry

, Volume 349, Issue 1–2, pp 195–204 | Cite as

Prolactin alters the mRNA expression of osteoblast-derived osteoclastogenic factors in osteoblast-like UMR106 cells

  • Kannikar Wongdee
  • Warut Tulalamba
  • Jirawan Thongbunchoo
  • Nateetip Krishnamra
  • Narattaphol Charoenphandhu
Article

Abstract

Prolactin (PRL) is known to participate in the lactation-induced maternal bone loss, presumably by inducing the release of receptor activator of nuclear factor-κB ligand (RANKL), a potent osteoclastogenic factor from osteoblasts. Since maternal bone resorption was too massive to be solely explained by RANKL and osteoclasts did not express PRL receptors (PRLR), the involvement of some other osteoblast-derived osteoclastogenic modulators was anticipated. Herein, the authors used quantitative real-time PCR to investigate the mRNA expressions of various osteoclastogenic factors in osteoblast-like UMR106 cells directly exposed to PRL for 48 h. These cells were found to express PRLR and respond to 300 ng/ml PRL by increasing RANKL mRNA expression. This PRL concentration (comparable to plasma PRL levels in lactation) also induced the upregulation of monocyte chemoattractant protein (MCP)-1, cyclooxygenase (Cox)-2, and ephrin-B1, whereas a higher concentration (500 ng/ml) was required to upregulate tumor necrosis factor (TNF)-α and interleukin (IL)-1. However, 100–500 ng/ml PRL affected neither the cell proliferation, the cell viability nor the mRNA expressions of macrophage colony-stimulating factor, IL-6, ephrin type-B receptor 4 and ephrin-B2. In conclusion, besides RANKL overexpression, PRL upregulated the expressions of other osteoclastogenic modulators, i.e., MCP-1, Cox-2, TNF-α, IL-1, and ephrin-B1, thus, further explaining how PRL induced bone loss in lactating mothers.

Keywords

Hyperprolactinemia Osteoblast-derived factors Osteoclastogenesis Prolactin receptor RANKL Real-time PCR 

Notes

Acknowledgments

The authors thank Amporn Nuntapornsak and Wacharaporn Tiyasatkulkovit for their excellent technical assistance. This research was supported by grants from the Faculty of Science, Mahidol University (SCY52-02 and SCR53-06 to N. Charoenphandhu), the Faculty of Allied Health Sciences, Burapha University (to K. Wongdee), and Thailand Research Fund (RSA5180001 to N. Charoenphandhu).

Conflict of interest

None.

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Copyright information

© Springer Science+Business Media, LLC. 2010

Authors and Affiliations

  • Kannikar Wongdee
    • 1
    • 2
  • Warut Tulalamba
    • 1
    • 3
  • Jirawan Thongbunchoo
    • 1
  • Nateetip Krishnamra
    • 1
    • 4
  • Narattaphol Charoenphandhu
    • 1
    • 4
  1. 1.Consortium for Calcium and Bone Research (COCAB), Faculty of ScienceMahidol UniversityBangkokThailand
  2. 2.Faculty of Allied Health SciencesBurapha UniversityChonburiThailand
  3. 3.Molecular Medicine Graduate Program, Faculty of ScienceMahidol UniversityBangkokThailand
  4. 4.Department of Physiology, Faculty of ScienceMahidol UniversityBangkokThailand

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