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M-CSF potently augments RANKL-induced resorption activation in mature human osteoclasts

Hodge, Jason M, Collier, Fiona M, Pavlos, Nathan J, Kirkland, Mark A and Nicholson, Geoffrey C 2011, M-CSF potently augments RANKL-induced resorption activation in mature human osteoclasts, PLoS one, vol. 6, no. 6, pp. 1-8, doi: 10.1371/journal.pone.0021462.

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Title M-CSF potently augments RANKL-induced resorption activation in mature human osteoclasts
Author(s) Hodge, Jason M
Collier, Fiona M
Pavlos, Nathan J
Kirkland, Mark A
Nicholson, Geoffrey C
Journal name PLoS one
Volume number 6
Issue number 6
Article ID e21462
Start page 1
End page 8
Total pages 8
Publisher Public Library of Science
Place of publication San Francisco, Calif.
Publication date 2011-06
ISSN 1932-6203
Keyword(s) actins
blotting, western
cells, cultured
humans
macrophage colony-stimulating factor
mitogen-activated protein kinase 1
mitogen-activated protein kinase 3
NF-kappa B
NFATC transcription factors
osteoclasts
proto-oncogene proteins c-fos
RANK ligand
Summary Macrophage-CSF (M-CSF) is critical for osteoclast (OC) differentiation and is reported to enhance mature OC survival and motility. However, its role in the regulation of bone resorption, the main function of OCs, has not been well characterised. To address this we analysed short-term cultures of fully differentiated OCs derived from human colony forming unit-granulocyte macrophages (CFU-GM). When cultured on dentine, OC survival was enhanced by M-CSF but more effectively by receptor activator of NFκB ligand (RANKL). Resorption was entirely dependent on the presence of RANKL. Co-treatment with M-CSF augmented RANKL-induced resorption in a concentration-dependent manner with a (200-300%) stimulation at 25 ng/mL, an effect observed within 4-6 h. M-CSF co-treatment also increased number of resorption pits and F-actin sealing zones, but not the number of OCs or pit size, indicating stimulation of the proportion of OCs activated. M-CSF facilitated RANKL-induced activation of c-fos and extracellular signal-regulated kinase (ERK) 1/2 phosphorylation, but not NFκB nor nuclear factor of activated T-cells, cytoplasmic-1 (NFATc1). The mitogen-activated protein kinase kinase (MEK) 1 inhibitor PD98059 partially blocked augmentation of resorption by M-CSF. Our results reveal a previously unidentified role of M-CSF as a potent stimulator of mature OC resorbing activity, possibly mediated via ERK upstream of c-fos.
Language eng
DOI 10.1371/journal.pone.0021462
Field of Research 110399 Clinical Sciences not elsewhere classified
MD Multidisciplinary
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2011, Hodge et al
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30101101

Document type: Journal Article
Collections: Institute for Frontier Materials
Open Access Collection
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.