Active caspase-3 is required for osteoclast differentiation
Document Type
Article
Publication Date
2006
Abstract
Based on our earlier observation that caspase-3 is present in osteoclasts that are not undergoing apoptosis, we investigated the role of this protein in the differentiation of primary osteoclasts and RAW264.7 cells (Szymczyk KH, et al, 2005, Caspase-3 activity is necessary for RANKL-induced osteoclast differentiation. The Proceedings of the 8th ICCBMT). We noted that osteoclast numbers are decreased in long bones of procaspase-3 knockout mice and that receptor activator of NF-κB ligand (RANKL) does not promote differentiation of isolated preosteoclasts. In addition, after treatment with inhibitors of caspase-3 activity, neither the wild-type primary nor the RAW264.7 cells express TRAP or became multinucleated. We found that immediately following RANKL treatment, procaspase-3 is cleaved and the activated protein is localized to lipid regions of the plasma membrane and the cytosol. We developed RAW264.7 procaspase-3 knockdown clonal cell lines using RNAi technology. Again, treatment with RANKL fails to induce TRAP activity or multinucleation. Finally, we evaluated NF-κB in procaspase-3 silenced cells. We found that RANKL treatment prevented activation and nuclear translocation of NF-κB. Together these findings provide direct support for the hypothesis that caspase-3 activity is required for osteoclast differentiation. © 2006 Wiley-Liss, Inc.
Publication Title
Journal of cellular physiology
Volume
209
Issue
3
First Page
836
Last Page
844
Recommended Citation
Szymczyk, K. H.; Freeman, T. A.; Adams, Christopher S.; Srinivas, V.; and Steinbeck, M. J., "Active caspase-3 is required for osteoclast differentiation" (2006). PCOM Scholarly Works. 1588.
https://digitalcommons.pcom.edu/scholarly_papers/1588
Comments
This article was published in Journal of cellular physiology, Volume 209, Issue 3, Pages 836-844.
The published version is available at http://dx.doi.org/10.1002/jcp.20770.Copyright © 2006.