AI Article Synopsis
- - Breast cancer cells can travel to bones and promote bone loss by activating osteoclasts, which are cells that break down bone tissue.
- - MacroH2A1.2, a specific form of a histone variant, can inhibit the formation of osteoclasts by breast cancer cells by reducing the expression of lysyl oxidase (LOX), a protein involved in bone remodeling.
- - The study shows that macroH2A1.2 works by interacting with another protein, EZH2, leading to changes in gene expression that prevent LOX from being produced, implying potential strategies for treating bone damage related to breast cancer.
Article Abstract
Breast cancer cells relocate to bone and activate osteoclast-induced bone resorption. Soluble factors secreted by breast cancer cells trigger a cascade of events that stimulate osteoclast differentiation in the bone microenvironment. MacroH2A is a unique histone variant with a C-terminal non-histone domain and plays a crucial role in modulating chromatin organization and gene transcription. Here, we show that macroH2A1.2, one of the macroH2A isoforms, has an intrinsic ability to inhibit breast cancer-derived osteoclastogenesis. This repressive effect requires macroH2A1.2-dependent attenuation of expression and secretion of lysyl oxidase (LOX) in breast cancer cells. Furthermore, our mechanistic studies reveal that macroH2A1.2 physically and functionally interacts with the histone methyltransferase EZH2 and elevates H3K27me3 levels to keep LOX gene in a repressed state. Collectively, this study unravels a role for macroH2A1.2 in regulating osteoclastogenic potential of breast cancer cells, suggesting possibilities for developing therapeutic tools to treat osteolytic bone destruction.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6061927 | PMC |
| http://dx.doi.org/10.1016/j.celrep.2018.06.020 | DOI Listing |
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