Abstract
About 1.5 million fractures occur annually due to osteoporosis, which affects nearly 20% of all women. Osteoporosis is the thinning of bone tissue and loss of bone density over time in which the accrual of fat within the bone results in decreased bone density. Bone turnover relies on a dynamic balance between bone forming cells (osteoblasts) and fat cells (adipocytes). Redirecting these fat cells would allow for new development in treatments for osteoporosis. Bone Morphogenetic Protein 2 (BMP2) initiates osteoblast and adipocyte differentiation. Casein Kinase 2 (CK2) interacts with the Bone Morphogenetic Protein receptor type Ia (BMPRIa) during BMP2 signaling and controls the key regulatory mechanism for osteogenesis; however the mechanism is yet to be determined. Endoglin, a TGF‐β binding protein, plays a part in BMP2 signaling by associating with BMPRIa, but the effect is unclear. Since CK2 release of BMPRIa induces endoglin expression, the effect of endoglin expression on stimulated C2C12 cells was investigated. Our data suggest that endoglin is up‐regulated during BMP2 stimulation and affects differentiation. We postulate that endoglin co‐localizes with the BMPRIa receptor to different membrane areas causing adipogenesis. Data analysis supports that endoglin induces adipogenesis and reduces mineralization through the DeltaC and PP domains. Research support provided by Charles Peter White Fellowship.
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