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  • Exogenous noggin binds the BMP-2 receptor and induces alkaline phosphatase activity in osteoblasts

    Author(s)
    Hashimi, Saeed M
    Griffith University Author(s)
    Hashimi, Saeed M.
    Year published
    2019
    Metadata
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    Abstract
    Osteogenesis is an important process in bone remodeling and is under strict cellular signaling governed by growth factors and antagonists. Bone morphogenetic protein 2 (BMP-2) is an important osteogenic factor involved in the transcription of key osteogenic genes such as alkaline phosphatase (ALP). While, antagonists such as noggin effectively restrict osteoblast differentiation through binding to BMP-2. In this study, we sought to understand the effect of exogenous noggin in osteoblasts and its role in BMP-2 activation of osteogenesis. Enzymatic activity of ALP was monitored to ascertain the effect of the noggin. Fluorescently ...
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    Osteogenesis is an important process in bone remodeling and is under strict cellular signaling governed by growth factors and antagonists. Bone morphogenetic protein 2 (BMP-2) is an important osteogenic factor involved in the transcription of key osteogenic genes such as alkaline phosphatase (ALP). While, antagonists such as noggin effectively restrict osteoblast differentiation through binding to BMP-2. In this study, we sought to understand the effect of exogenous noggin in osteoblasts and its role in BMP-2 activation of osteogenesis. Enzymatic activity of ALP was monitored to ascertain the effect of the noggin. Fluorescently labelled noggin was used to determine the binding of noggin to the BMP-2 receptor. The results demonstrated that noggin significantly increases the activity of ALP at concentrations of 50 to 400 ng/mL. While, it inhibited the activity of exogenous BMP-2. Furthermore, fluorescently labelled noggin showed strong binding to osteoblasts which were perturbed when cells were preincubated with BMP-2 suggesting that noggin shares a common receptor with BMP-2. These results suggest that exogenous noggin facilitates osteogenic differentiation and provide a novel mechanism for its interplay with BMP-2.
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    Journal Title
    JOURNAL OF CELLULAR BIOCHEMISTRY
    Volume
    120
    Issue
    8
    DOI
    https://doi.org/10.1002/jcb.28597
    Subject
    Biochemistry and cell biology
    Medical physiology
    Publication URI
    http://hdl.handle.net/10072/386026
    Collection
    • Journal articles

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