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  • Title: The role of chordin fragments generated by partial tolloid cleavage in regulating BMP activity.
    Author: Troilo H, Barrett AL, Wohl AP, Jowitt TA, Collins RF, Bayley CP, Zuk AV, Sengle G, Baldock C.
    Journal: Biochem Soc Trans; 2015 Oct; 43(5):795-800. PubMed ID: 26517884.
    Abstract:
    Chordin-mediated regulation of bone morphogenetic protein (BMP) family growth factors is essential in early embryogenesis and adult homoeostasis. Chordin binds to BMPs through cysteine-rich von Willebrand factor type C (vWC) homology domains and blocks them from interacting with their cell surface receptors. These domains also self-associate and enable chordin to target related proteins to fine-tune BMP regulation. The chordin-BMP inhibitory complex is strengthened by the secreted glycoprotein twisted gastrulation (Tsg); however, inhibition is relieved by cleavage of chordin at two specific sites by tolloid family metalloproteases. As Tsg enhances this cleavage process, it serves a dual role as both promoter and inhibitor of BMP signalling. Recent developments in chordin research suggest that rather than simply being by-products, the cleavage fragments of chordin continue to play a role in BMP regulation. In particular, chordin cleavage at the C-terminus potentiates its anti-BMP activity in a type-specific manner.
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