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Cutting edge: Bone morphogenetic protein antagonists Drm/Gremlin and Dan interact with slits and act as negative regulators of monocyte chemotaxis

  1. Author:
    Chen, B.
    Blair, D. G.
    Plisov, S.
    Vasiliev, G.
    Perantoni, A. O.
    Chen, Q.
    Athanasiou, M.
    Wu, J. Y.
    Oppenheim, J. J.
    Yang, D.

  2. Author Address

    NCI, SAIC Frederick Inc, Basic Res Program, Frederick, MD 21702 USA. NCI, Basic Res Lab, Ctr Canc Res, Frederick, MD 21702 USA. NCI, Comparat Carcinogenesis Lab, Canc Res Ctr, Frederick, MD 21702 USA. NCI, Mol Immunoregulat Lab, Ctr Canc Res, Frederick, MD 21702 USA. Vanderbilt Univ, Med Ctr, Nashville, TN 37232 USA Yang, D, NCI, SAIC Frederick Inc, Basic Res Program, Bldg 560,Room 31-19,1050 Boyles St, Frederick, MD 21702 USA
    1. Year: 2004
    2. Date: NOV 15
  2. Journal: Journal of Immunology
    1. 173
    2. 10
    3. Pages: 5914-5917
  4. Type of Article: Article
  1. Abstract:

    Drm/Gremlin and Dan, two homologous secreted antagonist of bone morphogenic proteins have been shown to regulate early development, tumorigenesis, and renal pathophysiology. In this study, we report that Drm and Dan physically and functionally interact with Slit1 and Slit2 proteins. Drm binding to Slits depends on its glycosylation and is not interfered with by bone morphogenic proteins. Importantly, Drm and Dan function as inhibitors for monocyte migration induced by stromal cell-derived factor 1alpha (SDF-1alpha) or fMLP. The inhibition of SDF-1alpha-induced monocyte chemotaxis by Dan is not due to blocking the binding of SDF-1alpha to its receptor. Thus, the results identify that Drm and Dan can interact with Slit proteins and act as inhibitors of monocyte chemotaxis, demonstrating a previously unidentified biological role for these proteins

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  1. View record in Web of Science®
  2. WOS: 000224999000003

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