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CUTTING EDGE |
* Basic Research Laboratory,
Laboratory of Comparative Carcinogenesis, and
Laboratory of Molecular Immunoregulation, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702;
Basic Research Program, SAIC-Frederick, Frederick, MD 21702; and
¶
Vanderbilt University Medical Center, Nashville, TN 37232
Drm/Gremlin and Dan, two homologous secreted antagonists 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 1
(SDF-1) or fMLP. The inhibition of SDF-1-induced monocyte chemotaxis by Dan is not due to blocking the binding of SDF-1 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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