Journal
JOURNAL OF IMMUNOLOGY
Volume 173, Issue 10, Pages 5914-5917Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.173.10.5914
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Funding
- NCI NIH HHS [N01 CO 12400] Funding Source: Medline
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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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