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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.

Authors: Chen, B  Blair, DG  Plisov, S  Vasiliev, G  Perantoni, AO  Chen, Q  Athanasiou, M  Wu, JY  Oppenheim, JJ  Yang, D 
Citation: Chen B, etal., J Immunol. 2004 Nov 15;173(10):5914-7.
Pubmed: (View Article at PubMed) PMID:15528323

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 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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CRRD Object Information
CRRD ID: 2303400
Created: 2009-02-11
Species: All species
Last Modified: 2009-02-11
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.