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

Bo Chen, Donald G. Blair, Sergei Plisov, Gennady Vasiliev, Alan O. Perantoni, Qian Chen, Meropi Athanasiou, Jane Y. Wu, Joost J. Oppenheim, De Yang*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

Abstract

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 1α (SDF-1α) or fMLP. The inhibition of SDF-1α-induced monocyte chemotaxis by Dan is not due to blocking the binding of SDF-1α 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.

Original languageEnglish (US)
Pages (from-to)5914-5917
Number of pages4
JournalJournal of Immunology
Volume173
Issue number10
DOIs
StatePublished - Nov 15 2004

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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