Wnt3a binds to several sFRPs in the nanomolar range

Danuta Wawrzak, Mourad Metioui, Erik Willems, Marijke Hendrickx, Erwin De Genst, Luc Leyns

Research output: Contribution to journalArticlepeer-review

85 Citations (Scopus)

Abstract

Secreted Frizzled-related proteins (sFRPs) are modulators of the Wnt signaling pathway that plays important roles in both embryogenesis and oncogenesis. sFRPs have been proposed to antagonize Wnt activity by binding to Wnts. However, the affinity of this binding is unknown. Here we show, using surface plasmon resonance and purified proteins, that sFRP1, sFRP2, sFRP4, and Frzb bind directly to Wnt3a with affinities in the nanomolar range. However, only sFRP1 and sFRP2 antagonize Wnt3a activity by blocking Wnt3a induced beta-catenin accumulation in L cells. Furthermore, sFRP2, but not Frzb, antagonizes Wnt3a signaling in an ES cell model of mesoderm differentiation. These results provide the first measurement of binding affinity of sFRPs for a Wnt, which together with the measurement of antagonistic activity of sFRPs could help understand how sFRPs regulate Wnt signaling.
Original languageEnglish
Pages (from-to)1119-1123
Number of pages5
JournalBiochem Biophys Res Commun
Volume357
Issue number4
Publication statusPublished - 2007

Keywords

  • Wnt
  • Wnt antagonist
  • Frzb

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