CCN2/CTGF binds the small leucine rich proteoglycan protein Tsukushi

Kunimasa Ohta, Eriko Aoyama, Shah Adil Ishtiyaq Ahmad, Naofumi Ito, Mohammad Badrul Anam, Satoshi Kubota, Masaharu Takigawa

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


Extracellular molecules coordinate the multiple signaling pathways spatiotemporally to exchange information between cells during development. Understanding the regulation of these signal molecule-dependent pathways elucidates the mechanism of intercellular crosstalks. CCN2/CTGF is one of the CCN family members that binds BMP2, fibronectin, aggrecan, FGFR2 - regulating cartilage and bone formation, angiogenesis, wound repair etc. Tsukushi (TSK), which belongs to the Small Leucine-Rich Proteoglycan (SLRP) family, binds nodal/Vg1/TGF-β1, BMP4/chordin, Delta, FGF8, Frizzled4, and is involved in the early body formation, bone growth, wound healing, retinal stem cell regulation etc. These two secreted molecules are expressed in similar tissues and involved in several biological events by functioning as extracellular signaling modulators. Here, we examine the molecular interaction between CCN2 and TSK biochemically. Co-precipitation assay and Surface Plasmon Resonance measurement showed their direct binding with the Kd value 15.3 nM. Further, the Solid-phase Binding Assay indicated that TSK binds to IGFBP and CT domains of CCN2. Our data suggest that CCN2 and TSK exert their function together in the body formation.

Original languageEnglish
Pages (from-to)113-118
Number of pages6
JournalJournal of Cell Communication and Signaling
Issue number1
Publication statusPublished - Mar 1 2019


  • SLRP
  • Soluble molecule
  • Tsukushi
  • Vertebrate development

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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