TY - JOUR
T1 - CCN2/CTGF binds the small leucine rich proteoglycan protein Tsukushi
AU - Ohta, Kunimasa
AU - Aoyama, Eriko
AU - Ahmad, Shah Adil Ishtiyaq
AU - Ito, Naofumi
AU - Anam, Mohammad Badrul
AU - Kubota, Satoshi
AU - Takigawa, Masaharu
N1 - Funding Information:
The authors thank Mitsue Kumamaru and Megumi Takiguchi. We also thank all members of our labs for their technical assistance and for valuable helps. This study was supported by the Kumamoto University International Research Core for Stem Cell-based Developmental Medicine and HIGOprogram and in part by grants from the programs Grants-in-Aid for Scientific Research (B) to MT (#JP15H05014) and for Challenging Exploratory Research to MT (#JP17K19757) from Japan Society for the Promotion of Sciences, Japan.
Publisher Copyright:
© 2018, The International CCN Society.
PY - 2019/3/1
Y1 - 2019/3/1
N2 - 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.
AB - 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.
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U2 - 10.1007/s12079-018-0487-x
DO - 10.1007/s12079-018-0487-x
M3 - Article
AN - SCOPUS:85053666340
SN - 1873-9601
VL - 13
SP - 113
EP - 118
JO - Journal of Cell Communication and Signaling
JF - Journal of Cell Communication and Signaling
IS - 1
ER -