CCN2/CTGF binds the small leucine rich proteoglycan protein Tsukushi

Journal of Cell Communication and Signaling

article

Ohta, Kunimasa¹  Aoyama, Eriko⁵  Ahmad, Shah Adil Ishtiyaq¹  Ito, Naofumi¹  Anam, Mohammad Badrul¹  Kubota, Satoshi⁵  Takigawa, Masaharu⁵ 

[1] Department of Developmental Neurobiology, Graduate School of Life Sciences, Kumamoto University;Program for Leading Graduate Schools “HIGO Program”, Kumamoto University;Global COE Cell Fate Regulation Research and Education Unit, Kumamoto University;Japan Agency for Medical Research and Development (AMED);Advanced Research Center for Oral and Craniofacial Sciences, Okayama University Dental School/Graduate School of Medicine, and Pharmaceutical Sciences;Department of Biotechnology and Genetic Engineering, Mawlana Bhashani Science and Technology University

关键词: CCN2/CTGF;    Tsukushi;    Soluble molecule;    SLRP;    Vertebrate development;   

DOI  :  10.1007/s12079-018-0487-x

学科分类：分子生物学，细胞生物学和基因

来源: Springer

【 摘 要 】

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.

【 授权许可】

CC BY