Antiadhesive Sites Present in the Fibronectin Type III-Like Repeats of Human Plasma Fibronectin

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  • Miura Shogo
    Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science
  • Kamiya Sadahiro
    Department of Clinical Sciences, Faculty of Pharmaceutical Sciences, Josai International University
  • Saito Yohei
    Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science
  • Wada Seiki
    Department of Clinical Sciences, Faculty of Pharmaceutical Sciences, Josai International University
  • Hayashi Ryo
    Department of Biochemistry, Faculty of Science and Engineering, Saga University
  • Taira Junichi
    Department of Biochemistry, Faculty of Science and Engineering, Saga University
  • Kodama Hiroaki
    Department of Biochemistry, Faculty of Science and Engineering, Saga University
  • Yajima Hirofumi
    Department of Applied Chemistry, Faculty of Science, Tokyo University of Science
  • Ueki Masaaki
    Department of Applied Chemistry, Faculty of Science, Tokyo University of Science
  • Fukai Fumio
    Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science

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  • Antiadhesive sites present in the fibronectin type 3-like repeats of human plasma fibronectin

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Abstract

We have found that fibronectin (FN) has a functional cryptic site opposing cell adhesion to extracellular matrix (ECM): a synthetic FN peptide derived from the 14th FN type III-like (FN-III) repeat, termed peptide FNIII14, inhibits cell adhesion to the FN without binding to β1 integrins. This antiadhesive activity of peptide FNIII14 depends on its C-terminal amino acid sequence YTIYVIAL. A 50-kDa membrane protein (p50) has been detected as a specific binding protein of peptide FNIII14. Here we showed that antiadhesive activity of peptide FNIII14 was depedent upon the presence of p50 on cell surfaces. Furthermore, we found that there exists a sequence, analogous to the YTIYVIAL, in the 10th FN-III repeat of the FN molecule and that a FN peptide containing this analogous sequence, termed peptide FNIII10, inhibited cell adhesion to the FN. Peptide FNIII10 appeared to share p50 with peptide FNIII14 in expressing the antiadhesive activity. As a physiological consequence of decreased adhesion, peptides FNIII10 and FNIII14 accelerated the anoikis-like apoptosis of normal fibroblasts by down-regulating Bcl-2 expression through blocking the FAK/PI3K/Akt signaling pathway. Thus, the YTIYVIAL-related sequences of the FN molecule may be involved in cell regulation by modulating negatively cell adhesion to the ECM, in which p50 probably serves as a membrane receptor.

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