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The C‐terminal region of NELL1 mediates osteoblastic cell adhesion through integrin α3β1
Author(s) -
Hasebe Ai,
Nakamura Yoko,
Tashima Hiroki,
Takahashi Kaneyoshi,
Iijima Masumi,
Yoshimoto Nobuo,
Ting Kang,
Kuroda Shun'ichi,
Niimi Tomoaki
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.014
Subject(s) - integrin , microbiology and biotechnology , cell adhesion , focal adhesion , extracellular matrix , cell adhesion molecule , chemistry , cell , signal transduction , biochemistry , biology
NELL1 is a secretory osteogenic protein containing several structural motifs that suggest that it functions as an extracellular matrix component. To determine the mechanisms underlying NELL1‐induced osteoblast differentiation, we examined the cell‐adhesive activity of NELL1 using a series of recombinant NELL1 proteins. We demonstrated that NELL1 promoted osteoblastic cell adhesion through at least three cell‐binding domains located in the C‐terminal region of NELL1. Adhesion of cells to NELL1 was strongly inhibited by function‐blocking antibodies against integrin α3 and β1 subunits, suggesting that osteoblastic cells adhered to NELL1 through integrin α3β1. Further, focal adhesion kinase activation is involved in NELL1 signaling.
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