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Journal of Biochemistry Advance Access published online on October 29, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp168
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

The third type III module of human fibronectin mediates cell adhesion and migration

Masanobu Obara*, Tetsushi Sakuma and Kazuyuki Fujikawa

Laboratory of Developmental Biology, Department of Biological Science, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashihiroshima, Hiroshima 739-8526, Japan

*To whom correspondence should be addressed: Masanobu Obara: Tel: +81 082 424 7442 Fax: +81 082 424 0734, E-mail: msobara{at}hiroshima-u.ac.jp

Received July 23, 2009; Accepted October 13, 2009


  Abstract

Fibronectin (FN) is a major extracellular matrix protein involved in various biological events. This study demonstrated that the third FN type III repeat (FnIII3) and several fragments containing the repeat promote cell spreading and migration of human dermal fibroblasts (HDFs), whereas the fourth repeat (FnIII4) did not. A variety of cell types also spread on FnIII3 in a cell-type specific manner, but not on FnIII4. Immunofluorescence assays revealed that FnIII3 induced the organization of focal contacts and stress fibers in HDFs. Cyclic [RGDFV] peptides with a D-Phe residue, which are selective inhibitors of cell adhesion to vitronectin, inhibited HDF spreading on FnIII3 equally with GRGDS, indicating little involvement of {alpha}V-integrins in FnIII3 spreading. An anti-β1 integrin mAb inhibited cell spreading on FnIII3 and FN. To our knowledge, this is the first demonstration that a novel domain of FnIII3 functions in cell spreading and migration through an interaction with unresolved β1 integrin(s) in an RGD-dependent manner.

Key Words: cell adhesion, fibronectin, type III3 repeat, migration


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