@article{oai:kanazawa-u.repo.nii.ac.jp:00014077,
 author = {滝野, 隆久 and 中田, 光俊 and 堂本, 貴寛 and 川尻, 秀一 and 佐藤, 博 and Takino, Takahisa and Yoshimoto, Taisuke and Nakada, Mitsutoshi and Li, Zichen and Domoto, Takahiro and Kawashiri, Shuici and Sato, Hiroshi},
 issue = {2},
 journal = {Biochemical and Biophysical Research Communications},
 month = {Jul},
 note = {Fibronectin matrix formation requires the increased cytoskeletal tension generated by cadherin adhesions, and is suppressed by membrane-type 1 matrix metalloproteinase (MT1-MMP). In a co-culture of Rat1 fibroblasts and MT1-MMP-silenced HT1080 cells, fibronectin fibrils extended from Rat1 to cell-matrix adhesions in HT1080 cells, and N-cadherin adhesions were formed between Rat1 and HT1080 cells. In control HT1080 cells contacting with Rat1 fibroblasts, cell-matrix adhesions were formed in the side away from Rat1 fibroblasts, and fibronectin assembly and N-cadherin adhesions were not formed. The role of N-cadherin adhesions in fibronectin matrix formation was studied using MT1-MMP-silenced HT1080 cells. MT1-MMP knockdown promoted fibronectin matrix assembly and N-cadherin adhesions in HT1080 cells, which was abrogated by double knockdown with either integrin β1 or fibronectin. Conversely, inhibition of N-cadherin adhesions by its knockdown or treatment with its neutralizing antibody suppressed fibronectin matrix formation in MT1-MMP-silenced cells. These results demonstrate that fibronectin assembly initiated by MT1-MMP knockdown results in increase of N-cadherin adhesions, which are prerequisite for further fibronectin matrix formation. © 2014 Elsevier Inc. All rights reserved.},
 pages = {1016--1020},
 title = {Membrane-type 1 matrix metalloproteinase regulates fibronectin assembly and N-cadherin adhesion},
 volume = {450},
 year = {2014}
}