Membrane-type 1 matrix metalloproteinase regulates fibronectin assembly and N-cadherin adhesion
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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.
収録刊行物
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- Biochemical and Biophysical Research Communications
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Biochemical and Biophysical Research Communications 450 (2), 1016-1020, 2014-07-25
Academic Press
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詳細情報 詳細情報について
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- CRID
- 1390578283209922688
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- NII論文ID
- 120005478703
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- NII書誌ID
- AA11542044
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- ISSN
- 10902104
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- Web Site
- http://hdl.handle.net/2297/39702
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- IRDB
- CiNii Articles