Regulation of N-cadherin-based cell–cell interaction by JSAP1

フォーマット:

論文

責任表示:

Bayarsaikhan, Munkhuu ; Takino, Takahisa ; Gantulga, Davaakhuu ; Yoshioka, Katsuji ; Sato, Hiroshi

言語:

英語

出版情報:

Elsevier, 2007-02-09

著者名:

• Bayarsaikhan, Munkhuu
• Takino, Takahisa
• Gantulga, Davaakhuu
• Yoshioka, Katsuji
• Sato, Hiroshi

掲載情報:

Biochemical and Biophysical Research Communications　

ISSN:

0006-291x      

巻:

353

通号:

2

開始ページ:

357

終了ページ:

362

バージョン:

author

概要:

金沢大学がん研究所がん分子細胞制御<br />金沢大学大学院医学系研究科<br />We previously reported that the level of c-Jun NH2-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1), a scaffold protein for JNK signaling, increases dra … matically during nerve growth factor (NGF)-induced differentiation of PC12h cells. In the present study, we investigated the function of JSAP1 during PC12h cell differentiation by knocking down the level of JSAP1. The depletion of JSAP1 caused NGF-treated PC12h cells to form aggregates and impaired their differentiation. The aggregation was not observed in JSAP1-depleted cells that were untreated or treated with epidermal growth factor. Immunocytochemical studies indicated that N-cadherin, but not E-cadherin, was localized to sites of cell–cell contact in the aggregated cells. Furthermore, an inhibitory anti-N-cadherin antibody completely blocked the aggregation. Taken together, these results suggest that JSAP1 regulates cell–cell interactions in PC12h cells specifically in the NGF-induced signaling pathway, and does so by modulating N-cadherin. 続きを見る

URL:

http://hdl.handle.net/2297/3640