Chemical Research in Chinese Universities ›› 2010, Vol. 26 ›› Issue (4): 578-582.

• Articles • Previous Articles     Next Articles

Expression and Emmprin Regulated Function of Aquaporin1 in SMMC7221 Cells

LI Jiang2, ZHANG Ai-li1, TONG Qian3, ZHANG Jun-fang1, LI Hai-jing1, ZHAO Bing1, MA Tong-hui1 and LI Xiao-meng1*   

  1. 1. School of Life Sciences, Northeast Normal University, Changchun 130024, P. R. China;
    2. Dental Hospital, 3. Department of Cardiology, First Hospital, Jilin University, Changchun 130021, P. R. China
  • Received:2010-01-13 Revised:3020-03-26 Online:2010-07-25 Published:2010-10-01
  • Contact: LI Xiao-meng. E-mail: lixm441@nenu.edu.cn
  • Supported by:

    Supported by the National Natural Science Foundation of China(Nos.30871301, 30700827), the Fund of Ministry of Science and Technology of China(No.2010DFA31430), the Jilin Provincial Science & Technology Department, China(Nos.20070719, 20080731, 200905116) and the Analysis and Testing Foundation of Northeast Normal University, China(No.NENU-STC07005).

Abstract: Herein lie the crosstalk and regulation between AQP1 and Emmprin in SMMC7221 cells by means of siRNA technology and deglycosylation method. Firstly, HAQP1, rather than hAQP3, was selectively upregulated in SMMC7221 cells by FBS, flollowed by the upregulated expression of Emmprin. Emmprin gene silencing caused a remarkable change in the expression of AQP1 gene, just like its downstream gene, MMP9, meanwhile the water permeability and cell migration were also descended prominently. Furthermore, when treated with tunicamycin, Emmprin was deglycosylated, which made the expression of AQP1 significantly declined, followed by remarkably decreased cell membrane water permeability and cell migration. Taken together, all the data indicates the expression level and the modification of Emmprin by glycosylation are the key factors in regulating the expression of AQP1.

Key words: Aquaporin1, Emmprin, Cell migration