Cell surface sialic acid inhibits Cx43 gap junction functions in constructed Hela cancer cells involving in sialylated N-cadherin推荐.pdfVIP

Mol Cell Biochem (2010) 344:241–251 DOI 10.1007/s11010-010-0548-9 Cell surface sialic acid inhibits Cx43 gap junction functions in constructed Hela cancer cells involving in sialylated N-cadherin Jing Li • Lei Cheng • Li-juan Wang • Hong-chun Liu • Li Li • Xiao-lu Wang • Mei-yu Geng Received: 27 January 2010 / Accepted: 23 July 2010 / Published online: 29 August 2010 Springer Science+Business Media, LLC. 2010 Abstract Numerous studies have shown that changes in underlies the intimate association between abnormal GJIC the glycan structures of cells correlate with tumorigenesis, and glycosylation on cancer development. however, a casual link between the altered glycan struc- tures and the abnormal GJIC in cancer cells is rarely Keywords Gap junction Cx43 Sialic acid studied. In this paper, we investigated the effects of sialic N-cadherin Cancer acid on the Cx43 gap junction functions, and clarified its potential mechanisms thereby. Sialidase significantly increased Cx43 gap junction functions in constructed Introduction Cx43-Hela cells along with down-regulation of cell surface sialic acid, which is dramatically reversed by sialidase Gap junctions are arrays of cell-to-cell channels that allow inhibitor NeuAc2en. Further study indicated that sialidase diffusion of small molecules between neighboring cells. failed to affect Cx43 at either protein or phosphorylation The individual channels are formed by the tetramembrane level, instead, it induced a considerable fraction of Triton spanning connexin (Cx) proteins [1, 2]. Cx43 is the first X-100 insoluble, as compared with the untreated cells. We identified connexin, the major connexin in myocardium also found that sialidase treatment reduced the N-cadherin and severa