作者: Deborah E. Britt , Dong-Fang Yang , Dong-Qin Yang , Donna Flanagan , Helen Callanan
DOI: 10.1016/J.YEXCR.2004.06.026
关键词:
摘要: Tight junctions (TJ) are multiprotein complexes that function to regulate paracellular transport of molecules through epithelial and endothelial cell layers. Many new tight junction-associated proteins have been identified in the past few years, their functional roles interactions just begun be elucidated. In this paper, we describe a novel protein LYsine-RIch CEACAM1 co-isolated (LYRIC) is widely expressed highly conserved between species. LYRIC has no domains would indicate does not appear member larger family. Data from analysis rat human tissue sections lines show colocalizes with junction ZO-1 occludin polarized cells, suggesting part complex. dissociates when junctional disrupted, as reform, relocalizes before LYRIC. These results suggest most likely structural component required for TJ formation, but rather recruited during maturation