Loss of alpha-dystroglycan laminin binding in epithelium-derived cancers is caused by silencing of LARGE.

ABSTRACT: The interaction between epithelial cells and the extracellular matrix is crucial for tissue architecture and function and is compromised during cancer progression. Dystroglycan is a membrane receptor that mediates interactions between cells and basement membranes in various epithelia. In many epithelium-derived cancers, beta-dystroglycan is expressed, but alpha-dystroglycan is not detected. Here we report that alpha-dystroglycan is correctly expressed and trafficked to the cell membrane but lacks laminin binding as a result of the silencing of the like-acetylglucosaminyltransferase (LARGE) gene in a cohort of highly metastatic epithelial cell lines derived from breast, cervical, and lung cancers. Exogenous expression of LARGE in these cancer cells restores the normal glycosylation and lami

SUBMITTER: de Bernabe DB 

PROVIDER: S-EPMC2670132 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature