The two endocytic pathways mediated by the carbohydrate recognition domain and regulated by the collagen-like domain of galectin-3 in vascular endothelial cells.

ABSTRACT: Galectin-3 plays an important role in endothelial morphogenesis and angiogenesis. We investigated the endocytosis of galectin-3 in human vascular endothelial cells and showed that galectin-3 could associate with and internalized into the cells in a carbohydrate-dependent manner. Our work also revealed that galectin-3 was transported to the early/recycling endosomes and then partitioned into two routes - recycling back to the plasma membrane or targeting to the late endosomes/lysosomes. Various N- and C-terminal truncated forms of galectin-3 were constructed and compared with the full-length protein. These comparisons showed that the carbohydrate-recognition domain of galectin-3 was required for galectin-3 binding and endocytosis. The N-terminal half of the protein, which comprises the N-te

SUBMITTER: Gao X 

PROVIDER: S-EPMC3530513 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature