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J Biol Chem. 2014 Apr 11;289(15):10510-7. doi: 10.1074/jbc.M113.538538. Epub 2014 Feb 24.

Galectin-3 regulates desmoglein-2 and intestinal epithelial intercellular adhesion.

Author information

1
From the Department of Pathology and Laboratory Medicine, Epithelial Pathobiology and Mucosal Inflammation Research Unit, Emory University, Atlanta, Georgia 30322 and.

Abstract

The desmosomal cadherins, desmogleins, and desmocollins mediate strong intercellular adhesion. Human intestinal epithelial cells express the desmoglein-2 isoform. A proteomic screen for Dsg2-associated proteins in intestinal epithelial cells identified a lectin referred to as galectin-3 (Gal3). Gal3 bound to N-linked β-galactosides in Dsg2 extracellular domain and co-sedimented with caveolin-1 in lipid rafts. Down-regulation of Gal3 protein or incubation with lactose, a galactose-containing disaccharide that competitively inhibits galectin binding to Dsg2, decreased intercellular adhesion in intestinal epithelial cells. In the absence of functional Gal3, Dsg2 protein was internalized from the plasma membrane and degraded in the proteasome. These results report a novel role of Gal3 in stabilizing a desmosomal cadherin and intercellular adhesion in intestinal epithelial cells.

KEYWORDS:

Cell-Cell Interaction; Desmoglein-2; Desmosome; Galectin; Galectin-3f; Intestinal Epithelium; Protein Stability

PMID:
24567334
PMCID:
PMC4036172
DOI:
10.1074/jbc.M113.538538
[Indexed for MEDLINE]
Free PMC Article
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