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Blood. 2012 Feb 16;119(7):1623-33. doi: 10.1182/blood-2011-10-384289. Epub 2011 Dec 15.

Regulation and function of the E-cadherin/catenin complex in cells of the monocyte-macrophage lineage and DCs.

Author information

1
Myeloid Cell Immunology Laboratory, Vrije Universiteit Brussel, Brussels, Belgium.

Abstract

E-cadherin is best characterized as adherens junction protein, which through homotypic interactions contributes to the maintenance of the epithelial barrier function. In epithelial cells, the cytoplasmic tail of E-cadherin forms a dynamic complex with catenins and regulates several intracellular signal transduction pathways, including Wnt/β-catenin, PI3K/Akt, Rho GTPase, and NF-κB signaling. Recent progress uncovered a novel and critical role for this adhesion molecule in mononuclear phagocyte functions. E-cadherin regulates the maturation and migration of Langerhans cells, and its ligation prevents the induction of a tolerogenic state in bone marrow-derived dendritic cells (DCs). In this respect, the functionality of β-catenin could be instrumental in determining the balance between immunogenicity and tolerogenicity of DCs in vitro and in vivo. Fusion of alternatively activated macrophages and osteoclasts is also E-cadherin-dependent. In addition, the E-cadherin ligands CD103 and KLRG1 are expressed on DC-, T-, and NK-cell subsets and contribute to their interaction with E-cadherin-expressing DCs and macrophages. Here we discuss the regulation, function, and implications of E-cadherin expression in these central orchestrators of the immune system.

PMID:
22174153
DOI:
10.1182/blood-2011-10-384289
[Indexed for MEDLINE]

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