Abstract |
p120-Catenin is the prototypic member of a subfamily of armadillo repeat domain proteins. Like its structural homologues, β- and γ- catenin, p120-catenin is an essential component of adherens junctions in endothelial cells and other polarized adherent cells. p120-Catenin binds directly to the cytoplasmic domain of cadherin and contributes to the regulation of cell-cell junctional integrity. Studies have demonstrated that p120-catenin plays important roles in cell-cell adhesion, embryonic development, cell proliferation and polarity, tumor cell migration, and cancer progression. However, recent insights have generated an entirely new perspective, suggesting that p120-catenin is implicated in the anti-inflammatory responses in the absence and presence of infection. This review summarizes the present knowledge and recent progress toward elucidating the novel role of p120-catenin in the regulation of innate immunity and inflammation.
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Authors | Guochang Hu |
Journal | Critical reviews in immunology
(Crit Rev Immunol)
Vol. 32
Issue 2
Pg. 127-38
( 2012)
ISSN: 1040-8401 [Print] United States |
PMID | 23216611
(Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't, Review)
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Chemical References |
- Armadillo Domain Proteins
- Catenins
- Desmosomal Cadherins
- Delta Catenin
- CTNND1 protein, human
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Topics |
- Adherens Junctions
- Animals
- Armadillo Domain Proteins
(immunology, metabolism)
- Catenins
(metabolism)
- Cell Adhesion
- Desmosomal Cadherins
(metabolism)
- Endothelial Cells
(immunology, metabolism)
- Humans
- Immunity, Innate
- Immunomodulation
- Inflammation
(metabolism)
- Delta Catenin
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