| Information |
|---|
| catenin (cadherin-associated protein), beta 1, |
| InnateImmunity |
|
chr3 (+) (chr3:41216016-41256938) |
|
NM_001904
|
| 27 |
| 0 |
| 4 |
| 0 |
|
[ SNPper ]
[ GoldenPath ]
[ Gene Image ]
[ LocusLink ]
[ Omim ]
[ PubMed ]
|
|
ß-catenin a transcriptional coactivator, is part of the intracellular signal transduction pathways triggered by LPS in human macrophages, and appears to be involved in both LPS-induction of gene transcription and LPS-dependent regulation of vascular permeability. Exposure of alveolar macrophages to bacterial LPS results in the activation of a number of signal transduction pathways. An early event after the alveolar macrophage comes in contact with LPS is activation of PI 3-kinase and phosphorylation of Akt. In turn, Akt activation results in the phosphorylation-dependent inactivation of glycogen synthase kinase (GSK-3). Inactivation of GSK-3 reduces the ubiquitination of ß-catenin, resulting in nuclear accumulation and expression of genes that require nuclear ß-catenin for their activation. On the other hand, LPS induces actin reorganization, increased paracellular permeability, and endothelial cell detachment from the underlying extracellular matrix. Components of cell-cell (γ- and ß-catenin) and cell-matrix adherens junctions are cleaved by caspases activated during apoptosis. Cleavage of focal adhesion kinase leads to its dissociation from the focal adhesion-associated signaling protein, paxillin, resulting in reduced paxillin tyrosine phosphorylation. Therefore, endotoxin-induced disruption of endothelial monolayer integrity and survival signaling events is mediated, in part, through caspase cleavage of adherens junction proteins.
( See Omim for more ... ) |
