Disease relevance of CTNNB1

• It is tempting to speculate that the Wnt-4-beta-catenin pathway contributes to the recovery from acute renal failure (ARF) [1].

High impact information on CTNNB1

• CONCLUSION: Our results indicate that the combination of vibration and HA activates the production of proteoglycan in 3-dimensional cultured chondrocytes and stimulates MAPK and beta-catenin [2].
• Since beta-catenin is a component of intact adherens junctions, but when liberated from destabilized contacts may act as a transcriptional co-activator, we investigated its role in TGF-beta 1-provoked EMT [3].
• Immunofluorescence analysis showed that beta-catenin and VE-cadherin staining changed from a uniform distribution along the membrane of control cells to a diffuse pattern for both proteins and finger-like projections for beta-catenin in neutrophil-exposed monolayers [4].
• Finally, beta-catenin and VE-cadherin from neutrophil-treated endothelial cells showed a significant increase in tyrosine phosphorylation [4].
• The endothelial adherens junction is formed by complexes of transmembrane adhesive proteins, of which beta-catenin is known to connect the junctional protein vascular endothelial (VE)-cadherin to the cytoskeleton and to play a signaling role in the regulation of junction-cytoskeleton interaction [4].

Biological context of CTNNB1

• Taken together, these data suggest that the Wnt-4-beta-catenin pathway plays a key role in the cell cycle progression of renal tubules in ARF [1].
• Lrp5, a known low-density receptor-related protein, plays an essential role in cellular proliferation and osteoblastogenesis via the beta-catenin signaling pathway [5].
• Atorvastatin reduced bone formation, cellular proliferation, and Lrp5/beta-catenin protein levels in the AVs [5].

Anatomical context of CTNNB1

• After 24 or 48 hours of shear, staining for VE-cadherin, alpha-catenin, and beta-catenin was intense and peripheral, forming a band of "dashes" (adherens plaques) that colocalized with the ends of stress fibers that inserted along the lateral membranes of cells [6].
• These data suggest that neutrophils may regulate endothelial barrier function through a process conferring conformational changes to beta-catenin and VE-cadherin [4].
• The relocation of beta-catenin and vinculin away from intercalated discs in failing myocytes may impair the mechanical linkage between N-cadherin and thin filaments and adversely affect myocyte shape [7].
• The AVs were examined for cellular proliferation, Lrp5/beta-catenin, and bone matrix markers [5].
• Focal adhesion kinase was tyrosine phosphorylated more by basolateral than by apical EGFR; however, beta-catenin was tyrosine phosphorylated to a much greater degree following the activation of mislocalized apical EGFR [8].

Associations of CTNNB1 with chemical compounds

• CONCLUSIONS: Hypercholesterolemic AV calcification is attenuated by atorvastatin and is mediated in part by the Lrp5/beta-catenin pathway [5].
• Dynein intermediate chain, alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptors, kainate receptors, N-cadherin, beta-catenin, N-ethylmaleimide-sensitive factor, an hsc70 protein, and actin reside on the surface of the PSD [9].
• Moreover, lithium increased inhibitory phosphorylation of GSK3, augmented nuclear translocation of beta-catenin in a dose- and time-dependent manner [10].
• Change in morphology of cells was monitored under microscopy, and expression of beta-catenin, phosphorylated GSK3 and involucrin, a squamous differentiation marker, were dectected by Western blotting, while expression of mRNA of another squamous differentiation marker, small proline-rich protein, was detected by RT-PCR [10].

Other interactions of CTNNB1

• Western blot analysis indicated that protein levels of VE-cadherin, alpha-catenin, and plakoglobin decreased, whereas beta-catenin levels increased after 8.5 hours of shear stress [6].

Analytical, diagnostic and therapeutic context of CTNNB1

• Smaller-molecular-weight fragments recognized by VE-cadherin and beta-catenin antibodies were also obtained from VE-cadherin immunoprecipitation, indicating degradation of endothelial cell adherens junctions [11].
• Immunoblotting of total lysates revealed an increase in smaller-molecular-weight fragments of VE-cadherin, beta-catenin, and gamma -catenin after post-CPB perfusion, indicating partial protein degradation [11].

References