δ-Catenin Affects the Localization and Stability of p120-Catenin by Competitively Interacting with E-Cadherin

Yang, Ilhwan; Chang, Ockyoung; Lü, Qun; Kim, Kwonseop

doi:10.1007/s10059-010-0030-2

Cited by 15 publications

(15 citation statements)

References 22 publications

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“…For example, we showed that polymorphisms in PAX6 and d-catenin (CTNND2) are associated with high-grade myopia 29,32,33,35 . PAX6 can directly control both CTNND2 and WNT7B expression 62,63 , and both molecular pathways can result in increased b-catenin nuclear translocation to activate Wnt signaling 64,65 . Independently, the CREAM consortium found that polymorphisms in RSPO1 and ZNRF3, which regulate Wnt signaling by controlling the turnover of Wnt receptors, were significantly associated with axial length 12,66 .…”

Section: Discussionmentioning

confidence: 99%

Identification of myopia-associated WNT7B polymorphisms provides insights into the mechanism underlying the development of myopia

et al. 2015

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Myopia can cause severe visual impairment. Here, we report a two-stage genome-wide association study for three myopia-related traits in 9,804 Japanese individuals, which was extended with trans-ethnic replication in 2,674 Chinese and 2,690 Caucasian individuals. We identify WNT7B as a novel susceptibility gene for axial length (rs10453441, P meta ¼ 3.9 Â 10 À 13 ) and corneal curvature (P meta ¼ 2.9 Â 10 À 40 ) and confirm the previously reported association between GJD2 and myopia. WNT7B significantly associates with extreme myopia in a case-control study with 1,478 Asian patients and 4,689 controls (odds ratio (OR) meta ¼ 1.13, P meta ¼ 0.011). We also find in a mouse model of myopia downregulation of WNT7B expression in the cornea and upregulation in the retina, suggesting its possible role in the development of myopia.

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Section: Discussionmentioning

confidence: 99%

Identification of myopia-associated WNT7B polymorphisms provides insights into the mechanism underlying the development of myopia

et al. 2015

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“…It would be interesting to compare the tumor growth rates and metastatic potentials of cells differentially expressing p120 and δ-catenin. Furthermore, our recent published data shows that p120 and δ-catenin compete with each other to interact with E-cadherin [53]. Therefore, future investigations are required to determine whether E-cadherin processing and/or endocytosis induced by p120 result in the same consequences as those induced by δ-catenin.…”

Section: Discussionmentioning

confidence: 99%

δ-Catenin promotes E-cadherin processing and activates β-catenin-mediated signaling: Implications on human prostate cancer progression

Kim

Yang

et al. 2012

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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δ-Catenin binds the juxtamembrane domain of E-cadherin and is known to be overexpressed in some human tumors. However, the functions of δ-catenin in epithelial cells and carcinomas remain elusive. We found that prostate cancer cells overexpressing δ-catenin show an increase in multi-layer growth in culture. In these cells, δ-catenin colocalizes with E-cadherin at the plasma membrane, and the E-cadherin processing is noticeably elevated. E-Cadherin processing induced by δ-catenin is serum-dependent and requires MMP- and PS-1/γ-secretase-mediated activities. A deletion mutant of δ-catenin that deprives the ability of δ-catenin to bind E-cadherin or to recruit PS-1 to E-cadherin totally abolishes the δ-catenin-induced E-cadherin processing and the multilayer growth of the cells. In addition, prostate cancer cells overexpressing δ-catenin display an elevated total β-catenin level and increase nuclear distribution, resulting in the activation of β-catenin/LEF-1-mediated transcription and their downstream target genes as well as androgen receptor-mediated transcription. Indeed, human prostate tumor xenograft in nude mice, which is derived from cells overexpressing δ-catenin, shows increased β-catenin nuclear localization and more rapid growth rates. Moreover, the metastatic xenograft tumor weights positively correlate with the level of 29 kD E-cadherin fragment, and primary human prostate tumor tissues also show elevated levels of δ-catenin expression and the E-cadherin processing. Taken together, these results suggest that δ-catenin plays an important role in prostate cancer progression through inducing E-cadherin processing and thereby activating β-catenin-mediated oncogenic signals.

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“…E-cadherin is a member of the cadherin family of Ca(2+)-dependent cell-cell adhesion molecules (26). It is a 120 kDa cell-cell adhesion molecule involved in the establishment of epithelial adherens junctions (27), and also is an important cell adhesion molecule that plays paramount roles in organ development and the maintenance of tissue integrity and normal epithelial cell phenotype (28).…”

Section: Discussionmentioning

confidence: 99%

E-cadherin and caveolin-1 alterations in the heart of rats having undergone chlorpromazine-induced toxicity

Huang

Liu

2011

Mol Med Report

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Abstract. Heart damage induced by chlorpromazine (CPZ) toxicity is associated with changes in the expression of various enzymes and proteins. This study aimed to investigate CPZ-induced alterations in cardiac E-cadherin and caveolin-1 (cav-1) after CPZ administration. Male Wistar rats were randomly divided into two groups: a control group and a CPZ group. The CPZ group was administered CPZ intraperitoneally at a single dose of 10 mg/kg for 21 days; the controls were given the same amount of saline via the same route. On Day 22, the rats were anesthetized, and a thoracotomy was performed in all animals. Immunohistochemical analysis was performed to evaluate protein expression of E-cadherin and cav-1. Sections were analyzed by digital image analysis. Results of the present study revealed that cardiac protein expression of E-cadherin and cav-1 was altered after CPZ-induced toxicity in the rat. The expression of E-cadherin was significantly reduced, while expression of cav-1 was significantly increased after CPZ treatment, as supported by integrated optical density analysis, compared with the control (P<0.05). The current findings indicate that such changes in the expression of E-cadherin and cav-1 may be reflected in abnormal cardiac function, and these proteins may be useful in revealing the mechanisms underlying CPZ-induced toxicity and may also provide additional insight for further research.

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δ-Catenin Affects the Localization and Stability of p120-Catenin by Competitively Interacting with E-Cadherin

Cited by 15 publications

References 22 publications

Identification of myopia-associated WNT7B polymorphisms provides insights into the mechanism underlying the development of myopia

Identification of myopia-associated WNT7B polymorphisms provides insights into the mechanism underlying the development of myopia

δ-Catenin promotes E-cadherin processing and activates β-catenin-mediated signaling: Implications on human prostate cancer progression

E-cadherin and caveolin-1 alterations in the heart of rats having undergone chlorpromazine-induced toxicity

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