δ‐catenin overexpression promotes angiogenic potential of CWR22Rv‐1 prostate cancer cells via HIF‐1α and VEGF

He, Yongfeng; Kim, Hangun; Ryu, Taeyong; Kang, Youra; Kim, Jeong-Ae; Kim, Bo‐Hyun; Lee, Jae-Hyuk; Kang, Keon Wook; Lü, Qun; Kim, Kwonseop

doi:10.1016/j.febslet.2012.11.024

Cited by 13 publications

(10 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In our previously study, we found that δ-catenin induces E-cadherin processing and activates the δ-catenin signaling pathway in prostate cancer [23]. We also demonstrated that δ-catenin promotes angiogenesis through stabilizing HIF-1α to activate VEGF in the CWR22Rv-1 prostate cancer cell line [24]. These studies suggest the important role of δ-catenin in prostate cancer.…”

Section: Introductionmentioning

confidence: 79%

C-Src-mediated phosphorylation of δ-catenin increases its protein stability and the ability of inducing nuclear distribution of β-catenin

Kim

Ryu

et al. 2014

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Self Cite

View full text Add to dashboard Cite

Although δ-catenin was first considered as a brain specific protein, strong evidence of δ-catenin overexpression in various cancers, including prostate cancer, has been accumulated. Phosphorylation of δ-catenin by Akt and GSK3β has been studied in various cell lines. However, tyrosine phosphorylation of δ-catenin in prostate cancer cells remains unknown. In the current study, we demonstrated that Src kinase itself phosphorylates δ-catenin on its tyrosine residues in prostate cancer cells and further illustrated that Y1073, Y1112 and Y1176 of δ-catenin are predominant sites responsible for tyrosine phosphorylation mediated by c-Src. Apart from c-Src, other Src family kinases, including Fgr, Fyn and Lyn can also phosphorylate δ-catenin. We also found that c-Src-mediated Tyr-phosphorylation of δ-catenin increases its stability via decreasing its affinity to GSK3β and enhances its ability of inducing nuclear distribution ofβ-catenin through interrupting the integrity of the E-cadherin. Taken together, these results indicate c-Src can enhance the oncogenic function of δ-catenin in prostate cancer cells.

show abstract

Section: Introductionmentioning

confidence: 79%

C-Src-mediated phosphorylation of δ-catenin increases its protein stability and the ability of inducing nuclear distribution of β-catenin

Kim

Ryu

et al. 2014

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Self Cite

View full text Add to dashboard Cite

show abstract

“…δ-Catenin has also been implicated in the cell-cell interaction and signaling transduction in cancers including prostate (Burger et al, 2002;Lu et al, 2005;Lu et al, 2009), lung (Dai et al, 2011;Li et al, 2012;Zhang et al, 2010;Zhang et al, 2013b), ovarian (Fang et al, 2012), brain and colorectal tumors (Zhang et al, 2013a). Our previously published data shows that δ-catenin promotes angiogenesis through the stabilization of HIF-1α, activating VEGF in the CWR22Rv-1 prostate cancer cell line (He et al, 2013). We have also demonstrated that δ-catenin promotes E-cadherin processing, resulting in the activation of β-catenin-mediated oncogenic signals (Kim et al, 2012).…”

Section: Introductionmentioning

confidence: 90%

Investigation of the molecular mechanism of δ-catenin ubiquitination: Implication of β-TrCP-1 as a potential E3 ligase

Shrestha

Yuan

et al. 2016

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Self Cite

View full text Add to dashboard Cite

Ubiquitination, a post-translational modification, involves the covalent attachment of ubiquitin to the target protein. The ubiquitin-proteasome pathway and the endosome-lysosome pathway control the degradation of the majority of eukaryotic proteins. Our previous study illustrated that δ-catenin ubiquitination occurs in a glycogen synthase kinase-3 (GSK-3) phosphorylation-dependent manner. However, the molecular mechanism of δ-catenin ubiquitination is still unknown. Here, we show that the lysine residues required for ubiquitination are located mainly in the C-terminal portion of δ-catenin. In addition, we provide evidence that β-TrCP-1 interacts with δ-catenin and functions as an E3 ligase, mediating δ-catenin ubiquitin-proteasome degradation. Furthermore, we prove that both the ubiquitin-proteasome pathway and the lysosome degradation pathway are involved in δ-catenin degradation. Our novel findings on the mechanism of δ-catenin ubiquitination will add a new perspective to δ-catenin degradation and the effects of δ-catenin on E-cadherin involved in epithelial cell-cell adhesion, which is implicated in prostate cancer progression.

show abstract

“…It is interesting to note that the mechanism of hypoxic regulation is realized usually through transcription factor HIF, but there are many different factors which control the level of this transcription factor in low oxygen conditions as well as in malignant tumors under normoxic conditions [25,[28][29][30][31][32][33][34]. Hypoxia-inducible mir-210, transglutaminase, deltacatenin, c-Myc as well as ATR (ataxia telangiectasia and Rad3 related protein), which is a member of the phosphoinositide 3-kinase-related kinases family, are among them.…”

Section: Resultsmentioning

confidence: 99%

Expression of phosphoribosyl pyrophosphate synthetase genes in U87 glioma cells with ERN1 knockdown: effect of hypoxia and endoplasmic reticulum stress

Minchenko¹,

Garmash²,

Kovalevska³

et al. 2014

Ukr.Biochem.J.

View full text Add to dashboard Cite

Activation of pentose phosphate pathway is an important factor of enhanced cell proliferation and tumor growth. Phosphoribosyl pyrophosphate synthetase (PrPS) is a key enzyme of this pathway and plays a central role in the synthesis of purines and pyrimidines. Hypoxia as well as erN1 (from endoplasmic reticulum to nuclei-1) mediated endoplasmic reticulum stress response-signalling pathway is linked to the proliferation because the blockade of erN1 suppresses tumor growth, including glioma. We studied the expression of different PrPS genes in glioma cells with erN1 knockdown under hypoxic condition. It was shown that hypoxia decreases the expression of PrPS1 and PrPS2 genes in both types of glioma cells, being more pronounced in cells without erN1 function, but PrPSAP1 and PrPSAP2 gene expressions are suppressed by hypoxia only in glioma cells with blockade of erN1. Moreover, the blockade of endoribonuclease activity of erN1 does not affect the expression of PrPS1 and PrPS2 as well as PPrS-associated protein genes in U87 glioma cells. At the same time, the induction of endoplasmic reticulum stress by tunicamycin in glioma cells with suppressed activity of erN1 endoribonuclease decreases the expression level of PrPS1 and PrPS2 genes only. results of this investigation clearly demonstrated that the expression of different genes encoding subunits of PRPS enzyme is affected by hypoxia in U87 glioma cells, but the effect of hypoxia is modified by suppression of endoplasmic reticulum stress signaling enzyme erN1.

show abstract

δ‐catenin overexpression promotes angiogenic potential of CWR22Rv‐1 prostate cancer cells via HIF‐1α and VEGF

Cited by 13 publications

References 30 publications

C-Src-mediated phosphorylation of δ-catenin increases its protein stability and the ability of inducing nuclear distribution of β-catenin

C-Src-mediated phosphorylation of δ-catenin increases its protein stability and the ability of inducing nuclear distribution of β-catenin

Investigation of the molecular mechanism of δ-catenin ubiquitination: Implication of β-TrCP-1 as a potential E3 ligase

Expression of phosphoribosyl pyrophosphate synthetase genes in U87 glioma cells with ERN1 knockdown: effect of hypoxia and endoplasmic reticulum stress

Contact Info

Product

Resources

About