Restoring E-cadherin-mediated cell–cell adhesion increases PTEN protein level and stability in human breast carcinoma cells

Li, Zengxia; Wang, Liying; Zhang, Wen; Fu, Yi; Zhao, Hongbo; Ya-li, HU; Prins, Bram P.; Zha, Xiliang

doi:10.1016/j.bbrc.2007.08.154

Cited by 20 publications

(15 citation statements)

References 19 publications

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“…These results enhanced the hypothesis that PTEN and E-cadherin expression are associated, as previous suggested in human medicine (Fournier et al, 2009;Li et al, 2007). Simultaneous double immunofluorescence for PTEN and E-cadherin identified a co-localization of the two proteins within the same cell compartment in PTEN+/E-cadherin + group.…”

supporting

confidence: 81%

“…proposed that E-cadherin is necessary for PTEN expression, promoting its accumulation preventing its proteasome degradation (Li et al, 2007). However, other reports asserted that PTEN is necessary for E-cadherin expression and cell-to-cell adhesion, and not vice versa (Kotelevets et al 2001;Kotelevets et al, 2005).…”

Section: Accepted Manuscriptmentioning

confidence: 95%

“…Few reports have suggested the potential interaction between PTEN protein and Ecadherin in the regulation of the morphogenesis and the growth of healthy (Fournier et al, 2009) and neoplastic (Li et al, 2007) mammary cells. Data arising from these studies…”

Section: Accepted Manuscriptmentioning

confidence: 98%

“…For Fournier and colleagues (2009), cellular accumulation of PTEN is mediated by E-cadherin, and this up-regulation leads to the control or the arrest of acinar morphogenesis in mammary epithelial cells. In another article Li et al (2007) proposed that E-cadherin-mediated cell-tocell adhesion is necessary to prevent PTEN proteasome degradation and to promote its accumulation in human breast carcinoma cells. Other reports focused on PTEN influence on cellular junctions (Kotelevets et al 2001;Kotelevets et al, 2005), suggested that PTEN protein is essential for stabilizing cellular junctions, inhibiting the PI3K/AKT/mTOR pathway and preventing the E-to N-cadherin switch, which is a common event in melanoma and prostate cancer cells (Kotelevets et al 2001).…”

mentioning

confidence: 98%

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Co-localization of PTEN and E-cadherin in canine mammary hyperplasias and benign and malignant mammary tumors

Asproni

Ressel

Millanta

et al. 2015

Research in Veterinary Science

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Fifty-four canine mammary lesions (15 hyperplasias, 7 adenomas and 32 carcinomas) were submitted to immunohistochemical analysis for the evaluation of PTEN and E-cadherin co-expression. Subjects bearing mammary carcinomas were also submitted to a 2-year follow-up study to compare immunohistochemical results with overall survival. All the hyperplastic samples stained positive for both markers, 100% of adenomas were positive for PTEN and 86% for E-cadherin, and 69% and 34% of carcinomas were positive for PTEN and E-cadherin, respectively. Statistical analysis showed a positive correlation between these two proteins both considering all (p b 0.01) or malignant tumors (p < 0.05). The female dogs bearing tumors positively-stained for both markers had a longer overall survival (p < 0.05) and absence of lymphatics invasion (p < 0.05). Simultaneous double immunofluorescence confirmed the co-localization of the two proteins in neoplastic cells. Results reported in this study confirm the tumor suppressor effect of these two molecules.

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supporting

confidence: 81%

Section: Accepted Manuscriptmentioning

confidence: 95%

Section: Accepted Manuscriptmentioning

confidence: 98%

mentioning

confidence: 98%

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Co-localization of PTEN and E-cadherin in canine mammary hyperplasias and benign and malignant mammary tumors

Asproni

Ressel

Millanta

et al. 2015

Research in Veterinary Science

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“…PTEN stability and activity is regulated by phosphorylation of the carboxyterminal tail and by interactions with specific binding partners (Leslie et al 2008). Of note PTEN protein levels are controlled by AJ association and PTEN in turn stabilizes AJs (Kotelevets et al 2005;Subauste et al 2005;Li et al 2007;Fournier et al 2009). Interestingly, a direct link between PTEN and ROCKI was shown in primary bone marrow macrophages, in which ROCKI was required for PTEN stabilization, phosphorylation, and activity (Vemula et al 2010).…”

Section: Contractile Actomyosin Networkmentioning

confidence: 99%

Phosphoinositides in Cell Architecture

Shewan

Eastburn²,

Mostov

2011

Cold Spring Harbor Perspectives in Biology

173

159

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Inositol phospholipids have been implicated in almost all aspects of cellular physiology including spatiotemporal regulation of cellular signaling, acquisition of cellular polarity, specification of membrane identity, cytoskeletal dynamics, and regulation of cellular adhesion, motility, and cytokinesis. In this review, we examine the critical role phosphoinositides play in these processes to execute the establishment and maintenance of cellular architecture. Epithelial tissues perform essential barrier and transport functions in almost all major organs. Key to their development and function is the establishment of epithelial cell polarity. We place a special emphasis on highlighting recent studies demonstrating phosphoinositide regulation of epithelial cell polarity and how individual cells use phosphoinositides to further organize into epithelial tissues.P hosphoinositides (PIs) are essential components of cellular membranes in eukaryotes. Though these specialized lipids comprise less than 1% of the cellular lipid cohort, they play key roles in many fundamental biological processes (Di Paolo and De Camilli 2006;Saarikangas et al. 2010). PIs possess such far ranging roles by serving as specialized membrane docking sites for effectors of numerous cellular signal transduction cascades. PIs also serve as precursors of lipid second messengers. They are concentrated on the cytosolic face of cellular membranes (Fig. 1A) and rapidly diffuse within the plane of the membrane. Reversible phosphorylation of the myo-inositol head group of phosphatidylinositol (PtdIns) at positions 3, 4, and 5 (Fig. 1B) gives rise to the seven PI isoforms identified in eukaryotic cells. PtdIns(4)P and PtdIns(4,5)P 2 are constitutively present in membranes and comprise the largest pool of cellular PIs, whereas PtdIns(3,4,5)P 3 is essentially undetectable in most types of unstimulated cells (Lemmon and Ferguson 2000;Saarikangas et al. 2010).The spatiotemporally regulated production and turnover of phosphoinositides is crucial for localized PI signaling and function. Numerous phosphatidylinositol kinases and phosphatases are involved in regulating the metabolism of the various PI isoforms (Fig. 1)

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PRL PTPs: mediators and markers of cancer progression

Bessette

Qiu

Pallen

2008

Cancer Metastasis Rev

179

218

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Aberrant protein tyrosine phosphorylation resulting from the altered activity of protein tyrosine phosphatases (PTPs) is increasingly being implicated in the genesis and progression of human cancer. Accumulating evidence indicates that the dysregulated expression of members of the phosphatase of regenerating liver (PRL) subgroup of PTPs is linked to these processes. Enhanced expression of the PRLs, notably PRL-1 and PRL-3, promotes the acquisition of cellular properties that confer tumorigenic and metastatic abilities. Up-regulation of PRL-3 is associated with the progression and eventual metastasis of several types of human cancer. Indeed, PRL-3 shows promise as a biomarker and prognostic indicator in colorectal, breast, and gastric cancers. However, the substrates and molecular mechanisms of action of the PRLs have remained elusive. Recent findings indicate that PRLs may function in regulating cell adhesion structures to effect epithelial-mesenchymal transition. The identification of PRL substrates is key to understanding their roles in cancer progression and exploiting their potential as exciting new therapeutic targets for cancer treatment.

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Restoring E-cadherin-mediated cell–cell adhesion increases PTEN protein level and stability in human breast carcinoma cells

Cited by 20 publications

References 19 publications

Co-localization of PTEN and E-cadherin in canine mammary hyperplasias and benign and malignant mammary tumors

Co-localization of PTEN and E-cadherin in canine mammary hyperplasias and benign and malignant mammary tumors

Phosphoinositides in Cell Architecture

PRL PTPs: mediators and markers of cancer progression

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