scholarly journals Epithelial–mesenchymal transition in tumor metastasis: a method to the madness

2009 ◽  
Vol 5 (8) ◽  
pp. 1109-1111 ◽  
Author(s):  
Venkateshwar G Keshamouni ◽  
William P Schiemann
Keyword(s):  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Mesenchymal Transition

scholarly journals Phosphorylation of Serine 11 and Serine 92 as New Positive Regulators of Human Snail1 Function: Potential Involvement of Casein Kinase-2 and the cAMP-activated Kinase Protein Kinase A

2010 ◽  
Vol 21 (2) ◽  
pp. 244-253 ◽  
Author(s):  
Matthew Reid MacPherson ◽  
Patricia Molina ◽  
Serhiy Souchelnytskyi ◽  
Christer Wernstedt ◽  
Jorge Martin-Pérez ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Cop9 Signalosome ◽  
Mesenchymal Transition ◽  
Depth Analysis ◽  
Positive Regulators

Snail1 is a major factor for epithelial-mesenchymal transition (EMT), an important event in tumor metastasis and in other pathologies. Snail1 is tightly regulated at transcriptional and posttranscriptional levels. Control of Snail1 protein stability and nuclear export by GSK3β phosphorylation is important for Snail1 functionality. Stabilization mechanisms independent of GSK3β have also been reported, including interaction with LOXL2 or regulation of the COP9 signalosome by inflammatory signals. To get further insights into the role of Snail1 phosphorylation, we have performed an in-depth analysis of in vivo human Snail1 phosphorylation combined with mutational studies. We identify new phosphorylation sites at serines 11, 82, and 92 and confirmed previously suggested phosphorylations at serine 104 and 107. Serines 11 and 92 participate in the control of Snail1 stability and positively regulate Snail1 repressive function and its interaction with mSin3A corepressor. Furthermore, serines 11 and 92 are required for Snail1-mediated EMT and cell viability, respectively. PKA and CK2 have been characterized as the main kinases responsible for in vitro Snail1 phosphorylation at serine 11 and 92, respectively. These results highlight serines 11 and 92 as new players in Snail1 regulation and suggest the participation of CK2 and PKA in the modulation of Snail1 functionality.

Carboxypeptidase E-ΔN promotes migration, invasiveness, and epithelial–mesenchymal transition of human osteosarcoma cells via the Wnt–β-catenin pathway

2019 ◽  
Vol 97 (4) ◽  
pp. 446-453 ◽  
Author(s):  
Shuli Fan ◽  
Xiang Gao ◽  
Peng Chen ◽  
Xu Li
Keyword(s):  
Cell Migration ◽  
Tumor Metastasis ◽  
Molecular Mechanisms ◽  
Epithelial Mesenchymal Transition ◽  
Mesenchymal Transition ◽  
Human Osteosarcoma ◽  
Carboxypeptidase E ◽  
Human Osteosarcoma Cells ◽  
Cancer Types ◽  
Interfering Rna

Osteosarcoma (OS) is the most common malignant bone tumor in children and adolescents, and metastatic OS is the major cause of OS-related death. Carboxypeptidase E (CPE) is known to be highly expressed in some cancer types, and its N-terminal truncated form, CPE-ΔN, is implicated in tumor metastasis and poor prognosis. In this study, we investigated the effect of CPE-ΔN on cell migration, invasiveness, and the epithelial–mesenchymal transition (EMT) of OS cells, and illustrated the molecular mechanisms. We first constructed CPE-ΔN overexpressing human OS cell lines (143B and U2OS cells), and found that ectopic CPE-ΔN expression in OS cells enhanced cell migration and invasiveness, and promoted the EMT process. Further, overexpression of CPE-ΔN increased the levels of c-myc and nuclear β-catenin in OS cells, which suggested the CPE-ΔN promotes activation of the Wnt–β-catenin pathway in OS cells. Treatment with β-catenin small interfering RNA (siRNA) inhibited the migration and invasiveness of CPE-ΔN-overexpressing cells, and reduced the expression of E-cadherin. Together, these results suggest that CPE-ΔN promotes migration, invasiveness, and the EMT of OS cells via the Wnt–β-catenin signaling pathway.

scholarly journals Peroxisome Proliferator-Activated Receptor-γ Activation Inhibits Tumor Metastasis by Antagonizing Smad3-Mediated Epithelial-Mesenchymal Transition

2010 ◽  
Vol 9 (12) ◽  
pp. 3221-3232 ◽  
Author(s):  
Ajaya Kumar Reka ◽  
Himabindu Kurapati ◽  
Venkata R. Narala ◽  
Guido Bommer ◽  
Jun Chen ◽  
...  
Keyword(s):  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Mesenchymal Transition

scholarly journals Epithelial-mesenchymal transition in tumor metastasis

2016 ◽  
Vol 11 (1) ◽  
pp. 28-39 ◽  
Author(s):  
Kay T. Yeung ◽  
Jing Yang
Keyword(s):  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Mesenchymal Transition

scholarly journals CHIP-mediated CIB1 ubiquitination regulated epithelial–mesenchymal transition and tumor metastasis in lung adenocarcinoma

2020 ◽  
Author(s):  
Yuanqi Liu ◽  
Yanwu Zhou ◽  
Pengfei Zhang ◽  
Xizhe Li ◽  
Chaojun Duan ◽  
...  
Keyword(s):  
Lung Adenocarcinoma ◽  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Clinicopathological Characteristics ◽  
Interacting Protein ◽  
Mesenchymal Transition ◽  
Normal Tissues ◽  
Ubiquitin E3 Ligase ◽  
And Migration

Abstract CIB1 is a homolog of calmodulin that regulates cell adhesion, migration, and differentiation. It has been considered as an oncogene in many tumor cells; however, its role in lung adenocarcinoma (LAC) has not been studied. In this study, the expression levels of CIB1 in LAC tissues and adjacent normal tissues were examined by immunohistochemistry, and the relationship between CIB1 expression and patient clinicopathological characteristics was analyzed. The effects of CIB1 on epithelial–mesenchymal transition (EMT), migration, and metastasis of LAC cells were determined in vitro and vivo. Proteins interacting with CIB1 were identified using electrospray mass spectrometry (LS-MS), and CHIP was selected in the following assays. Carboxyl-terminus of Hsp70-interacting protein (CHIP) is a ubiquitin E3 ligase. We show that CHIP can degrade CIB1 via promoting polyubiquitination of CIB1 and its subsequent proteasomal degradation. Besides, lysine residue 10 and 65 of CIB1 is the ubiquitinated site of CIB1. Furthermore, CHIP-mediated CIB1 downregulation is critical for the suppression of metastasis and migration of LAC. These results indicated that CHIP-mediated CIB1 ubiquitination could regulate epithelial–mesenchymal and tumor metastasis in LAC.

scholarly journals Protein 4.1B Suppresses Tumor Metastasis by Regulating Epithelial-mesenchymal Transition Progression in Melanoma Cells

2019 ◽  
Vol 16 (4) ◽  
pp. 529-536 ◽  
Author(s):  
Chengbo Wang ◽  
Keyan Li ◽  
Yingli Men ◽  
Cong Ding ◽  
Juan Du ◽  
...  
Keyword(s):  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Melanoma Cells ◽  
Mesenchymal Transition ◽  
Protein 4.1B

scholarly journals Matrix compliance regulates Rac1b localization, NADPH oxidase assembly, and epithelial–mesenchymal transition

2012 ◽  
Vol 23 (20) ◽  
pp. 4097-4108 ◽  
Author(s):  
KangAe Lee ◽  
Qike K. Chen ◽  
Cecillia Lui ◽  
Magdalena A. Cichon ◽  
Derek C. Radisky ◽  
...  
Keyword(s):  
Nadph Oxidase ◽  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Breast Tumors ◽  
Mammary Tissue ◽  
Human Breast ◽  
Mesenchymal Transition ◽  
Downstream Signaling ◽  
Rac Gtpases ◽  
Epithelial Plasticity

Epithelial–mesenchymal transition (EMT) is a form of epithelial plasticity implicated in fibrosis and tumor metastasis. Here we show that the mechanical rigidity of the microenvironment plays a pivotal role in the promotion of EMT by controlling the subcellular localization and downstream signaling of Rac GTPases. Soft substrata, with compliances comparable to that of normal mammary tissue, are protective against EMT, whereas stiffer substrata, with compliances characteristic of breast tumors, promote EMT. Rac1b, a highly activated splice variant of Rac1 found in tumors, localizes to the plasma membrane in cells cultured on stiff substrata or in collagen-rich regions of human breast tumors. At the membrane, Rac1b forms a complex with NADPH oxidase and promotes the production of reactive oxygen species, expression of Snail, and activation of the EMT program. In contrast, soft microenvironments inhibit the membrane localization of Rac1b and subsequent redox changes. These results reveal a novel mechanotransduction pathway in the regulation of epithelial plasticity via EMT.

scholarly journals ATG4A promotes tumor metastasis by inducing the epithelial-mesenchymal transition and stem-like properties in gastric cells

Oncotarget ◽  
2016 ◽  
Vol 7 (26) ◽  
pp. 39279-39292 ◽  
Author(s):  
Shi-Wei Yang ◽  
Yi-Fang Ping ◽  
Yu-Xing Jiang ◽  
Xiao Luo ◽  
Xia Zhang ◽  
...  
Keyword(s):  
Tumor Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Mesenchymal Transition ◽  
Gastric Cells
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