E-cadherin on epithelial–mesenchymal transition in thyroid cancer

Abstract

Thyroid carcinoma is a common malignant tumor of endocrine system and head and neck. Recurrence, metastasis and high malignant expression after routine treatment are serious clinical problems, so it is of great significance to explore its mechanism and find action targets. Epithelial–mesenchymal transition (EMT) is associated with tumor malignancy and invasion. One key change in tumour EMT is low expression of E-cadherin. Therefore, this article reviews the expression of E-cadherin in thyroid cancers (TC), discuss the potential mechanisms involved, and outline opportunities to exploit E-cadherin on regulating the occurrence of EMT as a critical factor in cancer therapeutics.

The curcumin analogue PAC has potent anti-anaplastic thyroid cancer effects

“…3). It has been previously shown that modulation in the expression of E-cadherin affects the AMT process and the metastatic capacity of thyroid cancer cells 14 . Here, we have shown PAC-dependent E-cadherin upregulation and decrease in the migratory ability of TC cells, which could result from increased cell-cell adhesion property 15,16 .…”

Intramedullary Spinal Cord Metastases from Differentiated Thyroid Cancer, a Case Report

“…The ISCM-specific biochemical mechanism is not clearly known. As in other metastatic cancer models, it could involve membrane ligands, such as the TSH receptor [ 25 ], and extracellular matrix remodeling and degradation [ 26 , 27 ]. In particular, exosomal integrins and a compatible central nervous system microenvironment can drive metastatic cancer-specific trophism, including the central nervous system [ 28 , 29 ].…”

MACC1-induced migration in tumors: Current state and perspective

“…Previously, S100P was shown to affect myosin II, reduce the number of focal adhesions ( 206 ), interact with Cdc42 and Rac1 regulators, and affect cell migration via ezrin binding ( 207 ). In addition, ERK co-regulates E-cadherin ( 208 ) and was shown to be involved in protrusion formation via induction of actin polymerization at the leading edge ( 209 ). ERK was also suspected to be involved in FAK inactivation, regulation of RhoA and myosin II, downregulation of E-cadherin, and upregulation of N-cadherin and vimentin ( 197 , 209 , 210 ).…”

“…As discussed before, these molecules are involved in single-cell and collective migration, due to associations with cytoskeletal reorganization and cell–cell coupling. Likewise, MACC1 induced β-catenin expression and phosphorylation, an important signaling and adaptor protein in cell–cell junctions ( 169 , 180 , 203 , 215 – 217 ), negatively regulating E-cadherin ( 208 ). As mentioned earlier, MACC1 interacts with YWHAE which was shown to induce lower E-cadherin but higher N-cadherin and vimentin expression ( 186 ), being another explanation for the observed effects.…”