Cleavage and cell adhesion properties of human epithelial cell adhesion molecule (HEPCAM).

Abstract

During the generation of CRISPR-Cas9-mediated knock-out clones, the HCT-8 (rectum carcinoma) cell line was substituted for the FaDu (hypopharynx carcinoma) cell line. As a result, all of the data described in Figs. 6 and 7 represent results derived from cells of rectum carcinoma cell line HCT-8 and not FaDu cells. The conclusions drawn from results depicted in Figs. 6 and 7 have not been related to specific carcinoma entities, and the data are further substantiated by the use of siRNA and shRNA in esophageal carcinoma cell line Kyse30. The conclusions of the paper are not affected by this correction.

Study on the Selection of the Targets of Esophageal Carcinoma and Interventions of Ginsenosides Based on Network Pharmacology and Bioinformatics

“…By reviewing the study characteristics, the EpCAM gene contains 314 amino acids with a relative molecular weight of 40 kDa. Given today's resources, the characteristics of EpCAM that act as CSC markers can be considered [29,30]. It has been proved that CSC subpopulations can initiate cancer development, promote cancer metastasis and drug resistance, and even lead to recurrence of ESCA [31].…”

The Ca2+ mobilisation and the inhibition of akt reduced the binding of PEO-1 cells to fibronectin

“…The binding studies herein suggest that PEO-1 cells could be able to adhere to fibronectin in a dose dependent-manner and the maximum binding rate was reached after adhesion of cells to 50 μg/mL fibronectin. The binding capacity of PEO-1 cells was also measured in the presence or absence of calcium because integrin-mediated cell adhesion is regulated by extracellular Ca 2+ ions 24 , and an increased calcium concentration in the cytoplasm is essential for various signal transduction pathways such as proliferation and apoptosis and thus is also crucial in cancer. 25 TN induces endoplasmic stress by inhibiting glycosylation and leads to the accumulation of unfolded proteins.…”

EPCAMmutation update: Variants associated with congenital tufting enteropathy and Lynch syndrome

“…EpCAM has long been described as a cell adhesion molecule that mediates cell–cell interactions through homooligomerization (Balzar et al., ; Litvinov et al., ). In contrast, recent experiments have not been able to demonstrate EpCAM protein oligomerization in vitro and have not observed a role for EpCAM in the adhesion of carcinoma cell lines (Gaber et al., ; Tsaktanis et al., ). Additionally, EpCAM expression weakens cadherin‐mediated cell adhesion and promotes cell migration and cell invasion in a breast cancer cell line (Osta et al., ; Winter et al., ).…”

“…In normal tissues, human EpCAM is expressed on the surface of simple, pseudo‐stratified, and transitional epithelia in various tissues of the gastrointestinal tract, reproductive system, and respiratory tract. EpCAM has been implicated in a variety of important cellular functions including cell proliferation, migration, adhesion, differentiation, and cell signaling (Balzar et al., ; Litvinov et al., ; Trzpis, McLaughlin, de Leij, & Harmsen, ; Tsaktanis et al., ; Winter et al., ). EpCAM was first recognized as an antigen overexpressed on human carcinoma cells, including tumors of the gastrointestinal system, breast, thyroid, and kidney (Balzar, Winter, De Boer, & Litvinov, ).…”

“…In normal intestines, Claudin‐7 forms a stable protein complex with EpCAM, whereas CTE‐associated EPCAM mutations lead to instability of the EpCAM–Claudin‐7 interaction, decreasing its presence on the plasma membrane (Mueller, McGeough, Pena, & Sivagnanam, ). In addition to the critical role EpCAM plays in maintenance of the intestinal barrier, EpCAM has potent effects on cell proliferation and differentiation (Tsaktanis et al., ). EpCAM appears to play a role in morphogenesis and development of some tissues.…”