Application of enhancer of zeste homolog 2 immunocytochemistry to bile cytology

2021 ◽  
Author(s):  
Kiyoshi Tone ◽  
Sachiyo Ohno ◽  
Masatake Honda ◽  
Akifumi Notsu ◽  
Keiko Sasaki ◽  
...  
Keyword(s):  
Enhancer Of Zeste ◽  
Bile Cytology

Inhibition of enhancer of zeste homolog 2 prevents corneal myofibroblast transformation in vitro

2021 ◽  
pp. 108611
Author(s):  
Kai Liao ◽  
Zekai Cui ◽  
Yong Zeng ◽  
Jian Liu ◽  
Yini Wang ◽  
...  
Keyword(s):  
Enhancer Of Zeste

scholarly journals Enhancer of Zeste Homolog 2 Overexpression Has a Role in the Development of Anaplastic Thyroid Carcinomas

2011 ◽  
Vol 96 (4) ◽  
pp. 1029-1038 ◽  
Author(s):  
Eleonora Borbone ◽  
Giancarlo Troncone ◽  
Angelo Ferraro ◽  
Zuzana Jasencakova ◽  
Lovorka Stojic ◽  
...  
Keyword(s):  
Thyroid Carcinoma ◽  
Anaplastic Thyroid Carcinoma ◽  
Polycomb Group ◽  
Migration And Invasion ◽  
Polycomb Group Protein ◽  
Expression Levels ◽  
Thyroid Carcinomas ◽  
Enhancer Of Zeste ◽  
Pax8 Gene ◽  
Group Protein

Abstract Context: Enhancer of zeste homolog 2 (EZH2) is a histone lysine methyltransferase belonging to the polycomb group protein family. Overexpression of EZH2 has been found in several human malignancies including hematological and solid tumors. Objectives: In this study we investigated the expression levels of EZH2 and its polycomb group protein partners in thyroid carcinoma tissues with different degrees of malignancy to identify potential new therapeutic targets for anaplastic thyroid carcinoma (ATC). Results: We show that high EZH2 expression levels are characteristic of undifferentiated ATC, whereas no significant changes were observed in well-differentiated papillary and follicular thyroid carcinomas as compared with normal thyroid. Knockdown of EZH2 in ATC cell lines results in cell growth inhibition, loss of anchorage-independent growth, migration, and invasion properties. Moreover, we demonstrate that EZH2 directly controls differentiation of ATC cells by silencing the thyroid specific transcription factor paired-box gene 8 (PAX8). Conclusions: EZH2 is specifically overexpressed in ATC, and it directly contributes to transcriptional silencing of PAX8 gene and ATC differentiation.

High glucose-stimulated enhancer of zeste homolog-2 (EZH2) forces suppression of deptor to cause glomerular mesangial cell pathology

2021 ◽  
pp. 110072
Author(s):  
Falguni Das ◽  
Amit Bera ◽  
Nandini Ghosh-Choudhury ◽  
Kavitha Sataranatarajan ◽  
Amrita Kamat ◽  
...  
Keyword(s):  
High Glucose ◽  
Mesangial Cell ◽  
Glomerular Mesangial Cell ◽  
Enhancer Of Zeste

The Drosophila Polycomb-group gene Enhancer of zeste contains a region with sequence similarity to trithorax

1993 ◽  
Vol 13 (10) ◽  
pp. 6357-6366
Author(s):  
R S Jones ◽  
W M Gelbart
Keyword(s):  
Amino Acids ◽  
Sequence Similarity ◽  
Protein Product ◽  
Polycomb Group ◽  
Acute Leukemias ◽  
Trithorax Group ◽  
Acid Protein ◽  
Enhancer Of Zeste ◽  
Gene Enhancer ◽  
Carboxy Terminal

As is typical of Polycomb-group loci, the Enhancer of zeste [E(z)] gene negatively regulates the segment identity genes of the Antennapedia (ANT-C) and Bithorax (BX-C) gene complexes. A second class of loci, collectively known as the trithorax group, plays an antagonistic role as positive regulators of the ANT-C and BX-C genes. Molecular analysis of the E(z) gene predicts a 760-amino-acid protein product. A region of 116 amino acids near the E(z) carboxy terminus is 41.2% identical (68.4% similar) with a carboxy-terminal region of the trithorax protein. This portion of the trithorax protein is part of a larger region previously shown to share extensive homology with a human protein (ALL-1/Hrx) that is implicated in acute leukemias. Over this same 116 amino acids, E(z) and ALL-1/Hrx are 43.9% identical (68.4% similar). Otherwise, E(z) is not significantly similar to any previously described proteins. As this region of sequence similarity is shared by two proteins with antagonistic functions, we suggest that it may comprise a domain that interacts with a common target, either nucleic acid or protein. Opposite effects on transcription might then be determined by other portions of the two proteins.

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