1-{(1Z)-1-[6-(4-Chloro­phen­oxy)hex­y­l­oxy]-1-(2,4-difluoro­phen­yl)prop-1-en-2-yl}-1H-1,2,4-triazol-4-ium nitrate

In the title compound, C23H25ClF2N3O2 +·NO3 −, the triazole ring makes dihedral angles of 60.9 (4) and 25.0 (3)° with the 6-chloro­phenyl and 2,4-difluoro­phenyl rings, respectively. The mol­ecule adopts a Z configuration about the C=C double bond. In the crystal, the cations and anions are linked by N—H⋯O hydrogen bonds and weak C—H⋯O inter­actions

3,4-Dihy­droxy­phenethyl acetate

In the title compound, C10H12O4, the dihedral angle between the acetate group and the aromatic ring is 20.47 (10)°. In the crystal, mol­ecules are linked by O—H⋯O hydrogen bonds, forming [001] chains. Weak C—H⋯O inter­actions consolidate the packing

(4S,5S)-2-(3-Methoxy­phen­yl)-1,3-dioxolane-4,5-dicarboxamide

In the title compound, C12H14N2O5, the five-membered ring adopts an envelope conformation. In the crystal structure, inter­molecular N—H⋯O inter­actions link the mol­ecules into a three-dimensional network. A weak C—H⋯π inter­action is also found

The splice variant Ehm2/1 in breast cancer MCF-7 cells interacted with β--catenin and increased its localization to plasma membrane

Ehm2, which belongs to the FERM superfamily, is a metastasis-associated protein. However, its function in cancer metastasis and the associated molecular mechanism is not definitely clear. Alternative splicing is an important biological step during mRNA processing and has been reported to be related with many diseases including cancers. Ehm2 has two transcript variants. Transcript variant 1(Ehm2/1) encodes isoform 1 of 518 amino acids, while transcript variant 2(Ehm2/2) encodes isoform 2 of 913 amino acids. In this study, we found that Ehm2/1 was the main transcript variant in the MCF-7 breast cancer cell line. Forced expression of Ehm2/1 upregulated the total protein amount but had no effect on the mRNA levels of β-catenin. The increased β-catenin was found to be dominantly located at the cell membrane. Meanwhile, knockdown of Ehm2/1 in MCF-7 cells decreased the total protein amount but not the mRNA levels of β-catenin. Further results showed that Ehm2/1 interacted with β-catenin and colocalized with it at the cell membrane. E-cadherin, a partner of β-catenin in cadherin-catenin complexes, was also upregulated by the overexpression of Ehm2/1 and also colocalized with it at the cell membrane. Meanwhile, overexpression of Ehm2/1 inhibited the migration ability of MCF-7 cells. These results suggested that Ehm2/1 may render β-catenin at the cell membrane by interacting with β-catenin and E-cadherin

Implications for Tumor Microenvironment and Epithelial Crosstalk in the Management of Gastrointestinal Cancers

Rapid advances in technology are revealing previously unknown organization, cooperation, and limitations within the population of nontumor cells surrounding the tumor epithelium known as the tumor microenvironment (TME). Nowhere are these findings more pertinent than in the gastrointestinal (GI) tract where exquisite cell specialization supports a complex microenvironmental niche characterized by rapid stemness-associated cell turnover, pathogen sensing, epithelial orchestration of immune signaling, and other facets that maintain the complex balance between homeostasis, inflammation, and disease. Here, we summarize and discuss select emerging concepts in the precancerous microenvironment, TME, and tumor epithelial-TME crosstalk as well as their implications for the management of GI cancers

1,2-Bis(4-methyl­phen­oxy)ethane

In the title compound, C16H18O2, the two aromatic rings are almost orthogonal, making a dihedral angle of 89.41 (2)°. There is a C—H⋯π contact between the methyl­ene group and the 4-methyl­phenyl ring. The molecule exhibits twofold symmetry.