Emodin inhibits proliferation and invasion, and induces apoptosis in human esophageal cancer cell line ECA109

Purpose: To determine the anticancer effects of emodin in human esophageal carcinoma cell line ECA109.Methods: Cell viability was determined by MTT assay, while cell invasion and apoptosis were measured by Transwell assay and flow cytometry, respectively. Expression levels of MMP-2, Bax, Bcl-2 and caspase-3 proteins were determined by Western blot.Results: Flow cytometry data showed that the proportion of apoptotic cells was increased by emodin treatment. Apoptotic rates produced by 10, 20 and 50 μM emodin were 13.9 ± 3.8, 25.6 ± 6.2 and 39.8 ± 7.7 %, respectively. Transwell assay data revealed concentration-dependent suppression of the invasive rate of ECA109 cells by emodin (10, 20 and 50 μM) was 30.0 ± 4.5, 56.0 ± 6.8 and 69.0 ± 8.1 %, respectively. Furthermore, emodin treatment inhibited expressions of MMP-2 and Bcl-2 proteins, but induced the expression of Bax and caspase-3, when compared with control groups.Conclusion: These results suggest that emodin inhibits cell proliferation and cell invasion, but induces cell apoptosis in human esophageal cancer cell line ECA109. Thus, emodin is a potential candidate for development of an effective chemotherapeutic agent against esophageal cancer.Keywords: Emodin, Esophageal Cancer, Apoptosis, Cell invasion, Bax, Caspase-

1,8-Bis(4-fluoro­phen­yl)naphthalene

In the title compound, C22H14F2, the two benzene rings are oriented with respect to the naphthalene ring system at 67.76 (8) and 67.50 (8)°, and the two benzene rings are twisted with respect to each other at 18.95 (10)°. Weak inter­molecular C—H⋯π inter­actions are present in the crystal structure

Flemingia macrophylla Extract Ameliorates Experimental Osteoporosis in Ovariectomized Rats

Flemingia macrophylla (Leguminosae), a native plant of Taiwan, is used as folk medicine. An in vitro study showed that a 75% ethanolic extract of F. macrophylla (FME) inhibited osteoclast differentiation of cultured rat bone marrow cells, and the active component, lespedezaflavanone A (LDF-A), was isolated. It was found that oral administration of FME for 13 weeks suppressed bone loss in ovariectomized rats, an experimental model of osteoporosis. In addition, FME decreased urinary deoxypyridinoline concentrations but did not inhibit serum alkaline phosphatase activities, indicating that it ameliorated bone loss via inhibition of bone resorption. These results suggest that FME may represent a useful remedy for the treatment of bone resorption diseases, such as osteoporosis. In addition, LDF-A could be used as a marker compound to control the quality of FME

Microbial production of lipopeptides as biosurfactants for varied applications

Biosurfactants have excellent surface active properties and strong antimicrobial activities making them suitable candidates for applications in varied industries such as personal care, foods, animal feeds and agriculture. However, the high production cost severely limits their industrial applications. Hence, screening high titre of biosurfactant-producing strains and improving them via whole cell mutagenesis or metabolic engineering are crucial to make them commercially attractive. Bacillus subtilis CX1-2 was isolated, which is able to produce surfactin at 1.2 g/L. The surfactant production was improved by 30% by whole cell mutagenesis induced by the atmospheric room temperature plasma (ARTP). Anti-microbial studies showed that Bacillus subtilis CX 1-2 has inhibitory activity against Rhizobium radiobacter, a pathogen that causes food spoilage in a large number of products. The emulsification study indicated that the biosurfactant produced by Bacillus subtilis CX 1-2 has much better performance than commercial emulsifiers used in foods such as phosphatidylcholine from egg yolk. Bacillus subtilis 22.2 was isolated, which produces surfactin as the major product with small amount of fengycin. Preliminary experiments showed that this strain is able to tolerate 40 g/L of sodium surfactin. Whole cell mutagenesis and metabolic engineering of the isolates based on CRISPR/Cas9 are ongoing to improve the biosurfactant production

Matriptase cleaves EpCAM and TROP2 in keratinocytes, destabilizing both proteins and associated claudins

The homologs EpCAM and TROP2, which both interact with claudin-1 and claudin-7, are frequently coexpressed in epithelia including skin. Intestine uniquely expresses high levels of EpCAM but not TROP2. We previously identified EpCAM as a substrate of the membrane-anchored protease matriptase and linked HAI-2, matriptase, EpCAM and claudin-7 in a pathway that is pivotal for intestinal epithelial cells (IEC) homeostasis. Herein, we reveal that TROP2 is also a matriptase substrate. Matriptase cleaved TROP2 when purified recombinant proteins were mixed in vitro. TROP2, like EpCAM, was also cleaved after co-transfection of matriptase in 293T cells. Neither EpCAM nor TROP2 cleavage was promoted by protease-disabled matriptase or matriptase that harbored the ichthyosis-associated G827R mutation. We confirmed that EpCAM and TROP2 are both expressed in skin and detected cleavage of these proteins in human keratinocytes (HaCaT cells) after the physiologic inhibition of matriptase by HAI proteins was relieved by siRNA knockdown. Knockdown of EpCAM or TROP2 individually had only small effects on claudin-1 and claudin-7 levels, whereas elimination of both markedly diminished claudin levels. HAI-1 knockdown promoted EpCAM and TROP2 cleavage accompanied by reductions in claudins, whereas HAI-2 knockdown had little impact. Double knockdown of HAI-1 and HAI-2 induced nearly complete cleavage of EpCAM and TROP2 and drastic reductions of claudins. These effects were eliminated by concurrent matriptase knockdown. Decreases in claudin levels were also diminished by the lysosomal inhibitor chloroquine and cleaved EpCAM/TROP2 fragments accumulated preferentially. We demonstrate that TROP2 and EpCAM exhibit redundancies with regard to regulation of claudin metabolism and that an HAI, matriptase, EpCAM and claudin pathway analogous to what we described in IECs exists in keratinocytes. This study may offer insights into the mechanistic basis for matriptase dysregulation-induced ichthyosis

3,3′-Dibenzyl-2,2′-dimethyl-1,1′-methyl­enediimidazolium dipicrate

In the title salt, C23H26N4 2+·2C6H2N3O7 −, the dihedral angle between the imidazolium rings in the dication is 69.9 (1)°. The aromatic ring of the benzyl group is almost perpendicular to the N-heterocyclic ring that is directly connected to it [dihedral angles = 83.2 (2) and 77.3 (3)°]

1-(4-Methyl­phenyl­diazo­nium­yl)-2-naphtholate

In the title compound, C17H14N2O, the dihedral angle between the benzene ring and naphthalene ring system is 11.0 (3)°. The azo group adopts an anti configuration and an intra­molecular N—H⋯O hydrogen bond exists. Mol­ecules are packed by π–π inter­actions between adjacent mol­ecule (closest approach between centroids of benzene and naphthalene rings of 3.501 Å)