A solar-thermal energy harvesting scheme: enhanced heat capacity of molten HITEC salt mixed with Sn/SiO(x) core-shell nanoparticles.

We demonstrated enhanced solar-thermal storage by releasing the latent heat of Sn/SiO(x) core-shell nanoparticles (NPs) embedded in a eutectic salt. The microstructures and chemical compositions of Sn/SiO(x) core-shell NPs were characterized. In situ heating XRD provides dynamic crystalline information about the Sn/SiO(x) core-shell NPs during cyclic heating processes.

Cardiotonic steroids attenuate ERK phosphorylation and generate cell cycle arrest to block human hepatoma cell growth.

Recent studies revealed the potential of Na(+)/K(+)-ATPase as a target for anticancer therapy and showed additional modes of action of cardiotonic steroids (CSs), a diverse family of naturally derived compounds, as inhibitors of Na(+)/K(+)-ATPase. The results from epidemiological studies showed significantly lower mortality rates in cancer patients receiving CSs, which sparked interest in the anticancer properties of these drugs. The present study was designed to investigate the anticancer effect of CSs (ouabain or cinobufagin) and to elucidate the molecular mechanisms of CS activity in hepatoma cell lines (HepG2 and SMMC-7721).

Targeting the Na(+)/K(+)-ATPase alpha1 subunit of hepatoma HepG2 cell line to induce apoptosis and cell cycle arresting.

Recent research has shown that the Na(+)/K(+)-ATPase alpha1 subunit is a novel anti-cancer target, which plays pivotal roles in malignant cell ion transport, metabolism, migration and signal transduction. The purpose of the present study was to investigate the anti-cancer effects of ouabain and Na(+)/K(+)-ATPase alpha1 small interfering ribonucleic acid (siRNA) on HepG2 cell proliferation, apoptosis and cell cycle, and to explore the molecular mechanisms. The expression of Na(+)/K(+)-ATPase alpha1 subunit in human hepatocellular carcinoma (HCC), normal liver tissues and human HCC line (HepG2, SMMC-7721 and Bel-7402) has been investigated.

[Effect of Na(+)/K(+)-ATPase alpha1 siRNA and ouabain upon cell cycle in human hepatoma HepG2 cell and its mechanism].

Objective: To investigate the in vitro anti-cancer effects of ouabain combined Na(+)/K(+)-ATPase alpha1 siRNA upon HepG2 cells and its molecular mechanism.

Methods: The Na(+)/K(+)-ATPase alpha1 subunit expressions of human hepatoma tissue, normal liver tissue and human hepatoma cell lines (HepG2, SMC7721 and Bel7402) were determined. The cells received different treatments (0.

[Analyzing anti-cancer action mechanisms of dihydroartemisinin using gene chip].

Objective: To understand the action mechanisms of artesunate on inhibiting leukaemia cell line K562 on the molecular level.

Method: The gene chip was used to detect the expression panel of genes of leukaemia cell line K562 treated by dihydroartemisinin. K562 cells were treated with 1 x 10(-5), 4 x 10(-5), 16 x 10(-5), 64 x 10(-5), 256 x 10(-5) mol x L(-1) dihydroartemisinin for 24 h, and then studied the modality changes by invert microscope.

[The role of ouabain in cell death of vascular endothelial cells ECV304 and the changes of expression of Na+, K(+)-ATPase alpha1, beta1-subunit].

Aim: To study the effect of Na+, K(+)-ATPase inhibition by ouabain on growth and death of vascular endothelial cells ECV304 and involved mechanisms.

Methods: Growth inhibition of ouabain on ECV304 cells was analyzed using MTT assay. The feature of cell death was studied by Hoechst 33342/PI staining, transmission electron microscopy and DNA agarose gel electrophoresis in ECV304 cells treated with ouabain.

[Inducement effect of 9-cis retinoic acid on cell cycle arrest and apoptosis of gastric carcinoma cell line MGC803 and its mechanism].

Background & Objective: Antitumor effect of 9-cis retinoic acid (9-cis RA) on gastric carcinoma is unclear yet. This study was to explore the inducement effect of 9-cis RA on cell cycle arrest and apoptosis of gastric carcinoma cell line MGC803 and its mechanism.

Methods: The expression of RXRalpha, Cyclin D1, and CDK4 in MGC803 cells was detected by reverse transcription-polymerase chain reaction (RT-PCR).