Effects of Eriobotrya japonica (Lindl.) flower extracts on mercuric chloride-induced hepatotoxicity in rats

Mercury(II) is an important factor in hepatotoxicity that can enter the body through marine diets and amalgams.In the present study,the protective effect of the Eriobotrya japonica flower extract(EJFE) on HgCl 2-induced hepatotoxicity was investigated.Five mg/kg of mercuric chloride in drinking water was given to rats either with saline or EJFE(100 and 200 mg/kg as intraperitoneal(IP)) for 30 d.The mercury levels in different groups of liver tissues of the rats were measured with flameless atomic absorption spectroscopy(F-AAS).Also,mercury accumulation in the liver of the rats was modeled by using a parallel chemical kinetic model.The results showed that HgCl 2-induced oxidative damage led to a significant decrease in glutathione(GSH) and the total antioxidant capacity(TAC) levels,and to a significant increase in lipid peroxidation level.Accumulated mercury was 14.47% more in the livers of the stress groups than in those of the control groups(P<0.001),whereas the amount of Hg was adjusted to 13.49% and 13.93% in groups treated with 100 and 200 mg/kg of EJFE respectively,as compared with stress groups(P<0.001).HPLC analysis of EJFE revealed that hesperetin and gallic acid are the major antioxidants in EJFE.Results demonstrate that flowers of the Eriobotrya japonica cause a significant protection against HgCl 2 induced hepatotoxicity in all diagnostic parameters by strengthening the antioxidant defense mechanisms and they may have a therapeutic function in free radical mediated diseases.     

Effect of substrate miscut on the electron mobility in InSb（001） structures on Ge and Ge-on-insulator substrates

InSb epilayers and InSb/Al0.20In0.80Sb quantum wells were grown on Ge(001)substrates and Ge-on-insulator(GeOI)-on-Si(001)substrates by molecular beam epitaxy.Growth on both on-axis and 4°-off-axis substrate orientations was studied.Anti-phase domains were formed when InSb films were grown on on-axis substrates,but suppressed significantly by the use of 4°-off-axis substrates.Such off-axis substrates also reduced the densities of micro-twin defects and threading dislocations.The defect reduction resulted in an increase in the room-temperature electron mobility from 37,000 to 59,000 cm2/Vs in 4.0-lm-thick InSb epilayers and from 10,000 to20,000 cm2/Vs in 25-nm-thick InSb quantum wells on Ge(001)and GeOI-on-Si(001)substrates.     

Electrical conductivity retention and electrochemical activity of CSA doped graphene/gold nanoparticle@ polyaniline composites

This paper reports the synthesis of CTAB mediated CSA doped PANI and GN/GNP@ PANI composite nanofibers. The as synthesized composite nanofibers were examined by TEM, SEM, XRD, Raman spectroscopy; UV–visible diffused reflectance spectroscopy and TGA. The CTAB mediated CSA doped composite nanofibers showed 59% higher DC electrical conductivity at ambient temperature than that of PANI,which might be due to the enhancement in the mobility of the charge carriers and reduction in hopping distance in the composite system. The CTAB mediated CSA doped composite nanofibers compared to PANI was observed to be showing enhanced DC electrical conductivity retention after various cycles of heating, suggesting an enhancement in thermal stability of the composite structure, which could be attributed to the synergistic effect of GN,GNP and PANI. Additionally, the composite nanofibers showed greater electrochemical activity and better capacitive performance and reduced optical bandgap than that of PANI.     

Tumor suppressor C-RASSF proteins

Human genome has ten genes that are collectedly called Ras association domain family (RASSF). RASSF is composed of two subclasses, C-RASSF and N-RASSF. Both N-RASSF and C-RASSF encode Ras association domain-containing proteins and are frequently suppressed by DNA hypermethylation in human cancers. However, C-RASSF and N-RASSF are quite different. Six C-RASSF proteins (RASSF1–6) are characterized by a C-terminal coiled-coil motif named Salvador/RASSF/Hippo domain, while four N-RASSF proteins (RASSF7–10) lack it. C-RASSF proteins interact with mammalian Ste20-like kinases—the core kinases of the tumor suppressor Hippo pathway—and cross-talk with this pathway. Some of them share the same interacting molecules such as MDM2 and exert the tumor suppressor role in similar manners. Nevertheless, each C-RASSF protein has distinct characters. In this review, we summarize our current knowledge of how C-RASSF proteins play tumor suppressor roles and discuss the similarities and differences among C-RASSF proteins.