Effects of Deposition Temperature on the Device Characteristics of Oxide Thin-Film Transistors Using In-Ga-Zn-O Active Channels Prepared by Atomic-Layer Deposition.

We demonstrated the physical and electrical properties of the In-Ga-Zn-O (IGZO) thin films prepared by atomic-layer deposition (ALD) method and investigated the effects of the ALD temperature. The film composition (atomic ratio of In:Ga:Zn) and film density were examined to be 1:1:3 and 5.9 g/cm3, respectively, for all the temperature conditions. The optical band gaps decreased from 3.81 to 3.21 eV when the ALD temperature increased from 130 to 170 °C. The amounts of oxygen-related defects such as oxygen vacancies increased with increasing the ALD temperature. It was found from the in situ temperature-dependent electrical conductivity measurements that the electronic natures including the defect structures and conduction mechanism of the IGZO thin films prepared at different temperatures showed marked variations. The carrier mobilities in the saturation regions (µsat's) for the fabricated thin film transistors (TFTs) using the IGZO channel layers were estimated to be 6.1 to 14.8 cm2 V-1 s-1 with increasing the ALD temperature from 130 to 170 °C. Among the devices, when the ALD temperature was controlled to be 150 °C, the IGZO TFTs showed the best performance, which resulted from the fact that the amounts of oxygen vacancies and interstitial defects could be appropriately modulated at this condition. Consequently, the µsat, subthreshold swing, and on/off ratio for the TFT using the IGZO channel prepared at 150 °C showed 10.4 cm2 V-1 s-1, 90 mV/dec, and 2 × 109, respectively. The threshold voltage shifts of this device could also be effectively reduced to be 0.6 and -3.2 V under the positive-bias and negative-bias-illumination stress conditions. These obtained characteristics can be comparable to those for the sputter-deposited IGZO TFTs.

Atomic-layer-deposition-assisted ZnO nanoparticles for oxide charge-trap memory thin-film transistors.

ZnO nanoparticles (NPs) with monolayer structures were prepared by atomic layer deposition (ALD) to use for a charge-trap layer (CTL) for nonvolatile memory thin-film transistors (MTFTs). The optimum ALD temperature of the NP formation was demonstrated to be 160 °C. The size and areal density of the ZnO NPs was estimated to be approximately 33 nm and 4.8 × 109 cm-2, respectively, when the number of ALD cycles was controlled to be 20. The fabricated MTFTs using a ZnO-NP CTL exhibited typical memory window properties, which are generated by charge-trap/de-trap processes, in their transfer characteristics and the width of the memory window (MW) increased from 0.6 to 18.0 V when the number of ALD cycles increased from 5 to 30. The program characteristics of the MTFT were markedly enhanced by the post-annealing process performed at 180 °C in an oxygen ambient due to the improvements in the interface and bulk qualities of the ZnO NPs. The program/erase (P/E) speed was estimated to be 10 ms at P/E voltages of -14 and 17 V. The memory margin showed no degradation with the lapse in retention time for 2 × 104 s and after the repetitive P/E operations of 7 × 103 cycles.

Inhibitory effect of zinc on hypoxic HIF-1 activation in astrocytes.

Hypoxia-inducible factor-1 (HIF-1) regulates the expression of neuroprotective genes such as erythropoietin (EPO). We investigated the mechanism by which zinc, an excitotoxin-like metal, regulates HIF-1 under hypoxic conditions in astrocytes. In hypoxic LN215 cells, HIF-1alpha stabilized and accumulated in the nucleus, resulting in an increase in its DNA-binding activity to the EPO enhancer. Zinc inhibited hypoxia-induced increases in HIF-1 DNA-binding activity and the HIF-1-dependent mRNA expression of EPO. Zinc did not affect hypoxic stabilization of HIF-1alpha. Nuclear migration of HIF-1alpha upon hypoxia was reduced by zinc. Complete blockade of hypoxia-induced assembly of HIF-1alpha-HIF-1beta complex was observed after treatment of zinc. These findings suggest that zinc hampers hypoxia-stimulated HIF-1 activation in astrocytes by inhibiting nuclear HIF-1alpha translocation and subsequently disrupting HIF-1 heterodimerization.

Heparin Attenuates the Expression of TNFalpha-induced Cerebral Endothelial Cell Adhesion Molecule.

Heparin is a well-known anticoagulant widely used in various clinical settings. Interestingly, recent studies have indicated that heparin also has anti-inflammatory effects on neuroinflammation-related diseases, such as Alzheimer's disease and meningitis. However, the underlying mechanism of its actions remains unclear. In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses. Heparin selectively interfered with NF-kappaB DNA-binding activity in the nucleus, which is stimulated by TNFalpha. In addition, non-anticoagulant 2,3-O desulfated heparin (ODS) prevented NF-kappaB activation by TNFalpha, suggesting that the anti-inflammatory mechanism of heparin action in CECs lies in heparin's ability to inhibit the expression of cell adhesion molecules, as opposed to its anticoagulant actions.

Lithospermic acid B ameliorates the development of diabetic nephropathy in OLETF rats.

Lithospermic acid B (LAB), an active component isolated from Salvia miltiorrhizae, has been reported to have renoprotective effects in type 1 diabetic animal models. In the present study we investigated the effects of LAB on the prevention of diabetic nephropathy in type 2 diabetic Otsuka Long-Evans-Tokushima Fatty (OLETF) rats. LAB (20 mg/kg) was given orally once daily to 10-week-old male OLETF rats for 28 weeks. Treatment of OLETF rats with LAB had little effects on body weight and blood glucose levels. Treatment with LAB resulted in significant reduction in blood pressure. LAB markedly attenuated albuminuria and significantly lowered levels of lipid peroxidation, monocyte chemoattractant protein-1 (MCP-1), and transforming growth factor-beta (TGF-beta1) expression in renal tissues of OLETF rats. In addition, LAB inhibited the progression of glomerular hypertrophy, mesangial expansion, and expansion of the extracellular matrix in the renal cortex. Collectively, these results suggest that LAB has beneficial effects on the diabetic nephropathy in OLETF rats by decreasing blood pressure, oxidative stress, and MCP-1 expression. Our results suggest that LAB might be a new therapeutic agent for the prevention of nephropathy in type 2 diabetes.

Heparin inhibits NF-kappaB activation and increases cell death in cerebral endothelial cells after oxygen-glucose deprivation.

Heparin is a classic anticoagulant that is commonly used in the treatment of acute ischemic stroke (AIS). Its use remains controversial, however, due to the risk of cerebral hemorrhagic transformation. In addition to anticoagulant effects, diverse effects on transcription factors can be caused by heparin. Among the transcription factors potentially affected is nuclear factor kappa B (NF-kappaB), a protein that is reportedly related to the survival of cerebral endothelial cells. We investigated the effect of heparin on NF-kappaB activation and cell death following oxygen-glucose deprivation (OGD), an experimental model of AIS. We subjected bEnd.3 cells from a murine cerebral microvascular endothelial cell line to OGD. We examined the effect of heparin on OGD-induced NF-kappaB activation and its mechanism of action, using electrophoretic mobility shift assays, reporter gene analysis, real-time RT-PCR, Western blot analysis, and confocal microscopy. We also measured the effect of heparin on OGD-induced cell death using an MTT assay. Heparin inhibited both tumor necrosis factor alpha- and OGD-induced NF-kappaB activation. Heparin was taken up by endocytosis and then entered the nucleus. Heparin did not affect the nuclear translocation of NF-kappaB, but instead inhibited the DNA binding of NF-kappaB in the nucleus. Cells were more susceptible to OGD-induced cell death after heparin treatment. Besides producing an anticoagulation effect, heparin also inhibits NF-kappaB activation, resulting in increased susceptibility to OGD-induced cell death. This effect may be responsible for hemorrhagic transformation in patients following heparin treatment for AIS.