Aluminum doped zinc oxide (AZO) films are prepared by rf magnetron sputtering on glass or Si substrates using specifically designed ZnO targets containing different amount of Al2O3 powder as the Al doping source. The structural, electrical, and optical properties of the AZO films are investigated in terms of the preparation conditions, such as the Al2O3 content in the target, rf power, substrate temperature and working pressure. The crystal structure of the AZO films is hexagonal wurtzite. The orientation, regardless of the Al content, is along the c axis perpendicular to the substrate. The doping concentration in the film is 1.9 at. % for 1 wt % Al2O3 target, 4.0 at. % for 3 wt % Al2O3 target, and 6.2 at. % for 5 wt % Al2O3 target. The resistivity of the AZO film prepared with the 3 wt % Al2O3target is ∼4.7×10−4 Ω cm, and depends mainly on the carrier concentration. The optical transmittance of a 1500-Å-thick film at 550 nm is ∼90%. The optical band gap depends on the Al doping level and on the microstructure of the films, and is in the range of 3.46–3.54 eV. The optical band gap widening is proportional to the one-third power of the carrier concentration.

SU11248 is a highly effective tyrosine kinase inhibitor of the RET/PTC oncogenic kinase.

No abstract

Small heterodimer partner (SHP; NR0B2) is an atypical orphan nuclear receptor and acts as a coregulator of various nuclear receptors. Herein, we examined a novel cross talk between SHP and a forkhead transcription factor HNF3 (hepatocyte nuclear factor 3/Foxa. Transient transfection assay demonstrated that SHP inhibited the transcriptional activity of all three isoforms of HNF3, HNF3alpha, beta, and gamma. In vivo and in vitro protein interaction studies showed that SHP physically interacted with HNF3. Adenovirus-mediated overexpression of SHP significantly decreased the mRNA levels of glucose-6-phosphase (G6Pase), cholesterol 7-alpha-hydroxylase (CYP7A1), and phosphoenolpyruvate carboxykinase (PEPCK) in HepG2 cells and rat primary hepatocytes. Moreover, the mRNA level of G6Pase was notably increased by down-regulation of SHP with small interfering RNA. Interestingly, HNF3 transactivity was still repressed by SHPDelta128-139 that fails to repress nuclear receptors. Mapping of interaction domain revealed that SHP interacted with forkhead DNA binding domain of HNF3alpha. Gel mobility shift and chromatin immunoprecipitation assays demonstrated that SHP inhibits DNA binding of HNF3. These results suggest that SHP is involved in the regulation of G6Pase, CYP7A1, and PEPCK gene expression via novel mechanism of inhibition of HNF3 activity and expand the role of SHP as a coregulator of other family of transcription factors in addition to nuclear receptors.

The Gadd45 family of proteins includes Gadd45␣, MyD118/Gadd45␤, and CR6/OIG37/Gadd45␥. These proteins play important roles in maintaining genomic stability and in regulating the cell cycle. This study reports the cloning of a novel protein called CR6-interacting factor 1 (CRIF1) which interacts with Gadd45␣, MyD118/Gadd45␤, and CR6/OIG37/Gadd45␥. CRIF1 binds specifically to the Gadd45 family proteins, as determined by an in vitro glutathione Stransferase pull-down assay and an in vivo mammalian cell two-hybrid assay along with coimmunoprecipitation assays. CRIF1 mRNA is highly expressed in the thyroid gland, heart, lymph nodes, trachea, and adrenal tissues. CRIF1 localizes exclusively to the nucleus and colocalizes with Gadd45␥. Recombinant CRIF1 inhibits the histone H1 kinase activity of immunoprecipitated Cdc2-cyclin B1 and Cdk2-cyclin E, and the inhibitory effects were additive with Gadd45 proteins. Overexpression of CRIF1 increases the percentage of cells in G 1 , decreases the percentage of cells in S phase, and suppresses growth in NIH3T3 cells. The downregulation of endogenous CRIF1 by the transfection of the small interfering RNA duplexes resulted in the inactivation of Rb by phosphorylation and decreased the G 1 phase cell populations. Expression of CRIF1 is barely detectable in adrenal adenoma and papillary thyroid cancer and much lower than in adjacent normal tissue. The results presented here suggest that CRIF1 is a novel nuclear protein that interacts with Gadd45 and may play a role in negative regulation of cell cycle progression and cell growth.