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Ferritin (FT), a cage-protein composed of 24 subunits, may carry small molecules inside the core of cage. To enhance the potential of FT as a more functional drug carrier, FT genetically-fused with silaffin R5 peptide at N-terminus (R5FT) and silica-enveloped cage protein (SiO2/R5FT) were developed. Doxorubicin (Dox) can be loaded into cage interior by re-assembly of R5FT. The release of Dox loaded in internal cages was retarded by the silica-coated matrix and showed the pH-controlled behavior, in which the release amount is larger in acidic environments than neutral. R5FT provides a biocompatible and eco-friendly manufacturing process for the drug-laden silica nanoparticles over conventional production methods.

Hafnium-aluminum zinc oxide (HAZO) films as an active layer of oxide-transistors with different hafnium (Hf) contents were deposited via co-sputtering of separate targets. The effects of the sputtering power during co-sputtering on the structural, optical, electrical, and chemical properties of the HAZO films were examined. As the sputtering power increased, the structure of the HAZO films changed from polycrystalline to amorphous, and the Hf O bonds in the HAZO films increased, but the Zn O bonds decreased. Also, a bottom-gate-type thin-film transistor (TFT) using the HAZO film as its channel layer was fabricated and characterized. The TFTs using HAZO layer at room temperature as channel layer exhibited the device characteristics, such as a field effect mobility of 0.45 cm2/V·s, a threshold voltage of 17.18 V, a subthreshold swing of 0.85 V/decade, an on/off current ratio of 3.68 × 107, and a visible transmittance of 82.7%. It was discovered that the changes of the electrical characteristics of the HAZO TFTs were closely related to the changes of the Zn O/Hf O bonding ratio.

The SLC37 family consists of four sugar-phosphate exchangers, A1, A2, A3, and A4, which are anchored in the endoplasmic reticulum (ER) membrane. The best characterized family member is SLC37A4, better known as the glucose-6-phosphate (G6P) transporter (G6PT). SLC37A1, SLC37A2, and G6PT function as phosphate (Pi)-linked G6P antiporters catalyzing G6P:Pi and Pi:Pi exchanges. The activity of SLC37A3 is unknown. G6PT translocates G6P from the cytoplasm into the lumen of the ER where it couples with either glucose-6-phosphatase-α (G6Pase-α) or G6Pase-β to hydrolyze intraluminal G6P to glucose and Pi. The functional coupling of G6PT with G6Pase-α maintains interprandial glucose homeostasis and the functional coupling of G6PT with G6Pase-β maintains neutrophil energy homeostasis and functionality. A deficiency in G6PT causes glycogen storage disease type Ib, an autosomal recessive disorder characterized by impaired glucose homeostasis, neutropenia, and neutrophil dysfunction. Neither SLC37A1 nor SLC37A2 can functionally couple with G6Pase-α or G6Pase-β, and there are no known disease associations for them or SLC37A3. Since only G6PT matches the characteristics of the physiological ER G6P transporter involved in blood glucose homeostasis and neutrophil energy metabolism, the biological roles for the other SLC37 proteins remain to be determined.

Glycogen storage disease type Ia (GSD-Ia) patients, deficient in glucose-6-phosphatase-alpha, manifest disturbed glucose homeostasis with long-term renal disease. We have previously shown that renal fibrosis in GSD-Ia is mediated by the angiotensin/transforming growth factor-beta1 (TGF-beta1) pathway, which also elicits renal damage through oxidative stress. In this study, we further elucidate the mechanism of renal disease by showing that renal expression of Nox-2, p22(phox), and p47(phox), components of NADPH oxidase, are upregulated in GSD-Ia mice compared with controls. Akt/protein kinase B, a downstream mediator of angiotensin II and TGF-beta1, is also activated, leading to phosphorylation and inactivation of the Forkhead box O family of transcription factors. This in turn triggers downregulation of superoxide dismutase and catalase (CAT) activities that have essential roles in oxidative detoxification in mammals. Renal oxidative stress in GSD-Ia mice is shown by increased oxidation of dihydroethidium and by oxidative damage of DNA. Importantly, renal dysfunction, reflected by elevated serum levels of blood urea nitrogen, reduced renal CAT activity, and increased renal fibrosis, is improved in GSD-Ia mice treated with the antioxidant drug tempol. These data provide the first evidence that oxidative stress is one mechanism that underlies GSD-Ia nephropathy.