Effect of heat treatment in vacuum on photoluminescence of anodic alumina.

The results are presented of a study of the photoluminescent (PL) properties of an undoped porous anodic alumina (PAA) and PAA doped with manganese ions. The PAA samples were prepared by anodization of aluminum. The effect of annealing conditions in vacuum on the PL spectra was studied for the first time and a comparative analysis was made with the spectra of the PAA annealed in air. Vacuum annealing was used to obtain oxygen-deficient alumina. A strong dependence of the PAA PL intensity on the annealing temperature in vacuum has been found: for the samples annealed at 600°Ð¡, the PL intensity is 15 times higher than that measured on the initial samples, whereas for the samples annealed in air it increases only 4.5-fold with excitation at the wavelengths of 275 nm. This is the result of the formation of a high concentration of oxygen vacancies during annealing in vacuum under conditions of oxygen deficiency as compared with the samples annealed in air, where diffusion of oxygen from air leads to a decrease in vacancies. A significant increase in the PL intensity permits consideration of the vacuum-annealed PAA as a promising material for dosimetry.

Glyceraldehyde-3-phosphate dehydrogenase in neurodegeneration and apoptosis signaling.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a well-studied glycolytic enzyme that plays a key role in energy metabolism. GAPDH catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate in the glycolytic pathway. As part of the conversion, GAPDH converts NAD+ to the high-energy electron carrier NADH. GAPDH has been referred to as a "housekeeping" protein and based on the view that GAPDH gene expression remains constant under changing cellular conditions, the levels of GAPDH mRNA have frequently been used to normalize northern blots. In recent years, that view has changed since GAPDH is now known to contribute to a number of diverse cellular functions unrelated to glycolysis. Normative functions of GAPDH now include nuclear RNA export, DNA replication, DNA repair, exocytotic membrane fusion, cytoskeletal organization and phosphotransferase activity. Pathologically, GAPDH has been implicated in apoptosis, neurodegenerative disease, prostate cancer and viral pathogenesis (see Sirover (1999) for a recent review of GAPDH functions). Most recently, it has been shown that GAPDH is a target for deprenyl related compounds (Carlile et al., 2000; Kragten et al., 1998) and may contribute to the neuroprotection offered by those compounds.