Formation of Bright White Plasma Electrolytic Oxidation Films with a Uniform Maze-Like Structure by Anodizing Aluminum in Ammonium Tetraborate Solutions

Bright white plasma electrolytic oxidation (PEO) films with uniform maze-like structures were obtained by anodizing Al in an ammonium tetraborate solution. High-purity Al plates were galvanostatically anodized in 0.3-2.4 M ammonium tetraborate solutions at 303-343 K and 10-100 Am-2. A PEO film consisting of an outer porous layer consisting of amorphous alumina and crystalline alumina with alpha-and gamma-phases and an inner amorphous barrier alumina layer was obtained on the Al surface. An extremely uneven PEO film with various pore sizes and many cracks was formed in a 0.3 M ammonium tetraborate solution, whereas a relatively uniform porous PEO film with similar pore sizes was obtained in 0.9-2.4 M solutions. This difference in the PEO film morphology was due to the plasma generation behavior while anodizing. The lightness of the PEO film increased with increasing anodizing time and PEO film thickness; thus, a bright white PEO film measuring 87.5 in lightness (L*) was formed on the Al surface. The water wettability of the PEO film exhibited weak hydrophilicity. Moreover, a superhydrophobic PEO film with a contact angle of 154 degrees was easily fabricated by self-assembled monolayer modification. Similar bright white PEO coatings were successfully fabricated on various industrial alloys

Molecular Cloning, Expression Analyses, and Physiological Roles of Cathelicidins in the Bursa of Fabricius of the Japanese Quail, <i>Coturnix japonica</i>

Antimicrobial peptides (AMPs) act directly on pathogens and maintain the anti-inflammatory effects and activation of immunocompetent cells. Therefore, the activation of the immune system in poultry via the elevation of endogenous AMPs has been attempted. In this study, we focused on the host defense mechanisms in the bursa of Fabricius (BF) of Japanese quail, cloned the cDNA of cathelicidin (CATH)-1 to -3, and analyzed their expression sites. In situ hybridization experiments revealed the mRNA expression of the CATHs in the interfollicular epithelium surrounding the lumen of the quail BF, which suggests that each CATH may exert its antimicrobial action directly in the BF. The intravenous injection of bacterial lipoteichoic acid and lipopolysaccharide endotoxins into the quail promoted the mRNA expression of CATH-1 and CATH-3 in the BF. The addition of CATH-1 or CATH-2 at the time of the antigen injection into mice resulted in antiserum with high antibody titers. Ad libitum administration of butyrate, a short-chain fatty acid, in the drinking water induced an increase in CATH-2 mRNA expression in the BF under certain conditions. These results may improve the defense mechanisms of quail by stimulating CATH expression in the BF through their diet