Production and characterization of ZnO nanoparticles and porous particles by ultrasonic spray pyrolysis using a zinc nitrate precursor

ZnO nanoparticles and porous particles were produced by an ultrasonic spray pyrolysis method using a zinc nitrate precursor at various temperatures under air atmosphere. The effects of reaction temperature on the size and morphology of ZnO particles were investigated. The samples were characterized by energy dispersive spectroscopy, X-ray diffraction, transmission electron microscopy, and scanning electron microscopy. ZnO particles were obtained in a hexagonal crystal structure and the crystallite shapes changed from spherical to hexagonal by elevating the reaction temperature. The crystallite size grew by increasing the temperature, in spite of reducing the residence time in the heated zone. ZnO nanoparticles were obtained at the lowest reaction temperature and ZnO porous particles, formed by aggregation of ZnO nanoparticles due to effective sintering, were prepared at higher temperatures. The results showed that the properties of ZnO particles can be controlled by changing the reaction temperature in the ultrasonic spray pyrolysis method.     

ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and cause Walker-Warburg syndrome

Walker-Warburg syndrome (WWS) is clinically defined as congenital muscular dystrophy that is accompanied by a variety of brain and eye malformations. It represents the most severe clinical phenotype in a spectrum of diseases associated with abnormal post-translational processing of a-dystroglycan that share a defect in laminin-binding glycan synthesis1. Although mutations in six genes have been identified as causes of WWS, only half of all individuals with the disease can currently be diagnosed on this basis2. A cell fusion complementation assay in fibroblasts from undiagnosed individuals with WWS was used to identify five new complementation groups. Further evaluation of one group by linkage analysis and targeted sequencing identified recessive mutations in the ISPD gene (encoding isoprenoid synthase domain containing). The pathogenicity of the identified ISPD mutations was shown by complementation of fibroblasts with wild-type ISPD. Finally, we show that recessive mutations in ISPD abolish the initial step in laminin-binding glycan synthesis by disrupting dystroglycan O-mannosylation. This establishes a new mechanism for WWS pathophysiology.