ABSTRACT
Ultrasonically assisted hydrothermal synthesis of PZT thin films was performed using an ultrasonic transducer integrated into the lid of an autoclave. Direct ultrasonic irradiation of 23 W at 53 kHz was carried out during the hydrothermal synthesis at a reaction temperature of 140 degrees C for 24 h. The resultant PZT thin film was characterized using scanning electron microscopy (SEM) and x-ray diffraction (XRD). The PZT thin film had fine nanoparticles of approximately 100 nm in diameter when the substrate was placed perpendicular to the plane of ultrasonic irradiation. The film exhibited predominantly (001) orientation when the substrate was placed parallel to the plane of ultrasonic irradiation.
ABSTRACT
BACKGROUND: The activity of adenylyl cyclase (AC) is enhanced by pharmacologically relevant concentrations of ethanol. The enhancing effect of ethanol on AC activity is AC isoform-specific. Therefore, we hypothesized that within a cyclic AMP-generating system, AC is the target of ethanol's action and that ethanol-sensitive AC molecules contain structural elements modulated by ethanol. The structural elements are designated as "ethanol responsive domains." METHODS: By using a series of chimeric mutants, we searched regions of the AC molecule that are important for the ethanol effect. These chimeric mutants were derived from 3 isoforms of AC: AC7 (type 7), the most ethanol responsive isoform; AC3 (type 3), an isoform that is far less responsive to ethanol; and AC2 (type 2), an isoform that is homologous to AC7 but less responsive to ethanol. RESULTS: We identified 2 discrete regions of the AC molecule that are important for the enhancement of AC activity by ethanol. The first is the N-terminal 28-amino-acid (aa) region of the C(1a) domain. The second is the C-terminal region ( approximately 140 aa) of the AC molecule. Sequence differences in the N-terminal tail, 2 putative transmembrane domains, and the C(1b) domain are not important for ethanol's effect. CONCLUSIONS: The current study with mammalian ACs provides a new class of alcohol-responsive protein and possibly a new mechanism of alcohol action on cellular function. The identification of ethanol responsive domains will facilitate the elucidation of the mechanisms by which ethanol enhances the activity of AC.
Subject(s)
Adenylyl Cyclases/drug effects , Central Nervous System Depressants/pharmacology , Ethanol/pharmacology , Adenylyl Cyclases/genetics , Cells, Cultured , Cyclic AMP/metabolism , Cyclic AMP/physiology , DNA, Complementary/genetics , Humans , Isoenzymes/drug effects , Isoenzymes/genetics , Models, Molecular , Molecular Sequence Data , Mutant Chimeric Proteins/genetics , Mutation , Signal Transduction/drug effects , TransfectionABSTRACT
Process extension is a most marked and characteristic neuronal feature that is observed during the development, regeneration and plasticity of nervous system tissues. Neuro-p24, a novel membranous protein with a molecular weight of 24 kDa, is specifically localized in neurons, particularly in the neurites. Based on its molecular structure and distribution pattern in the brain we proposed that Neuro-p24 plays a role in neurite extension. In the present study we have made several findings that support this hypothesis; first, Neuro-p24 was abundant in motor axonal fibers, neurites of dorsal root ganglia neurons and apical dendrites of cerebral cortex neurons when their extension or arborization was proceeding very actively. Secondly, when COS-7 epithelial cells were transfected with either wild-type or deletion-mutated Neuro-p24 cDNAs, ectopic expression of wild-type cDNA caused morphological alterations resulting in a neuron-like appearance. These observations firmly support our proposal and indicate that Neuro-p24 plays an important role in the nervous tissue.
