Expression of differential nitric oxide synthase isoforms in human normal gastric mucosa and gastric cancer tissue

The present study investigated the expression and distribution of three isoforms of nitric oxide synthase (NOS) in different anatomical regions of the human stomach and in gastric neoplastic tissues by immunohistochemistry using specific antibodies. Intracellular localization of individual isoenzymes of NOS was detected in normal gastric mucosa. Gastric cancer tissues had a marked reduction of all three NOS isoforms expression. The expression of the endothelial NOS, neuronal NOS and inducible NOS in the tumor tissue was significantly lower than in normal gastric mucosa (P = 0.01, P = 0.02, P < 0.01, respectively). In the tumor tissue the expression of inducible NOS was significantly lower than the expression of both constitutive forms of NOS (P < 0.01). There was a tendency to higher expression of both constitutive forms of NOS in earlier stages T2 of the tumor compared to advanced T4 tumor. In contrast, the expression of inducible NOS was higher than in the advanced T4 tumor than in the earlier stages T2 of the tumor. The mapping of the expression of endothelial NOS, neuronal NOS and inducible NOS in human stomach showed higher expression of NOS isoforms in the distal third than in the proximal third of the stomach (P = 0.03, P = 0.04, P = 0.01, respectively). We conclude that there is greater expression of NOS in the stomach corpus and in antrum than in the proximal third of the normal human stomach mirroring the anatomical predilection of common pathological changes in this part of the human stomach. Furthermore, there was loss of the expression of individual isoenzymes in gastric neoplasms.     

Genomics of industrial Aspergilli and comparison with toxigenic relatives

Aspergillus oryzae has been used in Japanese fermentation industries for more than a thousand years. The species produces large amounts of various hydrolytic enzymes and has been successfully applied to modern biotechnology. The size of the A. oryzae genome (37.5 Mb) is very close to that of A. flavus and A. niger, and 20-30% larger than that of either A. nidulans or A. fumigatus. A. oryzae and A. flavus have exactly the same number of aspartic proteinase genes, of which each orthologous pair shares highly conserved amino acid sequences. Synteny analysis with A. fumigatus and A. nidulans showed that the A. oryzae genome has a mosaic structure consisting of syntenic and non-syntenic blocks. In the microorganisms to be compared, the density of the genes having homologs was obviously higher on the syntenic than on the non-syntenic blocks. Expression analysis by the DNA microarray supported the significantly lower expression of genes on the non-syntenic than on the syntenic blocks.     

Temporal expression of PTHrP during endochondral bone formation in mouse and intramembranous bone formation in an in vivo rabbit model

Expression of parathyroid hormone-related protein (PTHrP) messenger RNA (mRNA) and protein was investigated throughout the developmental progression of endochondral bone formation in mouse and intramembranous bone formation in an in vivo model in rabbit, using in situ hybridization and immunohistochemistry. Endochondral bone formation was investigated in a developing embryo, newborn, and adult mouse. In fetal long bones through to newborn (day 7), PTHrP mRNA and protein were consistently expressed in chondrocytes within the proliferative, transitional, and hypertrophic zones. In addition, high levels of PTHrP were also detected in osteoblasts on the surface of trabecular bone surfaces. Similarly, at the adult stage (week 7), PTHrP mRNA and protein were consistently expressed in chondrocytes at epiphyseal ends of the subarticular cartilage, within cortical periosteum, as well as in osteoblasts located at the metaphyseal trabecular bone surfaces. Using an in vivo intramembranous bone formation model in rabbits, expression of PTHrP mRNA and protein was demonstrated in preosteoblasts prior to trabecular bone formation (1-week bone harvest). As bone formed (2-, 3-, and 4-week bone tissue harvests), PTHrP mRNA and protein were highly expressed in actively synthesizing osteoblasts and in those osteocytes embedded within the superficial layers of the bone matrix. Lining osteoblasts and osteocytes buried deeply in the bone matrix displayed weak or no signal for PTHrP. The pattern of spatial and temporal expression of PTHrP demonstrated in cartilage cells and osteoblasts in the two systems suggests an important role of PTHrP in both endochondral and intramembranous bone formation.     

Corrosion evaluation of Au-Cu-Pd ternary alloys

The corrosion resistivity of single-phase Au-Cu-11 at% Pd alloys was evaluated by using a parameterQ which represented the total amount of anodic reaction in a potentiostatic polarization test. The result was compared with those for binary Au-Cu, ternary Au-Cu-11 at % Ag and some commercial alloys. The validity of usingQ as a corrosion parameter was confirmed by the good agreement between the analysed and calculated values of copper ion dissolved into the test solution. By replacing a part of the copper in Au-Cu alloys with palladium the corrosion resistivity can be greatly improved, but silver has no such significant effect. The value ofQ decreased by both treatments of homogenization and grain refinement of the alloy. One of the advantages of the alloy having a single-phase structure is that inhomogeneity in the distribution of the constituents is small even in the as-cast state, which results in a small galvanic effect.     

Characteristics including electron velocity overshoot for0.1-μm-gate-length GaAs SAINT MESFET's

Short-channel effects, substrate leakage current, and average electron velocity are investigated for 0.1-μm-gate-length GaAs MESFETs fabricated using the SAINT (self-aligned implantation for n⁺-layer technology) process. The threshold-voltage shift was scaled by the aspect ratio of the channel thickness to the gate length ( a/L_g). The substrate leakage current in a sub-quarter-micrometer MESFET is completely suppressed by the buried p layers and shallow n⁺-layers. The average electron velocity for 0.1- to 0.2-μm-gate-length FETs is estimated to be 3×10⁶ cm/s from the analysis of intrinsic FET parameters. This high value indicates electron velocity overshoot. Moreover, a very high f_T of 93.1 GHz has been attained by the 0.1-μm SAINT MESFET     

On a fast reactor cycle scheme that incorporates a thoria-based minor actinide-containing cermet fuel

A fast reactor cycle scheme that incorporates a thoria-based minor actinide-containing cermet fuel is given. The present cermet fuel consists of an oxide solid solution of Th and minor actinides and Mo-inert matrix. It has been proposed as a high-performance device that can enhance minor actinide incineration in a fast reactor cycle. It is used in an independent small sub-cycle, whereby dedicated cycle technologies are adopted. Two-step reprocessing process was proposed for the present cermet fuel; it consists of a pre-removal of Mo-inert matrix and an actinide recovery. A preliminary test for the pre-removal of Mo-inert matrix was carried out using a surrogate cermet fuel. Burnup characteristics of a fast reactor core loaded with the cermet fuel were investigated by using neutronic calculation codes. It was revealed that a heterogeneous composition of Mo-inert matrix in inner and outer cores may lead to an effective transmutation of minor actinides and a flattened power density. It was concluded that the present cermet fuel was potentially promising as a high-performance incineration device of minor actinides for fast reactors.     

Purification, characterization, and steady-state kinetics of a meta-cleavage compound hydrolase from Pseudomonas fluorescens IPO1

2-Hydroxy-6-oxo-7-methylocta-2,4-dienoate (6-isopropyl-HODA) hydrolase (CumD), an enzyme of the cumene biodegradation pathway encoded by the cumD gene of Pseudomonas fluorescens IP01, was purified to homogeneity from an overexpressing Escherichia coli strain. SDS-polyacrylamide gel electrophoresis and gel filtration demonstrated that it is a dimeric enzyme with a subunit molecular mass of 32 kDa. The pH optima for activity and stability were 8.0 and 7.0-9.0, respectively. The enzyme exhibited a biphasic Arrhenius plot of catalysis with two characteristic energies of activation with a break point at 20 degrees C. The enzyme has a K(m) of 7.3 microM and a k(cat) of 21 s(-1) for 6-isopropyl-HODA (150 mM phosphate, pH 7.5, 25 degrees C), and its substrate specificity covers larger C6 substituents compared with another monoalkylbenzene hydrolase, TodR Unlike TodF, CumD could slightly hydrolyze 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate (6-phenyl-HODA). A mutant enzyme as to a putative active site residue, S103A, had 10(5)-fold lower activity than that of the wild-type enzyme.