Changes in α-Dicarbonyl Compound Contents during Storage of Various Fruits and Juices.

α-Dicarbonyl compounds (α-DCs) are commonly present in various foods. We conducted the investigation into concentration changes of α-DCs including 3-deoxyglucosone (3-DG), glyoxal (GO), and methylglyoxal (MGO) in fresh fruits and decapped commercial juices during storage at room temperature and 4 °C, as well as in homemade juices during storage at 4 °C. The studies indicate the presence of α-DCs in all samples. The initial contents of 3-DG in the commercial juices (6.74 to 65.61 µg/mL) are higher than those in the homemade ones (1.97 to 4.65 µg/mL) as well as fruits (1.58 to 3.33 µg/g). The initial concentrations of GO and MGO are normally less than 1 µg/mL in all samples. During storage, the α-DC levels in the fruits exhibit an initial increase followed by a subsequent decrease, whereas, in all juices, they tend to accumulate continuously over time. As expected, 4 °C storage reduces the increase rates of the α-DC concentrations in most samples. From the viewpoint of the α-DC contents, fruits and homemade juices should always be the first choice for daily intake of nutrients and commercial juices ought to be mostly avoided.

Review of conformal cooling system design and additive manufacturing for injection molds.

This paper points out the significance of cooling in injection molding and briefly reviews the development of cooling systems. The focus of this survey is on the physical model, development, and optimization of conformal cooling systems which have curved cooling circuits following the shape of mold cavity. Compared with traditional cooling systems, conformal cooling can greatly reduce the warpage defect and shorten the cooling cycle time. The computational design methods and additive manufacturing techniques that prompt the development of conformal cooling are deeply investigated. At the end of this survey, the future perspectives for conformal cooling design and manufacturing are discussed.

A20 overexpression under control of mouse osteocalcin promoter in MC3T3-E1 cells inhibited tumor necrosis factor-alpha-induced apoptosis.

AIM: To construct an A20 expression vector under the control of mouse osteocalcin promoter (OC-A20), and investigate osteoblastic MC3T3-E1 cell line, which stably overexpresses A20 protein prevented tumor necrosis factor (TNF)-alpha-induced apoptosis. METHODS: OC-A20 vector was constructed by fusing a fragment of the mouse osteocalcin gene-2 promoter with human A20 complementary DNA. Then the mouse MC3T3-E1 cell line, stably transfected by A20, was established. The expression of A20 mRNA and A20 protein in the cells were detected by reverse transcription-polymerase chain reaction (RT-PCR) and Western blot analysis, respectively. To determine the specificity of A20 expression in osteoblast, the mouse osteoblastic MC3T3-E1 cell line and mouse embryo fibroblast NIH3T3 cell line were transiently transfected with OC-A20. The anti-apoptotic role of A20 in MC3T3-E1 cells was determined by Flow cytometric analysis (FACS), terminal dUTP nick endo-labeling (TUNEL) and DNA gel electrophoresis analysis (DNA Ladder), respectively. RESULTS: Weak A20 expression was found in MC3T3-E1 cells with the primers of mouse A20. A20 mRNA and A20 protein expression were identified in MC3T3-E1 cells transfected with OC-A20 using RT-PCR and Western blot analysis. Only A20 mRNA expression was found in MC3T3-E1 cell after MC3T3-E1 cells and NIH3T3 cells were transient transfected with OC-A20. A decrease obviously occurred in the rate of apoptosis in the OC-A20 group compared with the empty vector (pcDNA3) group by FACS (P< 0.001). A significant increase in TUNEL positive staining was found in the pcDNA group compared with OC-A20 group (P< 0.001). Simultaneously, similar effects were demonstrated in DNA gel electrophoresis analysis. CONCLUSION: We constructed an osteoblast-specific expression vector that expressed A20 protein in MC3T3-E1 cells and confirmed that A20 protects osteoblast against TNF-alpha-induced apoptosis.

Genome Structure and the p10 Gene of the Helicoverpa armigera Nucleopolyhedrovirus.

The genomic DNA of Helicoverpa armigera single-nucleocapsid nucleopolyhedrovirus (C1 clone) was digested with BamHI, EcoRV, HindIII, KpnI, PstI and XbaI, respectively, and formed 11, 31, 13, 6, 7, and 25 fragments larger than 400 bp, respectively. The size of genome was estimated to be about 130.7 kb. A detailed physical map was constructed for the six restriction enzymes. The five homologous region, hr1, hr2, hr3, hr4 and hr5, and the ten genes including polyhedrin gene (ph), immediate-early gene(ie1), p74, p10, chitinase gene, DNA directed DNA polymerase gene (DNApol), helicase gene, superoxide dismutase gene (sod), alkaline-exonuclease gene (alk-exo), ecdysteroid UDP-glucosyltransferase gene (egt) were identified and their locations in the genome were determined. The genome organization of HaSNPV is quite different from those of other NPVs ever determined. The p10 gene was located in the fragment BamHI-I(1.89 kb) with the transcriptional direction opposite to the polyhedrin gene. Upstream and downstream of the p10 gene were p26 and p74 gene, respectively. The transcriptional direction of p26 is the same as that of p10 gene, and opposite to that of the p74 gene. The ORF encoding p10 was 261 nucleotide long and encoding a putative 87 amino acid polypeptide of 9.3 kD. The immediate upsteam region of the p10 was an A-rich region, and aconserved TAAG motif, associated with transcriptional start sites in other p10 genes, was identified at a site 52 nucleotides upstream of the start codon ATG. A putative polyadenylation signal, AATAAA, was found 20 nucleotides downstream of the termination codon.