Genetic algorithms (GA), a global searching method, is applied to select wavelength variables of near infrared spectroscpy (NIR) for multivariate calibration made by partial least squares (PLS) method. Two application examples of NIR analysis show that this wavelength selection method for PLS modeling not only simplifies and optimizes calibration model but also increases the prediction ability of calibration model. The method is especially adequate for the system where only PLS is difficult to correlate.

Objective To observe the effect of high expression of β-catenin on senescent phenotypes in normal human skin fibroblasts (NHSFs) induced by hydrogen peroxide (H2O2).Methods Cultured NHSFs were classified into three groups: β-catenin + H2O2 group transfected with a recombinant plasmid pcDNA3.1-β-catenin and treated with H2O2 of 150 μ mol/L for two hours,H2O2 group transfected with the empty vector pcDNA3.1 and treated by H2O2 of 150 μmol/L for two hours,and vector group transfected with the empty vector pcDNA3.1 and receiving no treatment.Reverse transcription (RT)-PCR and Western blot were performed to quantify the mRNA and protein expressions of β-catenin in these cells,microscopy to observe the morphological changes of cells.The activity of senescence-associated β-galactosidase (SA-β-Gal) and superoxide dismutase (SOD) as well as the level of reactive oxygen species (ROS) were detected by using commercial kits.Data were processed with the software SPSS 13.0,and analysis of variance (ANOVA) was conducted for multiple group comparisons.Results The expression of β-catenin was significantly upregulated in NHSFs transfected with the recombinant plasmid pcDNA3.1-β-catenin.Both the mRNA and protein expression levels of β-catenin described as β-catenin/ glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ratio were significantly lower in the H2O2 group compared with the vector group (0.2900 ± 0.0195 vs.0.5963 ± 0.0400,0.3130 ± 0.0171 vs.0.6190 ± 0.0090,both P ＜0.05),while the protein expression level of β-catenin was statistically higher in the β-catenin + H2O2 group than in the H2O2 group (0.7953 ± 0.0074 vs.0.3130 ± 0.0171,P ＜0.05).Significant differences were observed between the vector group,H2O2 group and β-catenin+ H2O2 group in the percentage of SA-β-gal-positive cells ((2.9667 ± 0.2517)％ vs.(37.70 ± 0.9539)％ vs.(29.330 ± 0.6359)％,P ＜0.05),ROS activity ((50.9963 ±9.2688)％ vs.(109.9190 ± 11.5215)％ vs.(75.1063 ± 3.0138)％,P ＜0.05),and SOD levels ((88.0856 ±3.9181) vs.(35.5585 ± 3.4438) vs.(61.7029 ± 3.1716) U/mg,P ＜0.05).Conclusion The overexpression of β-catenin can downr_egulate the activity of SA-β-Gal and ROS level,but enhance the activity of SOD.

Objective To investigate the effect of highly expressed β-catenin on the proliferative activity of and expressions of two apoptosis-related genes Bcl-2 and Bax by human skin fibroblasts induced by hydrogen peroxide (H2O2).Methods Normal human skin fibroblasts (HSFs) from child foreskin were divided into three groups:empty vector group transfected with the empty vector pcDNA3.1,H2O2 group transfected with the empty vector pcDNA3.1 followed by treatment with H2O2 (150 μ mol/L) for 2 hours,β-catenin group transfected with pcDNA3.1-β-catenin followed by treatment with H2O2 (150 μ mol/L) for 2 hours.Subsequently,methyl thiazolyl tetrazolium (MTT) assay was conducted to estimate proliferative activity of fibroblasts,flow cytometry to detect cell apoptosis,and reverse transcription (RT)-PCR and Western blot were performed to measure the mRNA and protein expressions of Bcl-2 and Bax respectively.The relative expression levels of genes were expressed as the ratios between the targets and GAPDH.Results Significant differences were found between the empty vector group,H2O2 group and β-catenin group in cellular proliferative activity (expressed as absorbance value at 570 nm:0.792 ± 0.012 vs.0.462 ± 0.012 vs.0.521 ± 0.015,P＜ 0.01) and apoptosis rate (3.407％ ± 0.217％ vs.24.555％ ± 1.793％ vs.15.360％ ± 0.755％,P＜ 0.01).Both mRNA and protein expression levels of Bcl-2 were significantly lower in the H2O2 group (0.333 ± 0.003 and 0.336 ± 0.004 respectively) than in the empty vector group (0.507 ± 0.013 and 0.514 ± 0.021,respectively,both P ＜ 0.01) and β-catenin group (0.404 ± 0.006 and 0.411 ± 0.005,respectively,both P ＜ 0.01).Increased expression levels of Bax mRNA and protein were observed in the H2O2 group compared with the empty vector group and β-catenin group (mRNA:0.451 ± 0.002 vs.0.303 ± 0.005 and 0.339 ± 0.012,protein:0.460 ± 0.008 vs.0.320 ± 0.013 and 0.346 ± 0.013,all P＜ 0.01).Conclusion High expression of β-catenin can raise proliferative activity of aging HSFs.

Objective To compare the short-term therapeutic effects of reconstruction plate versus locking compression plate in the treatment of comminuted fracture of midshaft clavicle in the aged patients.Methods A retrospective analysis was performed of the 64 aged patients who had been treated from March 2009 to April 2015 for comminuted fracture of midshaft clavicle with reconstruction plate or locking compression plate.They were divided into 2 groups according to their treatment methods.There were 30 patients in the reconstruction plate group,14 males and 16 females with an average age of 67.9±5.6 years;there were 34 patients in the locking compression plate group,15 males and 19 females with an average age of 67.1 ± 5.3 years.The 2 groups were compared in terms of operation time,blood loss,fracture healing time,internal fixation failure and shoulder functional recovery.Results The reconstruction plate and locking compression plate groups were followed up for 13.2 ± 3.2 and 12.4 ± 2.9 months,respectively.For the 2 groups,respectively,the average operation time was 62.2 ± 10.7 min and 58.1 ± 11.4 min,the average amount of blood loss during operation 35.2 ± 10.7 mL and 30.4 ±9.6 mL,the average fracture healing time 4.7 ±0.7 months and 4.5 ± 0.7 months,and the excellent to good rate of shoulder function 86.7％ (26/30) and 91.2％ (31/34),showing no significant difference between the 2 groups (all P ＞ 0.05).Five cases (16.7％) reported plate breakage,screw loosening or delayed union due to fixation failure in the reconstruction plate group but none reported fixation failure in the locking compression plate group,showing a significant difference (P ＜ 0.05).There were no significant difference between the 2 groups in fracture nonunion,malunion,neurovascular injury or acromioclavicular arthritis (P ＞ 0.05).Conclusion Since locking compression plate may lead to a lower incidence of fixation failure compared with reconstruction plate,it is recommendable for elderly patients with comminuted fracture of midshafi clavicle.

Objective To investigate the relation between fragmentation of the Golgi apparatus and expression changes of Rab30 in HT22 neurons.Methods The routinely cultured HT22 neurons were divided into control group,thapsigargin 3 h group and thapsigargin 5 h group;neurons in the thapsigargin 3 h group and thapsigargin 5 h group were given 0.1 μg/mL thapsigargin treatment for 3 or 5 h,respectively.Morphology of Golgi apparatus and location of Rab30 were observed with cytochemistry immunofluorescence.The Rab30 mRNA expression was detected by real-time fluorescent quantitative PCR.The protein expressions ofRab30,cis-Golgi matrix protein 130 (GM130),and golgi anti-apoptotic protein (GAAP) were detected by Western blotting.Results Thapsigargin induced markedly Golgi fragmentation in HT22 neurons.The longer the neurons were exposed to thapsigargin,the more the Golgi fragmentation.Hippocampal neurons also expressed Rab30,which was mostly localized on Golgi apparatus.The Rab30 mRNA and protein expressions in the control group,thapsigargin 3 h group and thapsigargin 5 h group were decreased in sequence (relative transcript level:1.00±0.00,0.73±0.05 and 0.53±0.01),with significant differences (P＜0.05).The GM130 and GAAP protein expressions in control group,thapsigargin 3 h group and thapsigargin 5 h group were decreased in sequence,with significant difference (P＜0.05).Conclusion Thapsigargin can induce Golgi fragmentation,which may be related to the decreased expression of Rab30 in HT22 neurons.