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1.
Oncol Lett ; 18(4): 4136-4143, 2019 Oct.
Article in English | MEDLINE | ID: mdl-31516612

ABSTRACT

Quickly-pulse-to-pulse (Q-PTP) is the latest dual pulse mode Q-switched neodymium-doped yttrium aluminum garnet [QS Nd:YAG (QSNY)] laser technology that improves efficacy and minimizes side effects. In this study, the safety, efficacy, and advantages of Q-PTP and single-pulse laser mode of 1064-nm QSNY in the treatment of melasma were compared. Twelve healthy women were enrolled in this split-face study. Q-PTP and single-pulse laser mode of 1064-nm QSNY were applied to the treatment side and the control side, respectively. Physician's global assessment, patients' self-assessment and the modified melasma area and severity index (mMASI) scores were used to quantify pigmentation changes. Side effects were recorded. Mean mMASI scores were decreased significantly at the 4th and 12th-week follow-up visit compared to the baseline. Melasma lesion clearance was more than 50% in 58% of patients compared with the baseline. However, both sides of the same patient showed similar therapeutic effect. Minor pain experience and slighter skin erythema reaction were reported in Q-PTP laser mode treatment side compared with the control. No serious complications were found in any of the patients. Q-PTP laser mode of 1064-nm QSNY is an optimal laser therapy in the treatment of melasma with greater safety and superiority.

2.
Sci Rep ; 6: 32717, 2016 09 06.
Article in English | MEDLINE | ID: mdl-27596441

ABSTRACT

Soil alkalization severely affects crop growth and agricultural productivity. Alkali salts impose ionic, osmotic, and high pH stresses on plants. The alkali tolerance molecular mechanism in roots from halophyte Puccinellia tenuiflora is still unclear. Here, the changes associated with Na2CO3 tolerance in P. tenuiflora roots were assessed using physiological and iTRAQ-based quantitative proteomic analyses. We set up the first protein dataset in P. tenuiflora roots containing 2,671 non-redundant proteins. Our results showed that Na2CO3 slightly inhibited root growth, caused ROS accumulation, cell membrane damage, and ion imbalance, as well as reduction of transport and protein synthesis/turnover. The Na2CO3-responsive patterns of 72 proteins highlighted specific signaling and metabolic pathways in roots. Ca(2+) signaling was activated to transmit alkali stress signals as inferred by the accumulation of calcium-binding proteins. Additionally, the activities of peroxidase and glutathione peroxidase, and the peroxiredoxin abundance were increased for ROS scavenging. Furthermore, ion toxicity was relieved through Na(+) influx restriction and compartmentalization, and osmotic homeostasis reestablishment due to glycine betaine accumulation. Importantly, two transcription factors were increased for regulating specific alkali-responsive gene expression. Carbohydrate metabolism-related enzymes were increased for providing energy and carbon skeletons for cellular metabolism. All these provide new insights into alkali-tolerant mechanisms in roots.


Subject(s)
Adaptation, Physiological , Carbonates/metabolism , Plant Proteins/metabolism , Plant Roots/metabolism , Poaceae/metabolism , Proteomics , Alkalies , Biomass , Chromatography, Liquid , Crops, Agricultural , Gene Expression , Metals/metabolism , Plant Roots/physiology , Poaceae/genetics , Poaceae/growth & development , Poaceae/physiology , Protein Interaction Maps , Tandem Mass Spectrometry , Transcription Factors/metabolism
3.
BMC Vet Res ; 12(1): 175, 2016 Aug 26.
Article in English | MEDLINE | ID: mdl-27561335

ABSTRACT

BACKGROUND: Porcine cirovirus type 1 (PCV1) and type 2 (PCV2) are circulating in Chinese pig herds and the infected pigs develop antibodies to both viruses. Current commercial available ELISA kits cannot differentiate PCV2-specific antibodies from the mixtures of PCV1 and PCV2 antibodies in PCV1/2-infected or PCV2-vaccinated pigs. Therefore, the need for developing PCV2-specific ELISA methods is urgent to evaluate PCV2 antibody level in exclusion of PCV1 antibody interference after PCV2 vaccination. RESULTS: Virus-like particles (VLPs) of PCV2 based on the recombinant Cap protein were expressed in Escherichia coli. A competing ELISA was established by using the VLPs as coating antigen and a PCV2-specific monoclonal antibody as the competing antibody. The competing ELISA was compared with the results obtained by using an immunoperoxidase monolayer assay on 160 serum samples. The sensitivity and specificity of this competing ELISA were determined as 96.5 and 96.0 %, at 2 standard deviation from the mean or 91.8 and 100 % at 3 standard deviations from the mean. Next, a serological survey of 1297 vaccinated serum samples collected from commercial pig herds in Beijing, Hunan and Henan provinces in China was conducted. The results showed that 85.9 % of sera having positive PCV2 antibodies. CONCLUSIONS: The competing ELISA we developed in this study was both sensitive and specific to PCV2 and was suitable for large-scale PCV2 antibody monitoring in exclusion of PCV1 antibody interference after PCV2 vaccination.


Subject(s)
Antibodies, Viral/blood , Circoviridae Infections/veterinary , Circovirus/immunology , Enzyme-Linked Immunosorbent Assay/veterinary , Swine Diseases/virology , Animals , Antibodies, Monoclonal , Antibodies, Viral/isolation & purification , Antigens, Viral , Capsid Proteins/immunology , Circoviridae Infections/blood , Circoviridae Infections/immunology , Circoviridae Infections/virology , Circovirus/classification , Enzyme-Linked Immunosorbent Assay/methods , Hot Temperature , Reproducibility of Results , Sensitivity and Specificity , Specific Pathogen-Free Organisms , Swine , Swine Diseases/blood , Swine Diseases/immunology
4.
Monoclon Antib Immunodiagn Immunother ; 35(4): 227-30, 2016 Aug.
Article in English | MEDLINE | ID: mdl-27500643

ABSTRACT

Female BALB/c mice were immunized with a commercial PCV2 vaccine, and a monoclonal antibody (MAb) designated as 3H11 was achieved by hybridoma techniques. The MAb specifically reacted with Cap protein of PCV2, which has been identified by western blot. Immunoperoxidase monolayer assay results showed that 3H11 did not cross-react with PCV1-infected cells. Therefore, this work suggested that 3H11 could be a useful tool as a specific diagnostic reagent for PCV2 research.


Subject(s)
Antibodies, Monoclonal/immunology , Antibody Specificity/immunology , Capsid Proteins/immunology , Circovirus/immunology , Animals , Antibodies, Monoclonal/biosynthesis , Antibodies, Viral/immunology , Circovirus/pathogenicity , Epitope Mapping , Female , Mice , Mice, Inbred BALB C , Swine
5.
J Proteomics ; 143: 365-381, 2016 06 30.
Article in English | MEDLINE | ID: mdl-27130536

ABSTRACT

Alkali grass (Puccinellia tenuiflora), a monocotyledonous perennial halophyte species, is a good pasture with great nutritional value for livestocks. It can thrive under low temperature in the saline-alkali soil of Songnen plain in northeastern China. In the present study, the chilling-responsive mechanism in P. tenuiflora leaves was investigated using physiological and proteomic approaches. After treatment of 10°C for 10 and 20days, photosynthesis, biomass, contents of osmolytes and antioxidants, and activities of reactive oxygen species scavenging enzymes were analyzed in leaves of 20-day-old seedlings. Besides, 89 chilling-responsive proteins were revealed from proteomic analysis. All the results highlighted that the growth of seedlings was inhibited due to chilling-decreased enzymes in photosynthesis, carbohydrate metabolism, and energy supplying. The accumulation of osmolytes (i.e., proline, soluble sugar, and glycine betaine) and enhancement of ascorbate-glutathione cycle and glutathione peroxidase/glutathione S-transferase pathway in leaves could minimize oxidative damage of membrane and other molecules under the chilling conditions. In addition, protein synthesis and turnover in cytoplasm and chloroplast were altered to cope with the chilling stress. This study provides valuable information for understanding the chilling-responsive and cross-tolerant mechanisms in monocotyledonous halophyte plant species.


Subject(s)
Adaptation, Physiological , Cold Temperature , Poaceae/metabolism , Proteomics , Seedlings/chemistry , Carbohydrate Metabolism , China , Energy Metabolism , Photosynthesis , Plant Leaves/chemistry , Plant Leaves/enzymology , Plant Proteins/analysis , Poaceae/chemistry , Salt-Tolerant Plants/chemistry , Salt-Tolerant Plants/metabolism , Seedlings/metabolism
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