Dynamic Changes, Correlation of Basophils, and the Therapeutic Effect in Patients With Allergic Rhinitis During Allergen-specific Immunotherapy.

BACKGROUND: The role of basophils in allergic rhinitis (AR) has been studied extensively; however, there are very few reports on changes in basophils after allergen-specific immunotherapy (SIT). OBJECTIVE: To examine the changes and correlation of peripheral blood basophils and the therapeutic effect in patients with AR during allergen-SIT. METHODS: A total of 77 patients with AR who were allergic only to house dust mites received allergen-SIT. At 3 time points, patients underwent testing for the percentage and activation rate of basophils in peripheral blood, skin index (SI) measurement, visual analog scale (VAS) assessment, and rhinoconjunctivitis quality of life questionnaire (RQLQ) evaluation. The results were compared to a control group with congenital preauricular fistula. RESULTS: (1) Before treatment, the percentage and activation rate of basophils in patients with AR were significantly higher than those in controls. There was no significant difference in the percentages and activation rates of basophils at the 3 time points. (2) The SIs, VAS, and RQLQ scores of the patients immediately after treatment and 2 years posttreatment decreased significantly compared to those before treatment; the SI, VAS, and RQLQ scores of the patients 2 years posttreatment increased significantly compared with those immediately after treatment. (3) There was no correlation between the patients' basophil activation rate and percentage and the SI, VAS, and RQLQ scores at all time points. CONCLUSION: The percentage and activation rate of basophils were higher in patients with AR than in controls. The values did not change significantly after allergen-SIT and showed no correlation with treatment effectiveness. Therefore, the frequency and activation rate of basophils cannot be used as criteria for assessing the effectiveness of allergen-SIT for house dust mites. Allergen-SIT is effective for the management of AR, but the effect declines after the completion of therapy.

Comprehensive analysis of alfa defensin expression and prognosis in human colorectal cancer.

Introduction: Colorectal cancer (CRC) is a serious threat to human health. Screening new biomarkers can provide basis for improving the prognosis and individualized treatment of CRC. Although some members of the defensin family were found increased in pancreatic cancer and CRC, their exact function and clinical significance remain unclear. Methods: In this study, the expression, correlation, mutation, and functional enrichment of several defensin family members in pancreatic cancer and CRC were analyzed using tumor public databases and verified in several patients. Results: Results showed no significant correlation between the expression levels of DEFA1-4 and CRC. The expression levels of DEFA5 and DEFA6 significantly increased in CRC tissues compared with those in normal tissues. DEFA5 may be associated with better prognosis of CRC, while DEFA6 may be associated with poor prognosis. Immunohistochemistry (IHC) experiments showed that the expression of DEFA6 was significantly higher in adenoma than in normal mucosa and slightly higher in carcinoma than in normal mucosa. The Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis found that DEFAs were closely related to hsa05202: transcriptional misregulation in cancer and Hsa04015: Rap1 signaling pathway. DEFA5 may be a stable and good prognostic marker, and DEFA6 may be a poor prognostic marker in CRC of metastasis. Conclusion: Overall, DEFA5 and DEFA6 have a certain degree of sensitivity and specificity in predicting CRC.

Depth estimation method of surface of micropart in microassembly space based on microscopic vision tomographic scanning images.

Three-dimensional (3D) morphology of microparts has an important influence on performance of microassembly system that mainly assembles microparts in millimetre and micron scale. Because 3D morphology of microparts cannot be accurately obtained by conventional microscopic vision system, a depth estimation method of surface of micropart in microassembly space based on microscopic vision tomographic scanning (MVTS) images is proposed in this paper. The proposed method uses the positions of pixels with the largest focus values in MVTS image to construct the isodepth contours of surface of micropart and obtains the depth values of micropart's surface at the positions of MVTS by assigning depth values to corresponding isodepth contours. The MVTS images are obtained by MVTS and pixels with the largest focus values in MVTS image are obtained by focus measurement of MVTS images of micropart in microassembly space. On these bases, 3D spatial interpolation method is applied to map depth value of space between adjacent isodepth contours and to obtain depth values of all surface of micropart. Simulation experiments are carried out to verify the proposed method by generating simulated MVTS image array from two simulation objects, and the influence parameters of the proposed method are analysed. In established experimental setup of microassembly that can realise MVTS, experimental verification for the proposed depth estimation method are carried out by using cone cavity and end jaws of microgripper. 3D morphologies of depth maps of cone cavity and end jaws of microgripper are registered with their respective CAD models using iterative nearest point registration algorithm to quantify accuracy of depth estimation. The research results show that 3D morphology of micropart can be obtained by the proposed method and has better accuracy than those by conventional shape from focus method. This method provides a new way to obtain the morphology of microparts and lays a foundation for improving the accuracy and efficiency of gripping, alignment and approaching microparts in microassembly systems.

Molecular cloning, structural analysis and tissue expression of protein phosphatase 3 catalytic subunit alpha isoform (PPP3CA) gene in Tianfu goat muscle.

Calcineurin, a Ca(2+)/calmodulin-dependent protein phosphatase, plays a critical role in controlling skeletal muscle fiber type. However, little information is available concerning the expression of calcineurin in goat. Therefore, protein phosphatase 3 catalytic subunit alpha isoform (PPP3CA) gene, also called calcineurin Aα, was cloned and its expression characterized in Tianfu goat muscle. Real time quantitative polymerase chain reaction (RT-qPCR) analyses revealed that Tianfu goat PPP3CA was detected in cardiac muscle, biceps femoris muscle, abdominal muscle, longissimus dors muscle, and soleus muscle. High expression levels were found in biceps femoris muscle, longissimus muscle and abdominal muscle (p < 0.01), and low expression levels were seen in cardiac muscle and soleus muscle (p > 0.05). In addition, the spatial-temporal mRNA expression levels showed different variation trends in different muscles with the age of the goats. Western blotting further revealed that PPP3CA protein was expressed in the above-mentioned tissues, with the highest level in biceps femoris muscle, and the lowest level in soleus muscle. In this study, we isolated the full-length coding sequence of Tianfu goat PPP3CA gene, analyzed its structure, and investigated its expression in different muscle tissues from different age stages. These results provide a foundation for understanding the function of the PPP3CA gene in goats.

Molecular cloning and characterization of different expression of MYOZ2 and MYOZ3 in Tianfu goat.

The myozenin family of proteins binds calcineurin, which is involved in myocyte differentiation of skeletal muscle. Moreover, gene expression of myozenin is closely related to meat quality. To further understand the functions and effects of myozenin2 (MYOZ2) and myozenin3 (MYOZ3) genes in goat, we cloned them from Tianfu goat longissimus dorsi muscle. Sequence analyses revealed that full-length coding sequence of MYOZ2 consisted of 795 bp and encoded 264 amino acids, and full-length coding sequence of MYOZ3 consisted of 735 bp and encoded 244 amino acids. RT-qPCR analyses revealed that mRNA expressions of MYOZ2 and MYOZ3 were detected in heart, liver, spleen, lung, kidney, leg muscle, abdominal muscle, and longissimus dorsi muscle. Particularly high expression levels of MYOZ2 were seen in abdominal muscle and heart (P<0.01), low expression levels were seen in leg muscle (P<0.01), longissimus dorsi muscle (P>0.05) and very little expression were detected in liver, spleen, lung and kidney (P>0.05). In addition, high expression levels of MYOZ3 were seen in abdominal muscle, leg muscle, lungs and kidney (P<0.01), low expression levels were found in longissimus dorsi muscle and spleen (P<0.01) and very little expression were detected in heart and liver (P>0.05). Temporal mRNA expression results showed that MYOZ2 and MYOZ3 gene expression varied across four muscle tissues with different ages of the goats. Western blotting further revealed that MYOZ2 and MYOZ3 proteins were only expressed in goat muscle, with notable temporal expression differences in specialized muscle tissues from five development age stages. This work provides the first evidence that MYOZ2 and MYOZ3 genes are expressed abundantly in Tianfu goat muscle tissues from different development age stages, and lay a foundation for understanding the functions of MYOZ2 and MYOZ3 genes in muscle fiber differentiation.

Molecular cloning, sequence identification and expression analysis of novel caprine MYLPF gene.

Skeletal muscle genes are important potentially functional candidate genes for livestock production and meat quality. Myosin regulatory light chain (MLC) regulates myofilament activation via phosphorylation by Ca(2+) dependent myosin light chain kinase. The cDNA of the myosin light chain, phosphorylatable, fast skeletal muscle (MYLPF) gene from the longissimus dorsi of Tianfu goat was cloned and sequenced. The results showed that MYLPF full-length coding sequence consists of 513 bp and encodes 170 amino acids with a molecular mass of 19.0 kD. Two EF-hand superfamily domain of MYLPF gene conserved between caprine and other animals. The deduced amino acid sequence of MYLPF shared significant identity with the MYLPF from other mammals. A phylogenetic tree analysis revealed that the caprine MYLPF protein has a close genetic relationship and evolutional distance with MYLPF in other mammals. Analysis by RT-PCR showed that the MYLPF mRNA was detected in heart, liver, spleen, lung, kidney, gastrocnemius, abdominal muscle and longissimus dorsi. In particular, high expression levels of MYLPF mRNA were detected in the longissimus dorsi, gastrocnemius and abdominal muscle, and low level of expressions were observed in liver, spleen, lung and kidney. In addition, the temporal expression analysis further showed MYLPF expression decreased gradually with age in the skeletal muscle. This may be important as muscle growth occurs mainly in young age in goats. Western blotting results detected the MYLPF protein in four of the tissues in which MYLPF was shown to be expressed; the four exceptions were liver, spleen, lung and kidney.

Molecular cloning and tissue distribution of the phosphotyrosine interaction domain containing 1 (PID1) gene in Tianfu goat.

Phosphotyrosine interaction domain containing 1 (PID1) is an important mediator in the development of obesity-related insulin resistance in humans and animals. For a better understanding of the structure and function of the PID1 gene and to study its effect in caprine, the cDNA of the PID1 gene from the abdominal muscle of Tianfu goat was cloned and sequenced. The structure of PID1 was analyzed using bioinformatics tools. The results showed that the full sequence of the caprine PID1 cDNA was 896 bp long and contained a 654 bp long coding region that encoded a 217 amino acid sequence. Fifteen phosphorylation sites were predicted in the translated PID1 protein. The protein had a phosphotyrosine-binding domain between Arg(53) and Ile(199). A phylogenic tree based on the PID1 proteins from other species revealed that the caprine protein was closely related to cattle PID1. Fluorescence quantitative PCR analyses revealed that PID1 was expressed in the heart, liver, spleen, lung, kidney, leg muscle, abdominal muscle and longissimus dorsi muscle of goats. In particular, high expression levels of PID1 were detected in liver and abdominal muscle, and low expression levels were seen in lung. Furthermore, the PID1 mRNA expression levels in the longissimus dorsi muscles increased gradually with the age of the goats (P<0.05). Western blotting results detected the PID1 protein in six of the tissues in which PID1 was shown to be expressed; the two exceptions were liver and spleen.

A compact annular ring microstrip antenna for WSN applications.

A compact annular ring microstrip antenna was proposed for a wireless sensor network (WSN) application in the 2.4 GHz band. In this paper the major considerations of the conformal antenna design were the compact size and the impact on antenna's performance of a steel installation base. By using a chip resistor of large resistance (120 Ω) the antenna size was reduced to 38% of that a conventional annular ring patch antenna. With the addition of the steel installation base the resonant frequency of the antenna increases about 4.2% and the bandwidth reduces from 17.5% to 11.7% by adjusting the load resistance simultaneously. Several key parameters were discussed and optimized, and the antenna was fabricated and its performance measured. The antenna is well matched at 2.4 GHz with 34.2 dB return loss and -2.5 dBi peak gain. Meanwhile, it exhibits excellent radiation patterns with very low cross-polarization levels.

[Cloning and tissue expression of CAST transcript â ¡ in goat].

Calpastatin (CAST) gene is closely related with meat quality in livestock and poultry. Based on the bovine and ovine mRNA sequences, the cDNA of CAST Ⅱ gene in goat was amplified successfully for the first time by using RACE-PCR. Results showed that CAST Ⅱ of goat was 2474 bp in length with an open reading frame (ORF) 1695 bp long and encoded 564 amino acids, and there were four conserved domains and one conserved seven-peptide domain in amino acids sequences. Bioinformation analysis indicated that its secondary structures mainly were random coil and helical regions, and contained rich hydrophobic regions, certain phosphorylation sites, and protein kinase C (PKC) sites. Meanwhile, analysis of tissue expression of the gene in Tianfu meat goat demonstrated it was expressed in seven selected tissues. When the goat was of 6-month age, the highest expression was observed in longissimusdorsi, which was significantly higher than that of crureus (P<0.05) and other internal organ tissues (P<0.01).Furthermore, the expression of CAST II increased with the rise of the age and became the highest when the goat was at three-year age.