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1.
Chinese Journal of Experimental Traditional Medical Formulae ; (24): 14-19, 2019.
Article in Chinese | WPRIM | ID: wpr-802093

ABSTRACT

Objective: To explore the effect of Longdan Xiegantang on serum inflammatory factors, related proteins and immune function in patients of secretory otitis media (SOM) with liver and gallbladder wetness-heat Syndrome. Method:Totally 76 cases of SOM with liver and gallbladder wetness-heat syndrome admitted to our hospital from July 2017 to May 2018 were randomly divided into two groups, with 38 cases in each group. Control group was treated with triamcinolone acetonide and ambroxol. In addition to the therapy of control group, observation group was also treated with Longdan Xiegantang. Immunoglobulin (Ig) A, IgG, IgM, CD3+, CD4+, CD8+and NK, interleukin-1 beta (IL-1β), IL-5, IL-8, tumor necrosis factor-α (TNF-α), platelet activating factor (PAF), calcitonin (PCT) and water channel protein-1 (AQP-1), AQP-4, fiber link protein (Fn) and soluble interleukin-2 receptor (SIL-2R) levels of two groups were observed before and after treatment. Curative effect and adverse reaction were observed. Result:①Curative effect, after treatment, the total effective rate of observation group was 92.11%, which was higher than 76.32% of control group, with statistically significant differences (Z=2.108, Pα, PAF, PCT, IL-1β and IL-8 in observation group were lower than those in control group after treatment (PPP+, IgA, IgG and IgM of observation group were lower than those of control group (P+, CD4+, CD4+/CD8+ and NK were higher than those of control group (PConclusion:Longdan Xiegantang has a remarkable effect in treating patients of secretory otitis media with liver and gallbladder wetness-heat syndrome, and can restore symptoms, inhibit inflammatory response, activate cell and humeral immune system, reduce the secretion of AQP-1, SIL-2R and other proteins, and increase the secretion of AQP-4 and Fn proteins.

2.
Chinese Journal of Hematology ; (12): 618-621, 2011.
Article in Chinese | WPRIM | ID: wpr-251513

ABSTRACT

<p><b>OBJECTIVE</b>To explore the role of the amino acids between 551 and 565 in the cytoplasmic domain of glycoprotein (GP) I b alpha in the VWF binding to GP I b alpha.</p><p><b>METHODS</b>The VWF binding to GP I b alpha induced by ristocetin was analyzed by flow cytometry, in three GP I b-IX-expressing Chinese hamster ovary (CHO) cell lines 1b9, delta 565 and delta 551, adhesion of above cells on VWF by flow chamber analysis at shear rate of 200 s(-1). The spread of GP I b-IX-expressing cells were stimulated with botrocetin on VWF-coated coverslips by confocal microscope.</p><p><b>RESULTS</b>The VWF binding to GP I b alpha was higher in delta 565 cells stimulated by ristocetin than in delta 551 or 1b9 cells. The number of delta 565 cells adhered on the VWF-coated-chamber was more than that of controls at shear rate of 200 s(-1). Moreover, the surface spreading areas of delta 565 cells were greater than that of the controls on VWF-coated coverslips.</p><p><b>CONCLUSIONS</b>The amino acids between 551 and 565 in the cytoplasmic domain of GP I b alpha regulates the VWF binding to GP I b alpha.</p>


Subject(s)
Animals , Cricetinae , Female , Amino Acid Sequence , CHO Cells , Cricetulus , Platelet Adhesiveness , Platelet Glycoprotein GPIb-IX Complex , Genetics , Metabolism , von Willebrand Factor , Metabolism
3.
Journal of Experimental Hematology ; (6): 1560-1563, 2009.
Article in Chinese | WPRIM | ID: wpr-328600

ABSTRACT

The aim of this study was to construct Chinese Hamster Ovary (CHO) cell models expressing recombinant wild-type GPIb-IX and mutant GPIb-IX complex, so as to provide the platform to study the related physiologic functions of GPIb-IX. The plasmids were extracted from E.coli expressing wild-type or deletion mutant GPIbalpha and were identified by digestion with EcoR I. Three plasmids containing GPIbalpha, GPIbbeta, and GPIX genes were co-transfected into CHO cells, and then the expression of GPIb-IX complex was detected by immune coprecipitation, Western blot and flow cytometry. The results showed that the expression of GPIb-IX complex could be detected in the lysate and on the surface of CHO cells at 48 hours after transfection. In conclusion, CHO cell models expressing recombinant wild-type or mutation GPIb-IX complex has been successfully constructed.


Subject(s)
Animals , Cricetinae , CHO Cells , Cricetulus , Mutation , Plasmids , Platelet Glycoprotein GPIb-IX Complex , Genetics , Recombinant Proteins , Genetics
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