Objective To investigate the association of C-reactive protein (CRP) gene polymorphisms and plasma hs-CRP level,and effect on the genetic susceptibility of ischemic stroke (IS).Methods A case-control study was conducted and 548 patients with acute ischemic stroke and 993 agematched controls from community-based population were included in this study.Epidemiological questionnaires were managed to collect for demographic information.Blood pressure was measured and blood glucose,triacylglycerol,cholesterol,and high sensitivity C-reaction protein (hs-CRP) were detected.Polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) was used for genotyping of CRP gene in all participants.Results The levels of plasma hs-CRP and the proportion of elevated plasma hs-CRP (≥3.0 mg/L) in the ischemic stroke patients (3.534 ± 3.484) mg/L (43.1％) were significantly higher than those of controls (1.957 ±2.344) mg/L (16.6％),t =9.475,P ＜ 0.01,x2 =128.326,P ＜ 0.01.The results of association analysis indicated that rs3093059 and rs3091244 of CPR gene presented statistical associations with ischemic stroke.After correction for confounding factors,ORs (95％ CI) of additive model and dominant model of rs3093059 were 0.697 (0.528-0.921),0.671 (0.487-0.923) respectively.ORs 95％ CI) of dominant model of rs3091244 was 0.728 (0.536-0.988).Further analysis indicated the polymorphism of rs876537,rs3093059,rs3091244 of CPR genotyping were significantly associated with plasma hs-CRP elevation (≥ 3.0 mg/L) both in ischemic stroke patients and in controls (P ＜0.05).Conclusion The CRP genetic polymorphisms were negatively associated with ischemic stroke,and positively corrleted with plasma hs-CRP elevation.However,plasma hs-CPP was positively correlated with ischemic stroke.These results suggested that the plasma hs-CRP levels might be accompanied by ischemic stroke.

Objective: To observe the morphologic changes of pituitary adrenocorticotrophic hormone (ACTH) cells in Wistar rats at different altitudes, and clarify the mechanism of stress reaction to hypoxia in ACTH cells. Methods: Wistar rats were divided into three groups and moved to different altitudes (1700 m, 3100 m, 4050 m). After 12 days, changes of ACTH cells were observed by using immunohistochemisty, image analysis and electron microscopy. Results:The ratio (R) of immunoreactive cell area to scanned area and mean optical density (A) increased at higher altitude with statistically different R values between groups of 1700 m and 4050 m (P

Objective To study safety and efficacy of transurethral Thulium laser resection of high-risk stage bladder tumor in anticoagulant state.Methods A total of 26 non-muscle invasive bladder cancer patients receiving long-term anticoagulant therapy,including 16 cases with cerebral infarction,7 cases with coronary heart disease,3 patients with coronary stenting,were retrospectively analyzed in our hospital from July 2012 to July 2014.In condition not stopping anticoagulants,Thulium laser transurethral resection of bladder tumor was performed,and hemoglobin,thrombin time,the operative time,intraoperative blood loss,postoperative bladder irrigation duration,postoperative hospital stay,bladder tumor recurrence within two years,the postoperative complications were recorded before and after surgery.Results All patients were successfully treated.The operative time was(29.1 ± 12.8) min,int raoperative blood loss was (29.4 ± 16.9) ml portions,postoperative bladder irrigation time was (1.25 ± 0.55) d,postoperative hospital stay was(5.51 ± 1.06) d.Hemoglobin before and after operation were (131.35 ± 6.57) g/L and (129.75 ± 11.05) g/L respectively,there was no statistically significant differences (t =1.014,P ＞ 0.05) between them.Prothrombin time before and after operation were (12.50 ± 0.25) s and(12.44 ± 0.27) s,with no statistically significant difference (t =0.908,P＞0.05)between them.During the followed-up of 48 months,tumor recurred at heterotopia in 2 patients.Conclusions Thulium laser transurethral resection of bladder tumor is safe and effective for patients undergoing long-term oral anticoagulation drugs,without a needto stop taking anticoagulant drugs.

Objective To investigate the effect of thymosin ?1 (T?1) on cellular immune function in gastric cancer patients through observing its treatment on the differentiation of T-lymphocyte subsets from screened peripheral blood mononuclear cells (PBMCs). Methods PBMCs were obtained by centrifugation of blood samples from 18 healthy subjects and 32 patients with gastric cancer,and then cultured in the presence of culture medium with addition of T?1 at 50,10 and 1 ?g/ml for 2 d. T lymphocyte subsets (such as CD4+,CD8+ and CD4+ CD25+ Foxp3+ T cells) and Th1/Th2 multiplex cytokines were detected by flow cytometry (FCM). Results After PBMCs isolated from healthy people and patients were incubated with or without T?1,there was no significant change in percentage of CD4+,CD8+ peripheral lymphocyte subsets and ratio of CD4+/CD8+. There was no obvious change in the percentage of CD4+ CD25+ Foxp3+ T lymphocyte subsets in the normal control,but a significant increase was observed in the cells from patients with gastric cancer after treatment (P

Objective:To explore the transcriptional regulation mechanism of transforming growth factor β 1 (TGF-β 1) on Meox1 and its effect on cell migration of adult human dermal fibroblasts (HDF-a). Methods:(1) HDF-a cells were cultured in RPMI 1640 complete medium (hereinafter referred to as routinely cultured). The cells were divided into TGF-β 1 stimulation group and blank control group. The cells in TGF-β 1 stimulation group were stimulated with 10 μL TGF-β 1 in the mass concentration of 1 mg/μL, while the cells in blank control group were stimulated with the equal volume of phosphate buffer solution. After 72 hours in culture, partial cells in both groups were collected for transcriptome sequencing. The genes with differential expression ratio greater than or equal to 2 and P<0.01 between the two groups were selected to perform enrichment analysis and analysis of metabolic pathways of the Kyoto Gene and Genome Encyclopedia with, and the expression value of Meox1 per million transcripts (TPM) was recorded ( n=3). Partial cells from the two groups were used to detect the Meox1 mRNA expression by real-time fluorescent quantitative reverse transcription polymerase chain reaction (RT-PCR) ( n=3). (2) Cultured HDF-a cells in the logarithmic growth phase (the same growth phase of cells below) were divided into empty plasmid group, Smad2 overexpression (OE) group, Smad3 OE group, and Smad4 OE group, which were transfected respectively with 2 μg empty pcDNA3.1 plasmid and pcDNA3.1 plasmids separately carrying Smad2, Smad3, and Smad4 for 6 hours, and then were routinely cultured for 48 hours. The Meox1 mRNA expression in the transfected cells of each group was detected by real-time fluorescent quantitative RT-PCR ( n=3). (3) HDF-a cells were routinely cultured and grouped the same as in experiment (1). After 72 hours in culture, the enrichment of Smad2, Smad3, and Smad4 protein on the Meox1 promoter in the cells of each group was detected by chromatin immunoprecipitation-quantitative PCR (ChIP-qPCR) ( n=3). (4) HDF-a cells were routinely cultured and divided into negative interference group, small interference RNA (siRNA)-Smad2 group, siRNA-Smad3 group, siRNA-Smad4 group, empty plasmid group, Smad2 OE group, Smad3 OE group, and Smad4 OE group, which were transfected respectively with 50 μmol/L random siRNA, siRNA-Smad2, siRNA-Smad3, siRNA-Smad4, 2 μg empty pcDNA3.1 plasmid and pcDNA3.1 plasmids separately carrying Smad2, Smad3, and Smad4 for 6 hours and then routinely cultured for 48 hours. The enrichment of Smad2, Smad3, and Smad4 protein on the Meox1 promoter in the cells of corresponding group was detected by ChIP-qPCR ( n=3). (5) Two batches of HDF-a cells were cultured and divided into negative interference group, siRNA-Meox1 group, empty plasmid group, and Meox1 OE group, which were transfected respectively with 50 μmol/L random siRNA, siRNA-Meox1, 2 μg empty pcDNA3.1 plasmid and pcDNA3.1 plasmid carrying Meox1 for 6 hours and then routinely cultured for 24 hours. One batch of cells were subjected to scratch test with the scratch width being observed 24 hours after scratching and compared with the initial width for scratch wound healing; the other batch of cells were subjected to Transwell assay, in which the migrated cells were counted after being routinely cultured for 24 hours ( n=3). (6) From January 2018 to June 2019, 3 hypertrophic scar patients (2 males and 1 female, aged 35-56 years) were admitted to the First Affiliated Hospital of Army Medical University (the Third Military Medical University) 8-12 months after burns. The scar tissue and normal skin tissue along the scar margin resected during surgery were taken, and immunohistochemical staining was performed to observe the distribution of Meox1 protein expression. Data were statistically analyzed with one-way analysis of variance and independent sample t test. Results:(1) After 72 hours in culture, a total of 843 genes were obviously differentially expressed between the two groups, being related to tissue repair, cell migration, inflammatory cell chemotaxis induction process and potential signaling pathways such as tumor necrosis factor, interleukin 17, extracellular matrix receptor. The TPM value of Meox1 in the cells of blank control group was 45.9±1.9, which was significantly lower than 163.1±29.5 of TGF-β 1 stimulation group ( t=6.88, P<0.01) with RNA-sequencing. After 72 hours in culture, the Meox1 mRNA expression levels in the cells of blank control group was 1.00±0.21, which was significantly lower than 11.00±3.61 of TGF-β 1 stimulation group ( t=4.79, P<0.01). (2) After 48 hours in culture, the Meox1 mRNA expression levels in the cells of Smad2 OE group, Smad3 OE group, and Smad4 OE group were 198.70±11.02, 35.47±4.30, 20.27±2.50, respectively, which were significantly higher than 1.03±0.19 of empty plasmid group ( t=31.07, 13.80, 13.12, P<0.01). (3) After 72 hours in culture, the enrichment of Smad2, Smad3, and Smad4 protein on the promoter of Meox1 in the cells of TGF-β 1 stimulation group was significantly higher than that of blank control group respectively ( t=12.99, 41.47, 29.10, P<0.01). (4) After 48 hours in culture, the enrichment of Smad2 protein on the promoter of Meox1 in the cells of negative interference group was (0.200 000±0.030 000)%, significantly higher than (0.000 770±0.000 013)% of siRNA-Smad2 group ( t=11.67, P<0.01); the enrichment of Smad2 protein on the promoter of Meox1 in the cells of empty plasmid group was (0.200 000±0.040 000)%, significantly lower than (0.700 000±0.090 000)% of Smad2 OE group ( t=8.85, P<0.01). The enrichment of Smad3 protein on the promoter of Meox1 in the cells of negative interference group was (0.500 0±0.041 3)%, significantly higher than (0.006 0±0.001 3)% of siRNA-Smad3 group ( t=17.79, P<0.01); the enrichment of Smad3 protein on the promoter of Meox1 in the cells of empty plasmid group was (0.470 0±0.080 0)%, which was significantly lower than (1.100 0±0.070 0)% of Smad3 OE group ( t=9.93, P<0.01). The enrichment of Smad4 protein on the promoter of Meox1 in the cells of negative interference group was similar to that of siRNA-Smad4 group ( t=2.11, P>0.05); the enrichment of Smad4 protein on the promoter of Meox1 in the cells of empty plasmid group was similar to that of Smad4 OE group ( t=0.60, P>0.05). (5) Twenty-four hours after scratching, the scratch healing width of cells in siRNA-Meox1 group was narrower than that of negative interference group, while that of Meox1 OE group was wider than that of empty plasmid group. After 24 hours in culture, the number of migration cells in negative interference group was significantly higher than that in siRNA-Meox1 group ( t=9.12, P<0.01), and that in empty plasmid group was significantly lower than that in Meox1 OE group ( t=8.99, P<0.01). (6) The expression of Meox1 protein in the scar tissue was significantly higher than that in normal skin of patients with hypertrophic scars. Conclusions:TGF-β 1 transcriptionally regulates Meox1 expression via Smad2/3 in HDF-a cells, thus promoting cell migration.