Objective To explore the role of a new apoptosis related gene TFAR 19 in the pathogenesis of systemic lupus erythematosus (SLE) and the relationship between TFAR 19 and SLE.Methods ELISA was used to test if there is relation between TFAR 19 and SLE.Results It was found that in active SLE patients there was higher titer of TFAR 19 antibody than that in stability patients and normal controls.No significant difference was seen between stability patients and normal controls.Conclusion It is first put forward that TFAR 19 may be related with SLE pathogenesis and disease activity.

Objective To investigate the change of aquaporin 2 (AQP2) mRNA and protein levels in renal collecting duct of SD rats after hypoxin caused by rising of the altitude to 4600 m. Methods Forty male SD rats were randomly divided into 4 groups (24 h, 48 h, 72 h and 1 week group), and 10 rats in Xining city were used as control group. All the 40 SD rats were transported to Kekexili Natural Reservation areas (4600 m) in Qinghai province. Rats of four experimental groups were sacrificed and renal tissue samples were harvested at different time point respectively, the control group rats were treated in Xining city (2260 m) as well. The concentration of plasma antidiuretic hormone (ADH) was measured by radioimmunity method. The expression of AQP2 mRNA and proteins was evaluated by real-time fluorescent quantitative-PCR, Western blot and immunofluorescence assay. Results The concentration of plasma ADH was decreased at 24 h and was only 28.5% of that of control group, reaching the lowest concentration at 48 h [(86.94±6.49) μg/L vs (302.5±310.48) μg/L], then it increased gradually and was similar to the control group at 7 d [(306.46±11.14) μg/L vs (302.53±10.48)μg/L, P＞ 0.05]. There were significant differences of the control group with 24 h, 48 h and 72 h groups, respectively[(302.53± 10.48) μg/L vs (142.46±10.57)μg/L, (86.94±6.49)μg/L, (169.65±11.15) μg/L respectively, P＜0.01]. The change of AQP2 gene expression level was consistent with the change of ADH. It was decreased at the begining when exposure to altitude and it reached its lowest level at 48 h. It was then returned to high level similarly to that of the control group at 7 d (0.09±0.01 vs 0.09± 0.008, P＞0.05 ). There were significant differences of the control group with 24 h, 48 h and 72 h group, respectively (0.09±0.008 vs 0.04±0.005, 0.03±0.002, 0.04±0.003 respectively, P＜0.01 ). Conclusions AQP2 expression in the renal collecting duct of SD rats is altered over the period exposed to altitude. It is decreased in the early hypoxia period, and is increased in later period. This change may be related to the intensity of hypoxia, which is mediated by a potential adaptation mechanisms against hypoxia caused by high altitude.

Objective: in order to provide rapid and reliable method. Methods: Encoded Annexin Ⅴ cDNA was amplifyed from U937 cDNA libary by PCR and then subcloned into E coli expression vector. MS2-Annexin Ⅴ fusion protein could be overexpressed in E　coli. The MS2 bacteria protein could be removed by thrombin digestion.The mature Annexin Ⅴ was obtained by ion exchange chromatography and the FITC labled Annexin Ⅴ could be used in the detection of apoptosis. Results:Up to 37% of the total bacterial proteins was rhAnnexin Ⅴ as showed by SDS-PAGE. The purification of Annexin Ⅴ is over 99%. The FITC labled Annexin Ⅴ could efficiently detect apoptosis. Conclusion: We successfully established the technique procedure of obtaining a large quantity of Annexin Ⅴ and provided the basic routine for popularizing the detection of apoptosis' with high effciency.

Objective:To set up an effective and simple purification method to obtain highly purified prokaryotic protein of PDCD5 and study its stability. Methods:Recombinant PDCD5 protein expressed in E. coli was accumulated as an inclusion body. After washing, the inclusion body was denatured, renatured, digested with thrombine and then purified by two steps of chromatography. The purity of the products was analyzed by capillary electrophoresis and the stability was identified by SDS-PAGE. Results:Capillary electrophoresis showed that the purity of protein was 100%, and molecular weight was 15 800 with pI 5.9. Further bioactivity assay indicated that the purified PDCD5 could enhance the apoptosis of HL 60 cells withdrawing cytokine, which was in a dose dependent manner. Stability analysis showed that the PDCD5 protein was sensitive to temperature and easy to degrade at 4 ℃ and 25 ℃. However, it was relatively stable at -20 ℃ or lyophilized. Conclusion:Highly purified and stable recombinant PDCD5 protein was obtained, which lays a foundation for the functional study and application investigation of PDCD5 .