Application of self-made fine-tuning device in distal locking process of femoral interlocking intramedullary nail / 中国骨伤

OBJECTIVE@#To evaluate the curative efficacy of self-made fine-tuning setting in the process of femoral distal implantation of intramedullary nail.@*METHODS@#From October 2015 to October 2017, 66 cases of femoral shaft fracture were treated with anterograde interlocking intramedullary nail including 45 males and 21 females with a mean age of(37.21±11.18) years old. Among them, 36 cases were treated with the manufacture's aiming device and self-made fine-tuning setting (research group), other 30 cases were treated with the manufacture's aiming device(control group). The mean operation time, the times of C-arm scan in surgery, the post-operation complications and the fracture union were observed and compared in two groups.@*RESULTS@#Sixty-two cases acquired 8 to 15 months with a mean time of 12.4 months follow-up visit. The post-operation complications and the fracture union between the two groups had no significant difference(>0.05), the mean operation time and the times of C-arm scan in surgery had statistically significant difference(<0.05).@*CONCLUSIONS@#Self-made fine-tuning setting in the process of femoral interblocking intramedullary nail could shorten operation time and reduce the the times of C-arm scan.

The protein X4 of severe acute respiratory syndrome-associated coronavirus is expressed on both virus-infected cells and lung tissue of severe acute respiratory syndrome patients and inhibits growth of Balb/c 3T3 cell line / 中华医学杂志(英文版)

<p><b>BACKGROUND</b>The genome of the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) includes sequences encoding the putative protein X4 (ORF8, ORF7a), consisting of 122 amino acids. The deduced sequence contains a probable cleaved signal peptide sequence and a C-terminal transmembrane helix, indicating that protein X4 is likely to be a type I membrane protein. This study was conducted to demonstrate whether the protein X4 was expressed and its essential function in the process of SARS-CoV infection.</p><p><b>METHODS</b>The prokaryotic and eukaryotic protein X4-expressing plasmids were constructed. Recombinant soluble protein X4 was purified from E. coli using ion exchange chromatography, and the preparation was injected into chicken for rising specific polyclonal antibodies. The expression of protein X4 in SARS-CoV-infected Vero E6 cells and lung tissues from patients with SARS was performed using immunofluorescence assay and immunohistochemistry technique. The preliminary function of protein X4 was evaluated by treatment with and over-expression of protein X4 in cell lines. Western blot was employed to evaluate the expression of protein X4 in SARS-CoV particles.</p><p><b>RESULTS</b>We expressed and purified soluble recombinant protein X4 from E.coli, and generated specific antibodies against protein X4. Western blot proved that the protein X4 was not assembled in the SARS-CoV particles. Indirect immunofluorescence assays revealed that the expression of protein X4 was detected at 8 hours after infection in SARS-CoV-infected Vero E6 cells. It was also detected in the lung tissues from patients with SARS. Treatment with and overexpression of protein X4 inhibited the growth of Balb/c 3T3 cells as determined by cell counting and MTT assays.</p><p><b>CONCLUSION</b>The results provide the evidence of protein X4 expression following SARS-CoV infection, and may facilitate further investigation of the immunopathological mechanism of SARS.</p>

Expression and purification of truncated human recombinant nuclear apoptosis-inducing factor 1 in E.coli / 中国免疫学杂志

Objective:Nuclear apoptosis-inducing factor 1(NAIF1) is a novel apoptosis gene cloned in laboratory. To analyze the binding proteins of NAIF1 by pulldown method, the fusion expression vector of truncated human nuclear apoptosis-inducing factor 1〔NAIF1(73-327)〕 was constructed, were expressed and purified the recombinant GST-NAIF1(73-327) fusion protein in E.coli.Methods:The cDNA encoding human NAIF1(73-327) was amplified by PCR and cloned into pGEX-KG vector. The GST-NAIF1(73-327) fusion protein was expressed in E.coli and purified by affinity chromatography. The purified protein was detected by SDS-PAGE, Western blot and ESI-Q-TOF-MS/MS.Results:A prokaryotic expression vector of GST-NAIF1(73-327) was constructed and the GST-NAIF1(73-327) fusion protein was expressed in E.coli at high level. SDS-PAGE analyses indicated that the purified protein was about 53 kD. Western blot and MS/MS analyses verified the recombinant fusion protein.Conclusion:An efficient method for obtaining recombinant GST-NAIF1(73-327) fusion protein had been established and it could be used for further studies on the structure and function of NAIF1.