ABSTRACT
OBJECTIVE@#To explore the clinical effect of arthroscopic combined with small needle knife in the treatment of degenerative medial meniscus (MM) injury of knee joint by releasing the superficial layer of medial collateral ligament (SMCL).@*METHODS@#From February 2016 to November 2018, 56 patients (56 knees) with limited pain, strangulation and flexion in medial knee joint space were selected. X-ray Kellgren-Lawrence grading was I-II. MRI showed medial meniscus injury(III degree) of knee joint. There were 30 males(30 knees) and 26 females(26 knees). Arthroscopic MM plasty and small needle knife were used to release SMCL. The Lysholm knee score was used to evaluate the effect of operation.@*RESULTS@#All 56 patients were followed up, and the duration ranged from 3 to 24 months, with an average of 10 months. According to the Lysholm knee score standard, the final follow-up was compared with that of before operation. The results showed that the preoperative knee score was 37.24±1.32, the latest follow-up knee score was 85.72±5.28, the knee score was higher than that before the operation(<0.05).@*CONCLUSIONS@#Arthroscopy combined with small needle knife release of superficial medial collateral ligament in the treatment of degenerative medial knee meniscus injury can effectively improve the mechanical balance of the knee joint, improve Lysholm knee score in patients with knee meniscus injury, and promote the recovery of knee joint function, which has clinical value.
Subject(s)
Female , Humans , Male , Arthroscopy , Collateral Ligaments , Knee Joint , Medial Collateral Ligament, Knee , Menisci, Tibial , Treatment OutcomeABSTRACT
By briefly sorting out the urgent academic conundrums in acupuncture-moxibustion and the bottlenecks during its development in the time of internet plus, this article analyzed the historical background, forecasted the development orientation, and summarized the significance of the digitization of acupuncture-moxibustion: to promote the education of acupuncture-moxibustion major; to conform to needs of culture and knowledge popularization of traditional Chinese medicine; to protect and excavate the traditional knowledge of Chinese medicine; to promote the international communication of acupuncture-moxibustion, and implement the "One Belt, One Road" proposition.
ABSTRACT
By briefly sorting out the urgent academic conundrums in acupuncture-moxibustion and the bottlenecks during its development in the time of internet plus, this article analyzed the historical background, forecasted the development orientation, and summarized the significance of the digitization of acupuncture-moxibustion: to promote the education of acupuncture-moxibustion major; to conform to needs of culture and knowledge popularization of traditional Chinese medicine; to protect and excavate the traditional knowledge of Chinese medicine; to promote the international communication of acupuncture-moxibustion, and implement the "One Belt, One Road" proposition.
ABSTRACT
OBJECTIVE: To investigate the status of the quality of Mingmu Shangqing tablets and to carry out exploratory research on its quality standard. METHODS: Thirty-four batches of samples were tested according to the current quality standard in Pharmacopoeia of the People's Republic of China (2010) Volume I. The exploratory research including microscopic identification of the raw powders, analysis of the volatile constituents by GC, determination of the characteristic components of prepared Radix Et Rhizoma Rhei and Radix Glycytthiae by HPLC, and determination of the active components of Fructus Gardeniae, Radix Paeoniae Rubra, Fructus Aurantii, Pericarpium citri Reticulatae, and Radix Scutellariae by HPLC-DAD. RESULTS: Thirty-three batches (97.1%) met the current quality standard. CONCLUSION: The exploratory research can increase the specificity, controllability and safety of the quality standard of Mingmu Shangqing tablets. It will provide reference for further revise of the drug standard and monitoring the drug quality.
ABSTRACT
<p><b>OBJECTIVE</b>To clone the urea membrane channel gene (ureI) from Helicobacter pylori (Hp) for its expression in E. coli, and evaluate the expression conditions and immunological features of the fusion protein.</p><p><b>METHODS</b>ureI gene cloned by PCR from Hp was inserted into the plasmid pET32a (+) to construct the recombinant plasmid pET32a/ureI, followed by identification by BglII and HindIII digestion and sequencing. E. coli BL-21+(DE3) was transformed with pET32a/ureI to obtain the engineered bacterium BL21+/UreI, which was cultured at different temperatures and induced with 1.0 mmol/L IPTG for expression of the recombinant protein. The expressed proteins were identified by SDS-PAGE and analyzed by Pro-gel analyzer 4.0. Western blotting was performed to evaluate the immunogenicity of the expressed protein.</p><p><b>RESULTS</b>The cloned gene fragment was about 650 bp in length, and BglII and HindIII digestion of pET32a/ureI yielded a 650-bp band. Sequence analysis revealed that the cloned ureI gene contained 646 bp without reading frame alterations. Comparison against GenBank indicated a homology of 100% of the cloned gene with ureI gene of the corresponding Hp strains, and also one no less than 98.5% with ureI gene from other strains. The engineered E. coli BL21+/UreI could express recombinant UreI (rUreI) with His tag, and the target protein accounted for 20.2% of the total bacterial proteins after 1.0 mmol/L IPTG induction of the bacterium at 37 degrees C for 14 h. SDS-PAGE and Western blotting showed that the recombinant UreI protein was produced mainly in the inclusion bodies and fused with his-tag (rUreI/his), which could react with human anti-Hp and mAb to his tag but not with mAb to Hp UreB.</p><p><b>CONCLUSIONS</b>We have successfully cloned ureI gene and constructed the prokaryotic expression plasmid for efficient rUreI expression, and the fusion protein rUreI/his expressed in the inclusion bodies can react specifically with both Hp antibody and his-tag antibody.</p>
Subject(s)
Humans , Bacterial Proteins , Genetics , Metabolism , Blotting, Western , Cloning, Molecular , Electrophoresis, Polyacrylamide Gel , Escherichia coli , Genetics , Helicobacter pylori , Genetics , Membrane Transport Proteins , Genetics , Metabolism , Plasmids , Genetics , Recombinant Fusion Proteins , Genetics , MetabolismABSTRACT
<p><b>OBJECTIVE</b>To construct the prokaryotic and eukaryotic expression vectors pET32/E5 and pcDNA3.1/E5 for transformation into E. coli BL21 and NIH(3)T(3) cells respectively to observe the expression of human papillomavirus type 16 E5 protein (HPV16 E5).</p><p><b>METHODS</b>HPV16 E5 gene was amplified by PCR from clinical isolates of HPV 16 and inserted into the plasmid pET32a(+) followed by digestion with BamH I and Hind III. The recombinant plasmid pET32/E5 was transformed into E. coli JM109 and selected with ampicillin. The positive clones containing the recombinant plasmid pET32/E5 were verified by restriction endonucleases BamH I and Xho and sequence analysis. The expression of HPV16 E5-TRX fusion protein in E. coli BL21(ED3) was identified by SDS-PAGE and Western blotting. The digestion product of BamH I and Xho was purified and inserted into the eukaryotic expression vector pcDNA3.1(+) to construct pcDNA3.1/E5, which was identified by sequencing and transfected into NIH3T3 cells. The NIH(3)T(3) cells with stable expression of HPV16 E5 were selected by G418 and confirmed by RT-PCR.</p><p><b>RESULTS</b>The pET32/E5 and pcDNA3.1/E5 vectors were constructed successfully. E.coli BL21(DE3) transformed by the recombinant plasmid pET32/E5 expressed HPV16 E5-TRX fusion protein efficiently. In the presence of 1 mmol/L IPTG at 28 degrees C, HPV16 E5-TRX recombinant protein accounted for about 10% of the total bacterial proteins. NIH3T3 cells stably expressing HPV16 E5 were harvested by selection with 250 g/ml of G418. HPV16 E5 gene from pcDNA3.1/E5-transfected NIH(3)T(3) cells was amplified by RT-PCR, and sequence analysis demonstrated the acquisition of the full-length gene fragment.</p><p><b>CONCLUSIONS</b>The prokaryotic and eukaryotic vectors for the HPV16 E5 gene have been successfully constructed. The acquisition of E .coli and NIH(3)T(3) cells with stable expression of HPV16 E5 protein may facilitate subsequent research of the biological properties and the transformation mechanism of HPV16 E5 protein on specific cells.</p>