1.Clinical analysis of a case of acute mercury poisoning due to intramuscular injection of metallic mercury
Qifeng WU ; Ming HUA ; Danxia FANG ; Xia LI ; Pin CAI ; Yongguang ZHANG
China Occupational Medicine 2026;53(2):196-200
Objective To summarize the clinical features and treatment strategies of acute mercury poisoning caused by intramuscular injection of metallic mercury. Methods The clinical data of a patient with acute mercury poisoning following intramuscular injection of metallic mercury were collected, and a retrospective analysis of the diagnosis and treatment process was conducted. Results The patient was a 14-year-old boy who self-injected 20 g of metallic mercury into the left upper arm muscle. Clinical manifestations included fever, chest tightness, cough, and a painful mass at the injection site. Laboratory tests of the patient indicated that blood mercury level was 4.160 μmol/L, urinary mercury level was 6 545.50 μg/g creatinine, urinary retinol-binding protein was 6 556 μg/L, urinary β2-microglobulin was 8 726.48 μg/g creatinine, and urinary α1-microglobulin was 41.60 mg/L at day 11 after injection. Thoracoabdominal imaging revealed mercury deposition in the lungs, heart, liver, kidneys, and other organs. The patient's clinical symptoms were markedly relieved after one course of treatment with sodium dimercaptopropanesulfonate for mercury chelation. Subsequent treatment included continued mercury chelation therapy, debridement of muscle tissue at the injection site, removal of retained foreign bodies, and other supportive measures. Reexamination showed a blood mercury level of 2.810 μmol/L and urinary mercury level of 5 280 μg/L at day 127 after injection. Conclusion The clinical manifestations of intramuscular injection of metallic mercury poisoning differ from those of occupational mercury poisoning. Debridement of the injection site combined with sodium dimercaptopropanesulfonate chelation therapy can alleviate systemic symptoms and reduce mercury levels in such patients.
2.Factors affecting the prevalence of hyperuricemia in an island troop
Yongguang FANG ; Shujun SUN ; Chong TANG ; Chunyu LIU ; Qian XU ; Ying LIANG ; Huihui GUO ; Peng YANG ; Nannan CHEN
Journal of Navy Medicine 2025;46(6):574-578
Objective To analyze the factors affecting the prevalence of hyperuricemia(HUA)in an island troop.Methods A total of 1 113 soldiers stationed on an island from December 2021 to December 2022 were selected as research objects by cluster sampling.Their lifestyle and health information were collected.Physical examination and laboratory detection were conducted.Multivariate logistic regression was used to analyze the influencing factors of HUA.Results The prevalence rate of HUA was 21.02%(234/1 113).There were significant differences in the body mass index(BMI),waist-to-hip ratio,triglyceride,alanine aminotransferase,and creatinine between the soldiers with hyperuricemia and the soldiers with normal blood uric acid(P<0.05).Multivariate logistic regression analysis showed that BMI≥24(OR=1.49,95%CI:1.09-2.05),abnormal liver function(OR=2.26,95%CI:1.31-3.92),and dyslipidemia(OR=1.46,95%CI:1.01-2.12)were positively correlated with hyperuricemia;age>30 years old(OR=0.59,95%CI:0.37-0.93)and exercise time>1 h per week(OR=0.46,95%CI:0.22-0.97)were negatively correlated with HUA.Conclusion The prevalence rate of hyperuricemia is at a high level in an island troop.BMI≥24,age≤30 years old,exercise time≤1 h per week,abnormal liver function,and dyslipidemia are the risk factors for HUA.Prevention and control measures should be taken as early as possible for the soldiers with these risk factors.
3.Construction and identification of eukaryotic expression plasmid carrying hTERT-P2A-EGFP
Xiaona CHEN ; Xiaodan WANG ; Liguang SUN ; Fang FANG ; Weiwei CUI ; Yongguang YANG ; Ya LIU
Journal of Jilin University(Medicine Edition) 2017;43(2):213-219,封2
Objective:To construct the eukaryotic expression plasmid carrying hTERT-P2A-EGFP, and to explore its expression and transfection efficiency in the HEK293FT cells.Methods:The recombinant plasmid was constructed by using pBABE-puro-hTERT and pRRLSIN-cPPT-MSCV-EGFP plasmids.The hTERT,P2A,and EGFP genes were obtained using pBABE-puro-hTERT as template by PCR.And the correct hTERT was inserted into pRRLSIN-cPPT-MSCV-EGFP vector.Then the recombinant plasmid containing hTERT-P2A-EGFP gene was obtained and identified.The HEK293FT cells were transfected by the recombinant plasmid, and the expression of green fluorescence protein(GFP) was observed by fluorescence microscope.Results:The PCR results showed that the fragments of hTERT, P2A, and EGFP were 3 400, 110 and 720 bp.And the length of gene fragment(hTERT-P2A-EGFP)was 4 300 bp by enzyme digestion.The results of sequencing showed that the 1 547 site of the target gene was mutated.Using site-directed mutagenesis, the 1 547 site was successfully mutated.And the target gene sequence was completely identical with the sequence published in GenBank.The recombinant plasmid was transfected into the HEK293FT cells, and GFP was observed in the cells.The results of flow cytometry showed that the transfection efficiency of recombinant plasmid was 44.8%.Conclusion:The recombinant plasmid carrying hTERT-P2A-EGFP gene is successfully constructed, and it can be used for cell transfection.
4.Preparation and identification of the polyclonal antibody against the 3D polymerase of foot and mouth disease virus
Yu ZHANG ; Yonglu WANG ; Yongguang ZHANG ; Yuzhen FANG ; Li PAN ; Shoutian JIANG ; Jianliang LU ; Likuan LIU ; Zhongwang ZHANG ; Shugang ZHANG ; Zhengfeng LI ; Jinxin DU
Chinese Journal of Zoonoses 2010;(1):6-9
To prepare the polyclonal antibody against the 3D polymerase of foot and mouth disease virus (FMDV), the 3D polymerase gene of this virus was amplified by PCR and doubly digested with BamH I and Nde I. Then, it were cloned into expression vector pET-30a(+) to obtain the recombinant plasmid pET-3D and this plasmid was transformed to E.coli BL21(DE3) with induction by IPTG.The target protein was identified and purified with SDS+PAGE, and the inclusion bodies were extracted. The purified target protein was used as antigen to immunize New Zealand rabbits to prepare the polyclonal antibody against 3D polymerase of FMDV, which was then characterized by indirect ELISA and Western blotting. As demonstrated by SDS-PAGE, the target protein with a molecular weight at 46 ku was expressed. The polyclonal antibody showed high affinity and obvious specificity and its titer was above 1:8 000. This polyclonal antibody may lay a foundation for the further studies on the biological functions and epitopes of the 3D polymerase of FMDV.

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