Shan Qi soy has busting bags, bacteria sum overproof, continue acidification and other problems occasionally during the storage. It's probably caused by the Lactobacillus continue growth in the soy. We tried expounding the relationship between growth and producing acid when Lactobacillus growing in the thin fermented material.

To analyze and compare the protective effects of active components in different ethyl acetate extracts (EAEEPs) from Eclipta prostrate, in order to study the comparison of materials bases protecting normal human bronchial epithelial (NHBE) cells. The MTT assay was taken to compare the protective effect of different EAEEPs on cigarette smoke extracts (CSE) -induced NHBE cells. The ultra-performance liquid chromatography (UPLC) was applied to analyze the content of phenolic acid, coumaric grass ether and flavonoid in EAEEPs. According to the results, all of the eight EAEEPs (0-200 mg x L(-1)) showed certain protective effect on NHBE cells, with statistical difference. Specifically, the total mass of EAEEP VII (89.15 mg x L(-1)) and EAEEP VIII (57.44 mg x L(-1)), which showed the strongest activity, was not the highest, while EAEEP III (132.25 mg x L(-1)) displayed the highest total mass. In the combination with the "component structure" theory, the analysis showed a significant difference in the mass structure among phenolic acid, coumaric grass ether and flavonoid in EAEEP VIII and EAEEP VIII, which were 1.0: 1. 0: 0.5 and 1.0: 1.9: 0.8, respectively. The results suggested a specific optimal "component structure" relationship may exist in EAEEP, which could provide reference for the material base study and quality control.
Bronchi ; cytology ; drug effects ; Drugs, Chinese Herbal ; chemistry ; isolation & purification ; pharmacology ; Eclipta ; chemistry ; Epithelial Cells ; cytology ; drug effects ; Humans ; Protective Agents ; chemistry ; isolation & purification ; pharmacology ; Tobacco Smoke Pollution ; adverse effects

Objective To construct a Luciferace reporter vector containing the 3'untranslated region (3'UTR) of NFAT5 and measure the correlation between NFAT5 and miR-155.Methods The miR-155 targeting NFAT5 3'UTR was predicted by Target Scan,Mir Base and Pic Tar.NFAT5 and mutant NFAT5 sequence(NFAT5-mu) were then designed and synthesized,and they were cloned into pMIR-REPORTTM Luciferace reporter vector.Human embryonic kidney-293AD (HEK-293AD) cells of the 4th passage were divided into 4 groups according to the random number table.cells in plasimd +miR-155 mimics groups were transfected with pMIR-NFAT5 recombinant plasimid,pRL-Tk plasmid and miR-155 mimics;cells in plasimd + miR-155 mutated groups were transfected with pMIR-NFAT5-mu recombinant plasimid,pRL-Tk plasmid and miR-155 mimics;cells in plasimd + miR-155 control groups were transfected with pMIR-NFAT5 recombinant plasimid,pRL-Tk plasmid and miR-155 Negative control;cells in plasimd +miR-155 inhibitor were transfected with pMIR-NFAT5 recombinant plasimid,pRL-Tk plasmid and miR-155 inhibitor;and were respectively transfected into together by liposome.After culture for 24 h,the luciferase activity was detected by dual luciferase reporter assay system.Results TargetScan,Miranda and PicTar shared the results that NFAT5 has the complementary binding sites with 3'UTR of miR-155.And luciferase reporter vectorwas constructed.Therefore the result of sequencing and double digesting of recombined plasmid were completely correct.Dual-luciferase reporter assay showed that miR-155 possesses a target effect on 3'UTR of NFAT5.Compared to the pMIR-NFAT5 + miR-control group,the luciferase activity of the pMIR-NFAT5 + miR-1 5 5 mimics group was decreased,with statistically significant difference(P＜0.01),while there was no significant difference at other time points(P＞0.05).Conclusion The pMIR-NFAT5 recombinant plasmid and pMIR-NFAT5 recombinant mutated plasmid were confirmed with successful construction.and it was found that miR-155 can target NFAT5 mRNA 3'-UTR.The results provide the experiment data for further disclosing the mechanism of inhalation injury on the level of gene expression.

Adult ; Aged ; Bone Plates ; Dermatologic Surgical Procedures ; External Fixators ; Extremities ; injuries ; surgery ; Female ; Fracture Fixation ; Fractures, Bone ; surgery ; Humans ; Male ; Middle Aged ; Skin ; injuries ; Treatment Outcome ; Young Adult

Metastatic epidural compression of the spinal cord is a significant source of morbidity in patients with systemic cancer. With improvment of oncotheray, survival period in the patients is improving and metastatic cord compression is en- countered increasingly often. Surgical management performed for early circumferential decompression for the spinal cord com- pression with spine instability, and spine reconstruction performed. Patients with radiosensitive tumours without spine instabili- ty, radiotherapy is an effective therapy. Spinal stereotactic radiosurgery and minimally invasive techniques, such as vertebro- plasty and kyphoplasty, percutaneous pedicle screw fixation, radiofrequency ablation are promising options for treatment of cer- tain selected patients with spinal metastases.
Decompression, Surgical ; Humans ; Minimally Invasive Surgical Procedures ; Spinal Cord Compression ; therapy ; Spinal Neoplasms ; secondary ; therapy

OBJECTIVEUnder the premise of smoke inhalation injury, to explore the effects of microRNA-146a on Fas-associated factor 2 (FAF-2) and inflammatory factors in human lung adenocarcinoma A549 cells under the stimulation of cigarette smoke extract (CSE).

METHODS(1) The pMIR-FAF-2 recombinant plasmid and the pMIR-FAF-2 recombinant mutated plasmid were constructed. Human embryonic kidney 293 (HEK-293) cells of the third passage were divided into 3 groups according to the random number table, with 5 wells in each group. Cells in plasmid+ microRNA control group were transfected with pMIR-FAF-2 recombinant plasmid, pRL-TK plasmid, and microRNA control; cells in plasmid+ microRNA-146a group were transfected with pMIR-FAF-2 recombinant plasmid, pRL-TK plasmid, and microRNA-146a mimics; cells in mutated plasmid+ microRNA-146a group were transfected with pMIR-FAF-2 recombinant mutated plasmid, pRL-TK plasmid, and microRNA-146a inhibitor. After culture for 24 h, the relative luciferase activity in cells was assessed by dual-luciferase reporter gene assay. (2) Human lung adenocarcinoma A549 cells of the third passage were divided into 3 groups according to the random number table, with 4 wells in each group. Cells in microRNA control group were transfected with microRNA control; cells in microRNA-146a enhancement group were transfected with microRNA-146a mimics; cells in microRNA-146a inhibition group were transfected with microRNA-146a inhibitor. After culture for 24 h, the mRNA expression levels of microRNA-146a and FAF-2 in cells were determined with real-time fluorescent quantitative reverse transcription-PCR. (3) A549 cells of the third passage were stimulated by 0.8% CSE for 24 h after being divided and treated with the same method used in experiment (2). The mRNA expression levels of FAF-2, IL-8, monocyte chemotactic protein-1 (MCP-1), and growth-regulated oncogene-α (GRO-α) in cells were determined with real-time fluorescent quantitative reverse transcription-PCR. The protein expression levels of IL-8, MCP-1, and GRO-α in A549 cell culture supernatant were determined by enzyme-linked immunosorbent assay. The protein expression level of cyclooxygenase 2 (COX-2) of cells was assessed by Western blotting. Data were processed with one-way analysis of variance and LSD test.

RESULTS(1) The pMIR-FAF-2 recombinant plasmid and pMIR-FAF-2 recombinant mutated plasmid were confirmed with successful construction. The relative luciferase activity in HEK-23 cells of plasmid+ microRNA control group was close to that of mutated plasmid+ microRNA-146a group (P>0.05). The relative luciferase activity in HEK-23 cells of plasmid+ microRNA-146a group was significantly lower than that of plasmid+ microRNA control group and mutated plasmid+ microRNA-146a group (with P values below 0.01). (2) The expression level of microRNA-146a in A549 cells of microRNA control group was close to that of microRNA-146a inhibition group (P>0.05), and they were both significantly lower than the expression level of microRNA-146a in A549 cells of microRNA-146a enhancement group (with P values below 0.01). The mRNA expression level of FAF-2 in A549 cells of microRNA control group was close to that of microRNA-146a inhibition group (P>0.05), and they were both significantly higher than the mRNA expression level of FAF-2 in A549 cells of microRNA-146a enhancement group (with P values below 0.05). (3) After stimulation of CSE, the mRNA expression level of FAF-2 in A549 cells of microRNA control group (1.46±0.21) was close to that of microRNA-146a inhibition group (1.43±0.34, P>0.05), which were both significantly higher than the mRNA expression level of FAF-2 in A549 cells of microRNA-146a enhancement group (0.57±0.11, with P values below 0.05). The mRNA expression levels of IL-8, MCP-1, and GRO-α in A549 cells of microRNA-146a enhancement group were significantly lower than those of microRNA control group and microRNA-146a inhibition group (with P values below 0.01). The mRNA expression levels of IL-8, MCP-1, and GRO-α in A549 cells of microRNA-146a inhibition group were significantly higher than those of microRNA control group (with P values below 0.05). The protein expression levels of IL-8, MCP-1, and GRO-α in A549 cell culture supernatant of microRNA-146a enhancement group were significantly lower than those of microRNA control group and microRNA-146a inhibition group (with P values below 0.05). The protein expression level of IL-8 in A549 cell culture supernatant of microRNA-146a inhibition group was close to that of microRNA control group (P>0.05), while the protein expression levels of MCP-1 and GRO-α in A549 cell culture supernatant of microRNA-146a inhibition group were significantly lower than those of microRNA control group (with P values below 0.05). The protein expression level of COX-2 in A549 cells of microRNA-146a enhancement group was significantly lower than the levels of microRNA control group and microRNA-146a inhibition group (with P values below 0.05). The protein expression level of COX-2 in A549 cells of microRNA control group was close to that of microRNA-146a inhibition group (P>0.05).

CONCLUSIONSIn A549 cells, after being transfected with microRNA-146a and stimulated by CSE, microRNA-146a can decrease the expression of FAF-2 through integrating with the 3'-untranslated region of target gene FAF-2, thereby decrease the expression of inflammatory factors.

Adenocarcinoma ; chemically induced ; Blotting, Western ; Chemokine CCL2 ; metabolism ; Enzyme-Linked Immunosorbent Assay ; HEK293 Cells ; Humans ; Interleukin-8 ; Lung ; drug effects ; metabolism ; Lung Neoplasms ; chemically induced ; MicroRNAs ; analysis ; Plasmids ; RNA, Messenger ; Smoke ; adverse effects ; Smoking ; Transfection

Adult ; Electrocoagulation ; methods ; Female ; Humans ; Injections ; Intervertebral Disc Displacement ; therapy ; Lumbar Vertebrae ; Male ; Middle Aged ; Ozone ; administration & dosage ; Radio Waves ; therapeutic use

Objective To investigate bone mineral density ( BMD ) after filling in the bone scaffolds with anti-tuberculosis controlled-release microspheres, and provide experimental basis for decrease of the side effects of anti-tuberculosis therapy after spinal surgery.Methods The bone densitometer was used to observe the changes of bone mineral density before and after the infusion with the artificial allograft bone (Group A), the controlled release complex of the RFP controlled-release microspheres-artificial allograft bone (Group B), and RFP-artificial allograft bone complex (Group C), respectively.Results BMDs of three groups before perfusion were not different significantly [Group A:(0.191 ±0.018)g/cm2;Group B:(0.186 ±0.016)g/cm2;Group C:(0.189 ±0.018)g/cm2;P >0.05].BMDs of three groups after perfusion were not different significantly [Group A:(0.191 ±0.018)g/cm2;Group B:(0.179 ±0.023)g/cm2;Group C:(0.185 ±0.021)g/cm2;P >0.05].Conclusions RFP microspheres using ultrasonic vibration method and the porous bone were prepared to controlled-release anti-tuberculosis complex .BMD of three groups after perfusion were not influenced obviously .

Anemia, Hemolytic ; etiology ; Child ; Female ; Humans ; Insecticides ; poisoning ; Trichlorfon ; poisoning

Objective To investigate the effect of triggering receptor expression in myeloid cells-1 (TREM-1) on intestinal macrophage apoptosis in rat.Methods In vitro,the achieved rat intestinal macrophages were divided into 3 groups:control group,LPS (Lipopolysaccharides) group and LPS + LP17 group (n =6 holes of culture plate in each).The concentrations of LPS and LP17 were 1 mg/L and 0.1 mg/L,respectively.The intestinal macrophage apoptosis was measured by using TUNEL kit and flow cytometry after culture for 6 h.All data were statistically analyzed using SPSS 18.0 software.Results The shape and growth of rat intestinal macrophages were quite favorable after culture.The membrane marker of intestinal macrophages,CD14 was clearly observed under immunofluorescence.After macrophage was treated with specific procedure,the cell apoptosis found in LPS group (44.33 ± 7.74)％ was significantly higher than that in control group (19.17 ± 6.01) ％ (P=0.000) measured by TUNEL;the cell apoptosis in LPS +LP17 group (28.33 ± 6.53)％ apparently reduced compared with LPS group (44.33 ±7.74) ％ (P =0.004);there was no significant difference in cell apoptosis between control group (19.17 ± 6.01) ％ and LPS + LP17 group (28.33 ± 6.53) ％ (P =0.050).By flow cytometry,the apoptotic cells in LPS group (16.47 ± 1.66) ％ was significantly increased compared with control group (7.70 ± 1.52) ％ (P =0.000);apoptotic cells in LPS + LP17 group (11.47 ± 3.12) ％ was significantly reduced in comparison with LPS group (16.47 ± 1.66) ％ (P =0.018).There was no significant difference in apoptotic cells between control group (7.70±1.52)％ and LPS + LP17 group (11.47±3.12) ％ (P =0.061).Conclusion LP17 can inhibit TREM-1 expression in intestinal macrophages and reduce intestinal macrophage apoptosis.