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Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of South-Central Minzu University (Natural Science Edition) is the property of Journal of South-Central Minzu University (Natural Science Edition) Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective: To investigate the effect of cystathionine β-synthase (CBS) on the proliferation of lung adenocarcinoma A549 cells through the AKT/cyclin D1 pathway and its molecular mechanism. Methods: Expression of CBS and AKT/cyclinD1-related proteins in lung adenocarcinoma tissues was analyzed by cBioPortal database. The CBS expression in collected lung adenocarcinoma tissues from Chinese patients was verified by immunofluorescence method. WB assay was performed to detect the expression of cysteine metabolism and AKT/cyclin D1 pathway-related proteins in A549 cells and their transplanted tumors, and CBS DNA methylation sequencing was performed to detect the effect of its methylation on CBS mRNA expression in lung cancer cells. The pCW57.1-myrAKT plasmid was co-transfected with RNA interference control plasmid pGIPZ-CBS-nc-shRNA, interference plasmid pGIPZ-CBS-shNRA1 and pGIPZ-CBS-shNRA2, respectively, into A549 cells, which were further sub-divided into DOX+ and DOX- groups. The colony formation ability of A549 cells in each group after transfection was examined by cell colony formation assay. The effect of overexpression of CBS on the growth of transplanted tumors was examined by CBSwtA549 cell- and CBSI278TA549 celltransplanted tumor assay, and AzMC fluorescence staining and immunohistochemistry were used to detect H2S levels and Ki-67 positivity in transplanted tumor tissues, respectively. Results: Both database analysis and tissue specimens showed that CBS was lowly expressed in lung adenocarcinoma tissues compared with para-cancerous tissues (all P<0.01); CBS protein was lowly expressed in A549, SKMES1 and NCIH460 cells compared with SV-40 cells (all P<0.01), while p-AKT and cyclin D1 protein levels were highly expressed (all P<0.01). Overexpression of AKT in A549 cells significantly promoted the formation of cell colonies (P<0.01), and knockdown of CBS on this basis further promoted the formation of cell colonies (all P<0.01). Transplantation tumor experiments showed that CBS, RB and P21 protein expression was elevated, H2S level was increased, tumor volume was decreased and Ki-67 positivity was reduced in the DOX+ CBSWT group compared with those in the DOX- CBSWT group (all P<0.01); CBS expression was elevated in the DOX+ CBSI278T group compared with the DOX-CBSI278T group (P<0.01), but the changes in H2S level and transplantation tumor volume were not significant. Conclusions: CBS is lowly expressed in lung adenocarcinoma tissues and A549 cells, while the AKT/cyclinD1 pathway is activated. Overexpression or knockdown of CBS can inhibit or promote the growth of A549 cells and their transplanted tumors, and CBS and AKT/cyclin D1 pathway-related proteins may be the potential targets and markers for lung adenocarcinoma. [ABSTRACT FROM AUTHOR]

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective To investigate the role of autophagy in hypoxia-activated CaSR(calcium-sensing receptor,CaSR) in mediating migration of A549 cells. Methods A549 cells in the logarithmic growth phase were randomly divided into control group(N), hypoxia group (H), hypoxia agonist group (H+Gd), hypoxia inhibitor group (H+NPS), and autophagy pathway inhibitor group (H+Gd+3-MA).Western blot was used to detect the expression of CaSR and autophagy protein (Beclin-1) in the cells; Cell scratch experiment was used to detect migration of A549 cells; Transwell assay was applied to evaluate the invasion of A549 cells. Results Hypoxia resulted in increased CaSR expression in A549 cells (P＜0.05), a decreased expression of autophagic effector protein Beclin-1(P＜0.05), increased the percentage of cell healing per unit time (P＜0.05), and the number of cell invasion-permeable membranes (P＜0.05).GdCl3 strengthened the effect of hypoxia, while NPS2390 did weaken the effect of hypoxia. On the basis of hypoxia and GdCl3 conditions, 3-MA further increased the expression of metastasis related indicators of A549 cells, but not the autophagy related indicators. Conclusions CaSR activation promotes migration and invasion of A549 cells by down-regulating autophagy.

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective: To investigate the effect of lncRNA MAFG antisense RNA1 (lncRNA MAFG-AS1) regulating miR-532-3p on the glycolysis of lung cancer A549 cells. Methods: The expression levels of MAFG-AS1 and miR-532-3p in human lung cancer A549 cells and normal lung epithelial BEAS-2B cells were detected by qPCR. A549 cells with MAFG-AS1 downregulation or miR-532-3p overexpression were constructed by liposome transfection technique, respectively. The glucose consumption and lactate secretion in cell culture supernatant of A549 cells were detected by visible spectrophotometry, and the mRNA and protein expression levels of pyruvate kinase M2 (PKM2) and hexokinase 2 (HK2) in A549 cells were detected using qPCR and WB, respectively. The targeting relationship between MAFG-AS1 and miR-532-3p was verified by Dual luciferase reporter gene assay, and the effects of co-downregulation of MAFG-AS1 and miR-532-3p on glucose uptake, lactate secretion and expression of PKM2 and HK2 in A549 cells were observed. Results: Compared with BEAS-2B cells, the expression of MAFG-AS1 was upregulated while miR-532-3p expression was downregulated in A549 cells (all P<0.01). Glucose consumption, lactate secretion and the protein and mRNA expressions of PKM2 and HK2 were inhibited by MAFG-AS1 downregulation or miR-532-3p overexpression (all P<0.01). miR-532-3p could bind to MAFG-AS1 and inhibit the luciferase activity of wild-type MAFG-AS1 cells (P<0.01). Downregulation of MAFG-AS1 could increase the expression of miR-532-3p (P<0.01), while the co-downregulation of miR-532-3p could reverse the effect of MAFG-AS1 downregulation on glucose uptake, lactate secretion and the expression of PKM2 and HK2 in A549 cells (all P<0.01). Conclusion: Downregulation of MAFG-AS1 can inhibit the glycolysis of A549 cells by promoting the expression of miR-532-3p. [ABSTRACT FROM AUTHOR]

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective: To investigate the effects of overexpressed miR-497 targeting cyclin E1 (CCNE1) on epithelial-mesenchymal transition (EMT) in lung cancer A549 cells. Methods: Human lung cancer A549 cells were routinely cultured, and the experimental cells were divided into normal group (without any intervention), control group (transfected with miR-497 mimics-NC), and experiment group (transfected with miR-497 mimics). Transwell chamber experiment, immunofluorescence staining, qPCR, Western blotting were used to detect cell migration and invasion ability, the expressions of protein interstitial marker α-SMA and epithelial marker E-cadherin, and the expressions of miR-497 and CCNE1 in each group of cells, respectively. Dual luciferase reporter gene assay was used to verify the relationship between miR-497 and CCNE1. Results: Compared with the normal group, the number of migrated and invaded cells in the experiment group decreased significantly (all P<0.05), the green fluorescence intensity of the interstitial marker α-SMA of the experimental group cells was significantly weakened [(36.95±5.81) vs (98.69±2.36), (97.94±2.63), all P<0.05], while the green fluorescence intensity of the epithelium marker E-cadherin was significantly enhanced [(388.41±10.93) vs (100.95±6.37), (102.55±3.18), all P<0.05]; in addition, the expression of miR-497 in the cells of the experiment group was significantly increased (all P<0.05), while theexpression of CCNE1 was significantly decreased (all P<0.05). miR-497 could targetedly regulate the expression of CCNE1. Conclusion: In lung cancer A549 cells, miR-497 can targetedly regulate CCNE1 expression. Up-regulating the expression of miR-497 can significantly inhibit the migration and invasion ability of A549 cells and affect the expression of EMT related protein. [ABSTRACT FROM AUTHOR]

Objective: The phosphorproteomics technique was used to analyze the differential expression of phosphorylated proteins in the human lung adenocarcinoma A549 cells treated with antimicrobial peptide merecidin, and to explore the effect of merecidin on the protein activity and function of lung adenocarcinoma A549 cells and the signal pathway involved. Methods: A549 cells were treated with 9 μmol/L merecidin for 6 h. The total protein was collected and extracted, and SDS-PAGE experiment was used to test the total protein extraction efficiency. Pancreatin was added to digest the protein. The peptides obtained by enzymatic hydrolysis were labeled with TMT, fractionated by HPLC, enriching phosphorylated modified peptides by IMAC, and separate peptides by HPLC-MS/MS (liquid chromatographymass spectrometry) technology. The identified data were screened using the standard of localization probability>0.75, and the phosphoproteomics data were analyzed using GO (Gene Ontology) database, KEGG (Kyoto Encyclopedia of Genes and Genomes) database and STRING database. Results: SDS-PAGE results showed that the total protein separation of A549 cells treated with 9 μmol/L merecidin was clear and no obvious degradation, and there was significant difference in protein bands between the experimental group and the control group. A total of 10 320 phosphorylation modification sites on 3 089 proteins were identified by mass spectrometry, of which 753 proteins and 1 172 phosphorylation sites were screened out with |Fold Change| >1.5 and P<0.05 as the threshold. Protein function enrichment showed that functions of proteins with significant changes in phosphorylation level mainly focused on molecular binding, metabolic activity, molecular function regulation, cell process, biological function and other aspects. Bioinformatics results of integrated pathway showed that differentially expressed proteins were associated with Ras, PI3K/AKT, mTor, AMPK etc. COG database screening showed that the differentially expressed phosphorylated proteins were concentrated in cell signal transduction, processing and modification of RNA transcription and translation, protein synthesis of ribosome, formation of cytoskeleton proteins, intracellular substance transportation, secretion and vesicle transportation etc. At the protein interaction level, after merecidin treatment, an interaction network with MAPK1, RPL23A, SRSF3H, NCBP1, etc. as key proteins was formed in A549 cells; proteins such as ATG2B and ULK1 etc. were significantly up-regulated, while proteins such as MAPK1 and AKT1 etc. were significantly down-regulated. Conclusion: Phosphoproteomic analysis shows that the antimicrobial peptide merecidin may play a role in multiple biological functions and multiple signaling pathways through key proteins such as MAPK1, RPL23A, SRSF3H and AKT1, and promote the apoptosis and autophagy of lung adenocarcinoma A549 cells, thereby inhibiting cell proliferation. [ABSTRACT FROM AUTHOR]

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective: To investigate the effects of miR-625 and Resistin on the proliferation, invasion and migration of NSCLC cells as well as the growth of transplanted tumors in nude mice and their possible mechanisms. Methods: qPCR was used to detect the expression of miR-625 and Resistin in 80 pairs of NSCLC and corresponding para-cancerous tissues (specimens collected from NSCLC patients who were surgically treated in Xinjiang Uygur Autonomous Region People' s Hospital from March 2018 to October 2019) and four cell lines. Bioinformatics was adopted to predict the targeting relationship between miR-625 and Resistin, which was then verified by Dual luciferase gene reporter experiment. Overexpression or inhibition of miR-625 and Resistin in NSCLC cells was achieved with lipofection transfection technology, and the experimental cells were divided into miR-625 mimic group, miR-625 inhibitor group, si-Resisitin group, miR-625 inhibitor+si-Resisitin group and NC group. The effects of miR-625 and Resistin on proliferation, invasion and migration of NSCLC cells were detected by CCK-8, Transwell and Scratch test, respectively. Western blotting was used to detect the effects of miR-625 and Resistin on the expressions of PI3K/AKT/Snail pathway proteins related with EMT in NSCLC cells. A549 cell transplanted tumor model was constructed in nude mice to observe the effect of miR-625 and Resistin on the growth of xenografts. Results: Compared with para-cancerous tissues, miR-625 showed low expression while Resistin showed high expression in NSCLC tissues and four cell lines (both P<0.01), and the two were negatively correlated (r=-0.7183, P<0.01). The expression of Resistin was related to the degree of NSCLC differentiation, clinical stage and lymph node metastasis. Resistin was a target gene of miR-625. Compared with the Blank group and NC group, the proliferation, invasion and migration of NSCLC cell lines A549 and H226, as well as the growth of transplanted tumors in nude mice in the miR-625 mimic group and the si-Resistin group were significantly reduced (all P<0.05), while those indicators in the miR-625 inhibitor group were significantly improved (all P<0.05); However, co-transfection of miR-625 inhibitor and si-Resistin significantly reversed the effect of miR-625 inhibitor on above indicators (all P<0.05); And there was no significant difference between NC group and miR-625 inhibitor+si-Resistin group (all P >0.05). The protein expressions of p-AKT, p-PI3K, Snail, Twist1 and Vimentin also showed the same trend (all P<0.05), while the expression of E-cadherin protein changed in the opposite direction (P<0.05). Conclusion: miR-625 is lowly expressed in NSCLC tissues and cell lines, which can negatively regulate Resistin expression to inhibit the proliferation, invasion and migration of NSCLC cells and the growth of transplanted tumors in nude mice. The mechanism may be related to the PI3K/AKT/Snail signaling pathway. [ABSTRACT FROM AUTHOR]

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective To investigate the effect of siRNA silencing BAZ1A on radiosensitization of human lung adenocarcinoma A549 cells. Methods A549 cells were randomly divided into transfection reagent control (Ctrl) group, negative control siRNA (siNC) group, and siBAZ1A group. The expression of BAZ1A protein was evaluated by Western blot. The clone formation assay was applied to investigate the survival fraction (SF) of the A549 cells treated with different radiation doses (0, 2, 4, 6, 8, and 10Gy), and one-hit multi-target model was applied to analyze the radiation dose survival curve. MTS assay, scratch assay, and flow cytometry were utilized to determine the relative survival, cell migration abilities, and apoptosis, respectively. Results The expression level of BAZ1A protein in A549 cells was inhibited by BAZ1A-siRNA transfection. X-ray radiation inhibited the colony formation capacity of A549 cells, and the SF of siBAZ1A group was lower than that of the other two groups with radiation (P<0.05). Compared with those of Ctrl group, the sensitization enhancement ratio (SER) of siNC and siBAZ1A groups was 1.06 and 2.24. Moreover, with the transfection of BAZ1A-siRNA, the relative survival rate and cell migration ability were decreased after X-ray radiation. Besides, the apoptosis rate was higher in siBAZ1A group (P <0.05). Conclusion Silencing the expression of BAZ1A by siRNA can efficiently improve the sensitization of radiotherapy for A549 cells. [ABSTRACT FROM AUTHOR]

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Cancer Biotherapy is the property of Editorial Office of Chinese Journal of Cancer Biotherapy and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective: To study the role and mechanism of AFAP1 in A549 cells senescence induced by bleomycin. Methods: A549 cells were exposed to bleomycin and then p21 and SA-β-Gal positive proportion which are markers of cellular senescence were evaluated AFAP1 was overexpressed in A549 cells, the expression of p21, AFAP1 and c-Src were detected by western blot Results: AFAP1 expression was decreased in senescent A549 cells, the change of which was consistent with activated c-Src (Src pY416). However, there was few variations in total c-Src as well as inhibited c-Src (Src pY527). There was no difference in the p21, Src pY416 and senescent pheuotype between AFAP1-overexpressed cells and vehicle vector transfected control. Conclusion: AFAP1 expression decreased in senescent A549 cells induced by BLM, overexpression of AFAP1 could not alleviated the senescent phenotype and downstream molecular activated c-Src. [ABSTRACT FROM AUTHOR]

Objective: To study the effect of Kaempferol on the proliferation of human alveolar adenocarcinoma cell line A549. Methods: A549 cells was treated with different concentrations of Kaempferol(0, 5. 10. 20. 50 µg-mL-1). MTT assay and plate cloning experiments were contributed to study the effect of Kaempferol on the cell proliferation. The nucleolus transcription level was detected by real-time polymerase reaction experiment. Western blot was performed to detect the phosphorylation of upstream binding factor (UBF) protein. Results: MTT assay and plate cloning experiments showed that Kaempferol significantly decreased the viability of A549 cells in a dose dependent maimer. Moreover, Keampferol down-regulated the level of nucleolus transcription, declined the phosphorylated UBF protein level. Conclusions: Keampferol could inhibit the proliferation of A549 cells, which might be related to the down-regulation of pre-rRNA and p-UBF protein level. [ABSTRACT FROM AUTHOR]

Objective: To investigate the effects of early growth respons-1 (Egr-1) gene silence on the radiosensitivity of human lung adenocarcinoma A549 cells. Methods: The A549 cell line was selected and divided into the blank control group (only to join the RPMI-1640 Culture), the negative control group (to join LV3-NC-shRNA), the experimental group (to join EGRl-homo-2294-shRNA), Egr-1 gene expression was silenced in the experimental group with the ShRNA interference technique mediated by lentiviral vector. SliRNA transfection was analyzed by fluorescence microscopy and automated fluorescence quantitative cell imaging analysis system. The expression of Egr-1 was analyzed by FQ-PCR. And the difference of parameters of cell radiation sensitivity was detected by cell cloning experiment. Results: The negative control group and the experimental group cells were successfirlly transfected with the shRNA by lentiviral vector. There was no difference in the Egr-1 expression between the blank control group and the negative control group (P>0. 05). Compared with the blank control group and negative control group, the Egr-1 expression was significantly inhibited (P<0.05), the cell radiosensitivity parameters of DO and SF2 in the clone formation experiment also showed significant differences in the experimental group(P<0.05). Conclusion: Egr-1 gene silence reduced the radiosensitivity of A549 cells and the expression of Egr-1 was correlated with the radio sensitivity of tumor cells. [ABSTRACT FROM AUTHOR]

Objective To explore the effect of obstructive sleep apnea syndrome (OSAS), OSAS-like intermittent hypoxia (IH）on the expression levels of P -YAP and YAP in A549 lung cancer cell lines. Methods A549 cells were treated with IH exposure ( exposed to 5% O2 for 300 seconds and 21% O2 for 300 seconds) for 1, 3 and 6 h (IH1, IH3, IH6) or normoxia exposure (N group). Quantificational real-time PCR was used to measure the mRNA expression levels of YAP. Western blot assay was used to detect the protein expression levels of YAP and P-YAP. Results The mRNA expression levels of YAP were significantly increased with the increase of IH exposure time points in IH1 (2.50±0.18), IH3 (4.07±0.25) and IH6 (9.18±0.58) groups than those in N group (1.00±0.01) (all P＜0.05). The protein expression levels of YAP were significantly increased with the increase of IH exposure time points in IH1, IH3 and IH6 groups than those in N group. The protein expression levels of P-YAP were significantly decreased with the increase of IH exposure time points in IH1, IH3 and IH6 groups than those in N group. Conclusion YAP cell signaling plays an important role in the process of OSAS-like IH induced tumor development. [ABSTRACT FROM AUTHOR]

Background and objective Recent studies have shown that integrin α5β1 as a core in the integrin family plays an important role in metastasis, invasion and poor difference of non-small cell lung cancer. In this study, A549 cells were cultured and treated with integrin α5β1 small interfering RNA (siRNA) and extracelluar signal-regulated protein kinase (ERK) inhibitor PD98059 to investigate the effect of integrin α5β1 on proliferation and migration of A549 cells and explore its signal transduction mechanism. Methods A549 cells were divided into four groups: Untransfection, Lipofectamine, Integrin α5β1 siRNA-transfected group and PD98059 group. The protein expression levels of integrin α5β1 were detected by Western blot analysis and the expression levels of integrin α5β1 mRNA was measured by reverse transcription-polymerase chain reaction (RT-PCR). The protein expression level of ERK1/2, MMP-9 and caspase-3 were measured by Western blot analysis. The proliferation and apoptosis of A549 cells were measured by MTT assay and Annexin-V FITC PI double staining. Results Integrin α5β1 siRNA could inhibit the phosphorylated ratio of ERK by down-regulate the expression of ERK 1/2 proteins. In addition, integrin α5β1 siRNA or PD98059 could inhibit the proliferation of A549 cells, induce the apoptosis of A549 cells, up-regulate the expression of caspase-3 and down-regulate the expression of MMP-9. Conclusion Integrin α5β1 might involves the abnormal proliferation and migration of A549 cells through mediating ERK signal transduction pathway.

This study focuses on the therapeutical effect of flavonoids from Gynostemma pentaphyllum on human lung carcinoma A549 cells induced by H₂O₂ oxidative stress and its possible mechanisms. The oxidative damage model was established using different concentrations H₂O₂ to induce A549 cell for different hours, and then treated with the flavonoids for 10 hours. The effects of flavonoids from G. pentaphyllum on cell viability of A549 cell damaged by H₂O₂ were detected by MTT assay. The contents of ROS were detected by DCFH-DA fluorescent probe method via flow cytometer. The contents of MDA, SOD and GSH were detected by TBA，NBT and DTNB-linked colorimetry assay, respectively. Expressions levels of Nrf2, NQO1 and HO-1 in A549 cells were evaluated by Western blot. The results showed that the cell activity was decreasing with the rise of H₂O₂ concentration within the range of 200-700 μmol·L⁻¹. The cell viability was 60.4% after treated with 500 μmol·L⁻¹H₂O₂ for 10 h, so it was chosen to be as an oxidant stress model. Compared with normal group，the contents of SOD, GSH and HO-1 expressions were lower after damaged with H₂O₂. On the contrary, the contents of ROS and MDA expressions were increased. Compared with model group, the contents of SOD, GSH and the expressions of Nrf2, NQO1 and HO-1 were increased after treated with flavonoids from G. pentaphyllum. The above results demonstrate that flavonoids from G. pentaphyllum may attenuate the effect of H₂O₂-induced oxidative stress on A549 cell by resisting oxidation. The finding may provide a biological evidence for the application of the G. pentaphyllum to fight the oxidative stress related diseases., Competing Interests: The authors of this article and the planning committee members and staff have no relevant financial relationships with commercial interests to disclose., (Copyright© by the Chinese Pharmaceutical Association.)

Objectives: To investigate the effects of dexmedetomidine (Dex) on injury of A549 cells induced by hypoxia/reoxygenation(H/R)and the influence of C/EBP homologous protein (CHOP) expression., Methods: Logarithmic growth phase A549 cells(it originated from alveolar type Ⅱ epithelial cell line) were randomly divided into 4 groups ( n =10):normoxic control group (N), Dex group (D), hypoxia/reoxygenation group (H), hypoxia/reoxygenation + Dex group(HD). At the beginning of modeling, 1 nmol/L Dex was puted into D and HD groups. N and D groups were cultured in the normoxic incubator for 30 h. H and HD group were incubated in the anoxic cultivation for 6 h, fo llowed by normoxic culture for 24 h. Then A549 cells were observed under the inverted microscope to observe the morphological changes. Cell activity was detected by cell counting Kit-8(CCK-8) and the apoptosis index(AI) was detected by in situ end labeling (TUNEL) method. The expression of CHOP、glucose-regulated protein of molecular weight 78 kDa (Grp78)、cysteinyl aspirate-specificprotease-3 (caspase-3) protein and CHOP、Grp78 mRNA were detected by Western blot and RT-PCR., Results: Compared with N group, the number of adherent cells in H group decreased significantly, and cell morphology changed. The absorbance value in H group decreased obviously ( P <0. 01). The AI value and expression of CHOP, Grp78, caspase-3 proteins and CHOP, Grp78 mRNA were significantly increased ( P <0.01). Compared with H group, the cell damage in HD group was decreased, the absorbance value increased ( P <0.01), the number of apoptosis cells decreased relatively ( P <0.01), the expression of CHOP, caspase-3 protein and CHOP mRNA decreased ( P <0. 01)., Conclusions: Dex has notable effects against H/R injury, which may be related to effective inhibition of apoptosis mediated by the CHOP's signal path.

Objective: Construct a paraquat (PQ) cell fibrosis model in vitro, observe the effect of PQ on the expression of a disintegrin and metalloproteinase-17 (ADAM17) in A549 cells, and explore the role of ADAM17 in the pulmonary fibrosis induced by PQ poisoning. Methods: A549 cells are divided into normal control group, different concentration of PQ groups, CCK-8 is used to detect cell viability, screening concentration and time of PQ, cell morphology is observed under microscope; Enzyme-linked immunosorbent assay (ELISA) detectes fibrosis markers of collagen type I (Col I) and fibronectin (FN) expression. Establishment of cell model of fibrosis; distribution by immunocytochemical detection of ADAM17 in A549 cells, Reverse transcription-polymerase chain reaction and Western blot are used to detect the expression of ADAM17 mRNA and protein. Results: 1. With the increase of PQ concentration and the prolongation of the action time, the activity of A549 cells decreased ( P < 0.05) , which is dose-dependent and time dependent. 2.The normal A549 cells fusion is paving stone growth and arranged more closely. After PQ induction, the cell arrangement was loose, the intercellular connection became loose, and some cells dissolved and died. 3.ELISA showed that with the increase of PQ concentration, the expression of Col I and FN increased ( P <0.05) , and Col I and FN expression gradually increased with the prolongation of PQ time ( P <0.05) , and the fibroblast model is successfully established. 4. Immunocytochemistry showes that ADAM17 is expressed in the cytoplasm of A549 cells. 5. RT-PCR and Western blot showed that the expression of ADAM17 mRNA and protein increased significantly with the increase of PQ concentration ( P <0.05) , which is most obvious at PQ 200 μmol/L. With the prolonged action of PQ, the expression level of ADAM17 mRNA and protein also increased significantly ( P <0.05) , and reached the peak in 24 h. Conclusion: PQ can induce morphological changes of alveolar epithelial cells, cause cell damage, and successfully establish a cell fibrosis model, which has a dose and time dependence on the toxicity of A549 cells. ADAM17 is overexpressed in the A549 cells induced by PQ and may be involved in the process of pulmonary fibrosis induced by paraquat.