Publications by authors named "Mingcai Wu"

7 Publications

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Fusion proteins of biologic agents in the treatment of rheumatoid arthritis (RA): A network meta-analysis.

Medicine (Baltimore) 2021 Jun;100(24):e26350

Department of Epidemiology and Biostatistics.

Background: To evaluate the efficacy of fusion proteins biologics (Etanercept (ETN), Anakinra (ANA), and Abatacept) combinations in the treatment of rheumatoid arthritis (RA) using network meta-analysis to rank those according to their performance medicines. The performance of these processes is ranked according to the results of the analysis and an explanatory study of the possible results is carried out.

Methods: Multiple databases including PubMed, EMBASE, and Cochrane Library were used to identify applicable articles and collect relevant data to analyze using STATA (14.0) software. The literature included in this study was divided into a combination of a placebo, methotrexate (MTX), and an observation group (1 of the 3 drugs). The last search date was December 12, 2019.

Results: A total of 19 eligible randomized controlled trials of fusion proteins biologics were identified, a total of 1109 papers were included, and the results showed that the ETN + MTX had the highest probability of being the most clinically efficacious intervention, with a surface under the cumulative ranking curve of 91.6, was significantly superior (P < .05). Patients who had received ETN or ETN + MTX or ANA had effective compared with patients who had received placebo (95% CI 1.28%-8.47%; 1.92%-19.18%; 1.06%-10.45%).

Conclusions: 1. The combination of ETN and MTX had the highest probability of optimal treatment compared to other drugs and 2. ENT, ENT + MTX, and ANA were effective in the treatment of RA compared to placebo.
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http://dx.doi.org/10.1097/MD.0000000000026350DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8213327PMC
June 2021

Epigallocatechin Gallate Enhances Inhibition Effect of DDP on the Proliferation of Gastric Cancer BGC-823 Cells by Regulating p19Arf-p53-p21Cip1 Signaling Pathway.

Asian Pac J Cancer Prev 2021 Apr 1;22(4):1263-1270. Epub 2021 Apr 1.

Department of Biochemistry and Molecular Biology, Wannan Medical College, Wuhu, China.

Objective: To indicate the effect of Epigallocatechin gallate (EGCG) and Cisplatin (DDP) on proliferation of gastric cancer BGC-823 cells and the relative underlying mechanism.

Methods: Cultured BGC-823 cells were treated by 5 μg/mL DDP, 25 μg/mL EGCG and combined 5 μg/mL DDP with 25 μg/mL EGCG, a blank group was used as control. Cell morphology was observed by 4',6-diamidino-2-phenylindole (DAPI) staining. The ability of cell proliferation was detected by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT)assay. The cell cloning rate was determined by colony formation assay. The ability of cell migration was detected by cell scratch test. The cell cycle distributions and apoptosis were analyzed by flow cytometry, The expression of p19Arf, p53, p21Cip1 mRNA was determined by RT-qPCR. The protein levels of p19Arf, p53, p21Cip1 were measured by Western blot.

Results: Compared with DDP or EGCG treatment alone, EGCG combined with DDP treatment significantly caused nuclear shrinkage, reduced the proliferation rate, the ability of cell clone and migration. EGCG combined with DDP treatment caused cell cycle arrest in G1 phase in BGC-823 cells, increase of apoptosis (21.3%) vs EGCG (7.25%) and DDP (3.86%) single-use group (p <0.01), up-regulated gene and protein expressions of p19Arf, p53, p21Cip1 (p <0.01).

Conclusion: EGCG can enhance the effect of DDP on inhibiting BGC-823 cell proliferation and inducing apoptosis via activating the p19Arf-p53-p21Cip1 signaling pathway.
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http://dx.doi.org/10.31557/APJCP.2021.22.4.1263DOI Listing
April 2021

[Epigallocatechin gallate induces gene demethylation to promote acute myeloid leukemia cell apoptosis by regulating p19-p53-p21 signaling pathway].

Nan Fang Yi Ke Da Xue Xue Bao 2020 Sep;40(9):1230-1238

Department of Biochemistry and Molecular Biology, Wannan Medical College, Wuhu 241002, China.

Objective: To investigate the mechanism by which epigallocatechin gallate (EGCG) induces gene demethylation and promotes the apoptosis of acute myeloid leukemia KG-1 and THP-1 cell lines.

Methods: KG-1 and THP-1 cells treated with 25, 50, 75, 100 or 150 μg/mL EGCG for 48 h were examined for gene methylation using MSP and for cell proliferation using MTT assay. The changes in cell cycle and apoptosis of the two cell lines after treatment with EGCG for 48 h were detected using flow cytometry. The mRNA and protein expressions of DNMT1, CHD5, p19, p53 and p21 in the cells were detected using RT-quantitative PCR and Western blot.

Results: EGCG dose-dependently reversed hypermethylation of gene and reduced the cell viability in both KG-1 and THP-1 cells ( < 0.05). EGCG treatment caused obvious cell cycle arrest in G1 phase, significantly increased cell apoptosis, downregulated the expression of DNMT1 and upregulated the expressions of CHD5, p19, p53 and p21 in KG-1 and THP-1 cells ( < 0.05).

Conclusions: EGCG reduces hypermethylation of gene in KG-1 and THP-1 cells by downregulating DNMT1 to restore its expression, which results in upregulated expressions of p19, p53 and p21 and induces cell apoptosis.
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http://dx.doi.org/10.12122/j.issn.1673-4254.2020.09.02DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7544577PMC
September 2020

Cryptochrome 1 Alleviates the Antiproliferative Effect of Isoproterenol on Human Gastric Cancer Cells.

Dose Response 2020 Jul-Sep;18(3):1559325820939022. Epub 2020 Jul 9.

Province Key Laboratory of Active Biological Macro-molecules, Wannan Medical College, Wuhu, Anhui, China.

Background: Cryptochrome 1 (CRY1) is a key protein that regulates the feedback loop of circadian clock. The abnormal expression of CRY1 was reported in numerous cancers, and contributed to tumorigenesis and progression. But the underlying mechanism remains undefined.

Methods: overexpression was constructed by lentivirus vector. Gene and protein expression was detected by reverse transcription quantitative polymerase chain reaction and Western blot. Cell proliferation was analyzed by CCK-8 assay. Cell migration ability was analyzed by scratch assay and transwell migration assay. The cAMP concentration was measured by intracellular cAMP assay.

Results: Overexpression of showed slightly effect on the proliferation and migration of HGC-27 cells. Upon exposure to isoproterenol (ISO), a β-adrenergic receptor agonist, cell proliferation, and migration were inhibited while the cAMP/PKA pathway was activated and ERK1/2 phosphorylation was suppressed. overexpression reduced cAMP accumulation, retained ERK1/2 phosphorylation level and alleviated the antiproliferative effect upon exposure to ISO. However, overexpression was inoperative on the antiproliferative effect of forskolin (FSK), a direct activator of adenyl cyclase (AC), or 3-isobutyl-1-methylxanthine (IBMX), a phosphodiesterase (PDE) inhibitor.

Conclusions: Our results suggest overexpression may protect cells from the antiproliferative effects via activation of the cAMP/PKA pathway through interrupting signal transduction from G protein-coupled receptors to AC.
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http://dx.doi.org/10.1177/1559325820939022DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7350398PMC
July 2020

Reversal Effect of Dihydromyricetin on Multiple Drug Resistance in SGC7901/5-FU Cells.

Asian Pac J Cancer Prev 2020 May 1;21(5):1269-1274. Epub 2020 May 1.

Department of Biochemistry, Wannan Medical College, Wuhu, Anhui, P.R.China.

Background: One of the most common treatment for gastric cancer is chemotherapy, however, multiple drug resistance (MDR) induce the therapeutic effect which result in the failure of anticancer therapy. Dihydromyricetin (DMY) was reported to have antitumor activities on various human cancer cells in vitro, our previous studies demonstrated that DMY combined with mitomycin has inhibitory effect on proliferation of gastric carcinoma cells. However, the underlying role of DMY reversing the MDR of gastric carcinoma is poor understood. The aim of this study was to evaluate the reversal effect of DMY on MDR and investigate the molecular mechanisms in vitro.

Methods: Using MTT assay, we identified the toxicity of DMY on SGC7901 and SGC7901/5-FU cells. The effect of DMY on 5-FU induced apoptosis was evaluated by flow cytometry analysis. Using RT-PCR and Western blot, we determined the MDR1 mRNA and protein expression.

Results: DMY induced growth inhibition in both SGC7901 and SGC7901/5-FU cells, the IC50 value was 13.64±1.15 µg/mL, 20.69±1.82 µg/mL respectively. DMY treatment sensitized SGC7901/5-FU cells to cytotoxicity of 5-FU. The combination of DMY with 5-FU increased the apoptosis rate (9.91%, 16.67%) comparing with 5-FU alone (5.25%). Comparing with the control group, the MDR1 mRNA and protein expression in SGC7901/5-FU cells after treatment of DMY decreased significantly (P< 0.05).

Conclusion: In brief, our study demonstrated that DMY effectively reversed multi-drug resistance occurring in SGC7901/5-FU cells cultured in vitro, and the potential mechanism was involved in the downregulation of the MDR1 expression.
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http://dx.doi.org/10.31557/APJCP.2020.21.5.1269DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7541860PMC
May 2020

Residues at a Single Site Differentiate Animal Cryptochromes from Cyclobutane Pyrimidine Dimer Photolyases by Affecting the Proteins' Preferences for Reduced FAD.

Chembiochem 2017 06 15;18(12):1129-1137. Epub 2017 May 15.

Institute of Molecular Biology and Biotechnology, Anhui Normal University, 1# Beijing East Road, Wuhu, 241000, Anhui, China.

Cryptochromes (CRYs) and photolyases belong to the cryptochrome/photolyase family (CPF). Reduced FAD is essential for photolyases to photorepair UV-induced cyclobutane pyrimidine dimers (CPDs) or 6-4 photoproducts in DNA. In Drosophila CRY (dCRY, a type I animal CRY), FAD is converted to the anionic radical but not to the reduced state upon illumination, which might induce a conformational change in the protein to relay the light signal downstream. To explore the foundation of these differences, multiple sequence alignment of 650 CPF protein sequences was performed. We identified a site facing FAD (Ala377 in Escherichia coli CPD photolyase and Val415 in dCRY), hereafter referred to as "site 377", that was distinctly conserved across these sequences: CPD photolyases often had Ala, Ser, or Asn at this site, whereas animal CRYs had Ile, Leu, or Val. The binding affinity for reduced FAD, but not the photorepair activity of E. coli photolyase, was dramatically impaired when replacing Ala377 with any of the three CRY residues. Conversely, in V415S and V415N mutants of dCRY, FAD was photoreduced to its fully reduced state after prolonged illumination, and light-dependent conformational changes of these mutants were severely inhibited. We speculate that the residues at site 377 play a key role in the different preferences of CPF proteins for reduced FAD, which differentiate animal CRYs from CPD photolyases.
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http://dx.doi.org/10.1002/cbic.201700145DOI Listing
June 2017

Photoreactivation of Escherichia coli is impaired at high growth temperatures.

J Photochem Photobiol B 2015 Jun 23;147:37-46. Epub 2015 Mar 23.

Institute of Molecular Biology and Biotechnology, Anhui Normal University, Wuhu, Anhui, China. Electronic address:

Photolyase repairs UV-induced lesions in DNA using light energy, which is the principle of photoreactivation. Active photolyase contains the two-electron-reduced flavin cofactor. We observed that photoreactivation of Escherichia coli was impaired at growth temperatures ⩾37°C, and growth in this temperature range also resulted in decreased photolyase protein levels in the cells. However, the levels of phr transcripts (encoding photolyase) were almost unchanged at the various growth temperatures. A lacZ-reporter under transcriptional control of the phr promoter showed no temperature-dependent expression. However, a translational reporter consisting of the photolyase N-terminal α/β domain-LacZ fusion protein exhibited lower β-galactosidase activity at high growth temperatures (37-42°C). These results indicated that the change in photolyase levels at different growth temperatures is post-transcriptional in nature. Limited proteolysis identified several susceptible cleavage sites in E. coli photolyase. In vitro differential scanning calorimetry and activity assays revealed that denaturation of active photolyase occurs at temperatures ⩾37°C, while apo-photolyase unfolds at temperatures ⩾25°C. Evidence from temperature-shift experiments also implies that active photolyase is protected from thermal unfolding and proteolysis in vivo, even at 42°C. These results suggest that thermal unfolding and proteolysis of newly synthesized apo-photolyase, but not active photolyase, is responsible for the impaired photoreactivation at high growth temperatures (37-42°C).
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http://dx.doi.org/10.1016/j.jphotobiol.2015.03.012DOI Listing
June 2015