Jinjuan Liu

Central China Normal University, Wu-han-shih, Hubei, China

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Publications (2)6.59 Total impact

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    ABSTRACT: Actinomycin D (Act D), a well known of clinical antitumor drug, has been used for the treatment of some highly malignant tumors, however, the clinical application was limited by its extreme cytotoxicity. In the present study, we reported that methylated actinomycin D (mAct D), a novel actinomycin D analog isolated from Streptomyces sp. KLBMP 2541 in our previous study, could not only exert stronger inhibitory effects on several human cancer cells than Act D in dose- and time-dependent manner at ng concentrations, especially on HepG2 cells, but also lower cytotoxicity in normal cells (HL-7702). Base on these results, HepG2 cells were treated for further study to illustrate the potential mechanism of mAct D. The results of nuclei morphology examination, DNA fragmentation detection, sub-G(1) analysis, annexin V-FITC/PI staining and activation of caspase-3 indicated mAct D significantly induced HepG2 cells apoptosis. Semiquantitative RT-PCR and Western blot analysis revealed that mAct D induced apoptosis in HepG2 cells through mitochondria-dependent pathway by increasing levels of caspase-9, Bax, Bak while decreasing levels of Bcl-2, Bid, and Fas-dependent pathway by increasing levels of Fas, FasL, FADD, and caspase-8. Subsequently, pretreatment with specific inhibitor of caspase-8 Z-LEHD-FMK and caspase-9 Z-LEHD-FMK significantly attenuated caspase-3 activity, the cleavage of caspase-3 and PARP, meanwhile increased the cell viability. In addition, p53 and mitochondrial transcription factor A (mtTFA) were also upregulated. Taken together, ng concentrations mAct D induces the apoptosis of HepG2 through Fas- and mitochondria-mediated pathway and presents a potential novel alternative agent for the treatment of human hepatic carcinoma. © 2012 Wiley Periodicals, Inc.
    No preview · Article · Dec 2013 · Molecular Carcinogenesis
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    ABSTRACT: A fibrinolytic enzyme (SFE1) from Streptomyces sp. XZNUM 00004 was purified to electrophoretic homogeneity with the methods including ammonium sulfate precipitation, polyacrylamide gel, DEAE-Sepharose Fast Flow anion exchange and gel-filtration chromatography. The molecular weight of SFE1 was estimated to be 20 kDa by SDS-PAGE, fibrin zymography, and gel filtration chromatography. The isoelectric point was 4.9. K m and V max values were 0.96 mg/ml and 181.8 unit/ml, respectively. It was very stable at pH 5.0–8.0 and below 65 °C. The optimum pH for enzyme activity was 7.8. The optimum temperature was 35 °C. The fibrinolytic activity of SFE1 was enhanced by Na+, K+, Mn2+, Mg2+, Zn2+ and Co2+. Conversely, Cu2+ showed strong inhibition. Furthermore, the fibrinolytic activity was strongly inhibited by PMSF, and partly inhibited by EDTA and EGTA. SFE1 rapidly hydrolyzed the Aα-chain of fibrinogen, followed by the Bβ-chain and finally the γ-chain. The first 15 amino acids of the N-terminal sequence were APITLSQGHVDVVDI. Additionally, SFE1 directly digested fibrin and not by plasminogen activators in vitro. SFE1 can be further developed as a potential candidate for thrombolytic therapy.
    Preview · Article · Jul 2012 · World Journal of Microbiology and Biotechnology (Formerly MIRCEN Journal of Applied Microbiology and Biotechnology)

Publication Stats

7 Citations
6.59 Total Impact Points


  • 2013
    • Central China Normal University
      Wu-han-shih, Hubei, China
  • 2012
    • Jiangsu Normal University
      • Key Laboratory for Biotechnology on Medicinal Plants of Jiangsu Province
      Hsü-chuang, Shaanxi, China