排序方式: 共有15条查询结果,搜索用时 31 毫秒
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Wnt基因所编码的蛋白质与许多生长因子一样具有分泌型生长因子的结构特点,其家族成员Wnt-5A是许多恶性肿瘤的自分泌生长因子,在肾细胞癌中表达显著升高.为研究在细胞周期的不同阶段生长因子Wnt-5A在转录水平的表达情况,我们采用胸腺嘧啶双阻断及高压笑气处理的方法,使肾细胞癌细胞系GRC-1细胞同步化.用半定量反转录多聚酶链反应对处于细胞周期不同阶段的细胞cDNA进行扩增,S期与G1,M期Wnt-5A mRNA表达存在差异显著(P<0.05).结果提示生长因子Wnt-5A在肾细胞癌的发生中具有潜在的作用,在S期作用可能尤为显著. 相似文献
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过氧化氢诱导的2BS应激性早衰细胞后,自噬被发现增多.自噬特异抑制剂3-甲基腺嘌呤(3-MA )阻断年轻和早衰的2BS细胞的自噬作用36 h,用共聚焦显微镜,分析转染了自噬特异标志GFP-LC3融合质粒的年轻和早衰细胞,发现细胞自噬颗粒均明显减少,且GFP-LC3染色阳性/ 细胞数目也大大减少,说明3-MA有效地阻断了细胞的自噬过程.分别用流式细胞术和荧光显微镜分析年轻和早衰细胞的凋亡情况,发现年轻的2BS细胞自噬阻断后凋亡未见显著变化,而早衰的细胞凋亡明显增加,且有细胞坏死.由此推断,3-AM可使过氧化氢诱导的2BS早衰细胞自噬明显减少,而凋亡被诱导增多,提示自噬对过氧化氢诱导的早衰细胞具有避免凋亡和维持存活的保护作用. 相似文献
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Jie-Hua Shi Qi Wang Dong-Qi Pan Ting-Ting Liu Min Jiang 《Journal of biomolecular structure & dynamics》2017,35(7):1529-1546
The binding interactions of simvastatin (SIM), pravastatin (PRA), fluvastatin (FLU), and pitavastatin (PIT) with bovine serum albumin (BSA) were investigated for determining the affinity of four statins with BSA through multiple spectroscopic and molecular docking methods. The experimental results showed that SIM, PRA, FLU, and PIT statins quenched the intrinsic fluorescence of BSA through a static quenching process and the stable stains–BSA complexes with the binding constants in the order of 104 M?1 at 298 K were formed through intermolecular nonbond interaction. The values of ΔH0, ΔS0 and ΔG0 in the binding process of SIM, PRA, FLU, and PIT with BSA were negative at the studied temperature range, suggesting that the binding process of four statins and BSA was spontaneous and the main interaction forces were van der Waals force and hydrogen-bonding interactions. Moreover, the binding of four statins with BSA was enthalpy-driven process due to |ΔH°|>|TΔS°| under the studied temperature range. From the results of site marker competitive experiments and molecular docking, subdomain IIIA (site II) was the primary binding site for SIM, PRA, FLU, and PIT on BSA. The results of UV–vis absorption, synchronous fluorescence, 3D fluorescence and FT-IR spectra proved that the slight change in the conformation of BSA, while the significant changes in the conformation of SIM, PRA, FLU, and PIT drug in statin–BSA complexes, indicating that the flexibility of statin molecules plays an important role in increasing the stability of statin–BSA complexes. 相似文献
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