SOD对紫外辐射受损的苏云金芽孢杆菌作用的研究

探讨了超氧化物歧化酶 (SOD)等自由基清除剂对苏云金芽孢杆菌紫外辐射的影响。结果表明 ,SOD、绞股蓝皂甙等自由基清除剂能够明显地提高紫外辐射损伤细胞的存活率 ,并且SOD的保护作用表现为防护与恢复两种不同的作用。又通过细胞电泳与琼脂糖凝胶电泳发现紫外辐射后其细胞膜及质粒DNA均受到了明显的损伤 ;SOD对细胞膜损伤有一定的恢复作用 ,而对DNA不表现恢复效应。由此认为 :紫外线对细胞膜及DNA均有损伤 ,SOD恢复作用的主要部位在细胞膜而不是DNA分子。为进一步确定SOD的作用以及利用自由基清除剂制备高效的Bt农药提供了理论基础。     

辽东栎木材解剖特征与物理-力学性质的关系

本文借助通径系数分析及主成分分析等统计方法,以五株产自山西中条山的辽东栎为试验材料,详细研究了木材解剖特征的内在关系以及解剖特征与物理—力学性质的关系。结果表明,“细胞特征”(纤维、导管尺寸及微纤丝角等)和“组织比量”(导管、纤维及薄壁组织比量)两个主因子基本反映并代表了木材的所有解剖特征,同时也是影响木材物理—力学性质的两个基本解剖因子。     

酶活化处理条件及其对松木纤维胶合性能的影响初探

通过测定漆酶处理纤维压制纤维板的内结合强度 ,观察到漆酶对云南思茅松木纤维的活化作用及漆酶处理对木纤维自身胶合的贡献。不同pH值条件下漆酶处理木纤维的内结合强度显著高于水处理纤维压制的板材强度。失活后的酶液与水等效 ,说明对实现木材自身胶合起作用的主要是漆酶本身。初步探索了pH值、酶剂量、底物浓度、活化处理时间等因素对胶合效果的影响。采用试验得到的较好活化条件压制的板材内结合强度可达1 0MPa以上     

树木木质部细胞凋亡及心材形成机理研究进展

概述有关木纤维、管状分子与薄壁细胞等木质部细胞凋亡和心材形成方面的研究成果,探讨木质部细胞凋亡与心材形成之间的信号通路及调控机理,并基于当前研究现状,提出几点建议。     

干旱胁迫对白桦实生苗保护酶活性及脂质过氧化作用的影响

目前 ,活性氧自由基与植物抗逆性关系的研究正在日益深入 (戴金平等 ,1 991 ;王以柔等 ,1 995 ;许长城等 ,1 993;Ｊｏｈｎ ,1 992 ;Ｍａｒｃｅｌａｅｔａｌ.,1 993;阎秀峰等 ,1 999) ,对水分亏缺下活性氧对植物的氧化伤害及植物防御系统的反应也作了大量的研究 (陈立松等 ,1 998;1 999;沈秀瑛等 ,1 995 ;吕庆等 ,1 996;王爱国等 ,1 990 ;许长城等 ,1 993;阎秀峰等 ,1 999;Ｍｉｓｈｒａｅｔａｌ.,1 993)。在正常情况下 ,植物体内活性氧产生与清除处于平衡状态 ,不会导致细胞伤害 ,氧自由基的清除剂可分为酶促和非酶促两大类 (蒋明义等 ,1 996…     

Effect of proline-spirooxindole on viability and apoptosis of non-small-cell lung cancer A549 cells

AIM:To investigate the effect of proline-spirooxindole on the viability and apoptosis of human non-small-cell lung cancer A549 cells. METHODS:The effect of proline-spirooxindole on the viability of A549 cells was determined by CCK-8 assay. The apoptosis was analyzed by flow cytometry. The effects of proline-spirooxindole on the expression of PARP and p53 and the phosphorylation of mTOR were determined by Western blot. RESULTS:After A549 cells were treated with proline-spirooxindole (25, 50 and 100 mg/L), the cell viability was decreased (P<0.01) compared with DMSO control group. The apoptotic rate was increased compared with DMSO control group (P<0.01). The protein expression of p53 was up-regulated, the increased apoptotic protein cleaved PARP was observed, and the phosphorylation of mTOR was inhibited (P<0.01). CONCLUSION:Proline-spirooxindole inhibits the viability of A549 cells and induces apoptosis, which may be related to the phosphorylation of mTOR.     

FAM3C activates Akt to promote viability of oral squamous-cell carcinoma cells

AIM: To investigate the expression and roles of family with sequence similarity 3, member C (FAM3C) in oral squamous-cell carcinoma cells. METHODS: The mRNA and protein expression levels of FAM3C in dysplastic oral keratinocyte (DOK) and oral squamous-cell carcinoma WSU-HN6 cells were detected by RT-qPCR and Western blot. The WSU-HN6 cells were treated with siFAM3C or FAM3C antibody. After 24, 48 and 72 h, the viability of WSU-HN6 cells was measured by CCK-8 assay, and the activation of protein kinase B (Akt) was detected by Western blot. Adenovirus was used to mediate over-expression of FAM3C in the DOK cells. The DOK cell viability was measured by CCK-8 assay after adenovirus infection for 24, 48 and 72 h, and the activation of Akt was detected by Western blot. RESULTS: Compared with the DOK cells, the mRNA and protein levels of FAM3C were significantly increased in the WSU-HN6 cells (P<0.05). The viability of WSU-HN6 cells transfected with siFAM3C was significantly inhibited at 48 h and 72 h (P<0.05). siFAM3C treatment inhibited the activation of Akt (P<0.05). FAM3C antibody treatment also suppressed the viability of the WSU-HN6 cells at 48 h and 72 h and the activation of Akt (P<0.05). Over-expression of FAM3C in the DOK cells promoted the cell viability at 48 h and 72 h and activated Akt (P<0.05). CONCLUSION: FAM3C might promote oral squamous-cell carcinoma cell growth by activating Akt.     

PPARγ mediates effects of diosgenin on proliferation and apoptosis in human glioblastoma U87MG cells

AIM:To investigate the effect of diosgenin (Dio) on the proliferation, apoptosis and expression of peroxisome proliferator-activated receptor γ (PPARγ) in human glioblastoma U87MG cells and its possible mechanism. METHODS:Human astrocytes (HA) and U87MG cells were cultured in vitro and treated with Dio (0, 10, 20, 30, 40 and 50 μmol/L) and GW9662 (5 μmol/L) for 48 h, and then the cell viability was detected by CCK-8 assay. Cell colony formation assay was used to assess the proliferation potential. Flow cytometry was used to analyze the cell cycle distribution and apoptosis. The mRNA expression level of PPARγ was measured by RT-PCR. Western blot was used to determine the protein levels of PPARγ, cyclin D1, cyclin E1, Bcl-2 and Bax. RESULTS:Dio had no significant influence on the viabi-lity of HA (P>0.05). However, Dio remarkably reduced the viability of U87MG cells in a dose-dependent manner (P<0.05) with IC₅₀ of 24.31 μmol/L. Meanwhile, Dio remarkably diminished colony formation ability (P<0.05), induced G₀/G₁ phase arrest of the cell cycle and apoptosis (P<0.05), up-regulated the expression of PPARγ at mRNA and protein levels, increased the protein level of Bax (P<0.05), and down-regulated the protein levels of cyclin D1, cyclin E1 and Bcl-2 (P<0.05) in a dose-dependent manner. However, these effects induced by Dio were inhibited by GW9662 (P<0.05), a specific inhibitor of PPARγ. CONCLUSION:Dio may inhibit proliferation and induce apoptosis in human glioblastoma U87MG cells most likely via up-regulating the expression of PPARγ, and then down-regulating the protein levels of cyclin D1, cyclin E1 and Bcl-2, and up-regulating the protein level of Bax.     

F-box domain is involved in regulating the proliferation of MCF-7 cells by FBXO39 protein

AIM: To investigate the effect of F-box domain on the regulation of MCF-7 cell proliferation by FBXO39 protein. METHODS: The effect of F-box domain on the localization of FBXO39 protein in the MCF-7 cells was investigated. MCF-7 cell cDNA library was used as the template resource. The full-length cDNA sequence of FBXO39 was amplified by PCR method and subcloned into eukaryotic expression vector pEGFP-C2. The pEGFP-FBXO39ΔF (F-box domain deletion mutation) plasmid was successfully constructed with the template resource of pEGFP-FBXO39 plasmid. The recombinant plasmids were transfected into the MCF-7 cells, and then the expression of FBXO39 and FBXO39ΔF were determined by Western blot. The cellular localization of FBXO39 and FBXO39ΔF were observed by confocal microscopy. The localization of endogenous FBXO39 in the MCF-7 cells was detected by immunofluorescence staining. In addition, MTT and EdU assays were used to measure the cell proliferation, flow cytometry was used to measure the cell cycle distribution, and immunohistochemical staining was used to observe the expression of FBXO39 in the breast cancer and para-carcinoma tissues. RESULTS: The eukaryotic expression vector pEGFP-FBXO39 and pEGFP-FBXO39ΔF were constructed successfully. F-box domain had no effect on the cell localization of FBXO39. FBXO39 promoted MCF-7 cell proliferation but FBXO39ΔF did not. FBXO39 was highly expressed in the breast cancer tissues. CONCLUSION: F-box domain had no effect on the cellular localization of FBXO39 protein. However, it plays an important role in the biological function of FBXO39. FBXO39 may be related to breast cancer tumorigenesis.