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锰锌联合作用下大鼠生精细胞caspase-3和cyto-c的表达变化
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作者 郭海 才秀莲 王国秀 《河南职工医学院学报》 2012年第5期577-579,I0001,共4页
目的研究锰和锌对生精细胞caspase-3、cyto-c表达的影响。方法健康雄性SD大鼠80只随机分为10组,空白对照组,ZnCl2对照组,15 mg.kg-1和30 mg.kg-1MnCl2组;15 mg.kg-1MnCl2+ZnCl2组和30 mg.kg-1MnCl2+ZnCl2组。锰组分别给予MnCl2.4H2O腹... 目的研究锰和锌对生精细胞caspase-3、cyto-c表达的影响。方法健康雄性SD大鼠80只随机分为10组,空白对照组,ZnCl2对照组,15 mg.kg-1和30 mg.kg-1MnCl2组;15 mg.kg-1MnCl2+ZnCl2组和30 mg.kg-1MnCl2+ZnCl2组。锰组分别给予MnCl2.4H2O腹腔注射4周和6周;ZnCl2对照组给予100 mg Zn2+.kg-1饲料口服;锰加锌组分别染锰4周后再给予含锌饲料口服。各组大鼠分别于第4周末和第6周末处死,免疫组化法检测睾丸caspase-3、cyto-c表达。结果与空白组比较,各锰组和锰加锌组caspase-3阳性细胞率均升高,cyto-c阳性细胞率均降低(P<0.01)。与同剂量组比较,染锰6周caspase-3和cyto-c阳性细胞率分别较4周升高和降低(P<0.01)。与同时间组比较,30 mg.kg-1组caspase-3和cyto-c阳性细胞率分别较15 mg.kg-1组升高和降低(P<0.01)。与同剂量锰组比较,锰加锌组caspase-3和cyto-c阳性细胞率分别降低和升高。各组caspase-3和cyto-c阳性细胞率呈负相关(r=-0.817,P<0.01)。结论 15 mg.kg-1和30 mg.kg-1氯化锰均可诱发大鼠生精细胞caspase-3和cyto-c表达,并随染锰时间和剂量的增加而分别增加和降低,存在一定的时间-效应和剂量-效应关系,摄入含锌100 mg.kg-1的食物可抑制锰所诱发的caspase-3表达。 展开更多
关键词 生精细胞 CASPASE-3 cytochrome-c
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Overall Estimation of Anti-Oxidant Activity by Mammal Macrophage
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作者 Nobuo Yamaguchi Natsuko Kawada +4 位作者 Xinfeng Jia Kazuhiro Okamoto Katsuko Okuzumi Rui Chen Takashi Takahashi 《Open Journal of Rheumatology and Autoimmune Diseases》 2014年第1期13-21,共9页
Super oxide anion had been known as a critical role in a phagocytic cell when microorganisms invade inside. However, this radical seldom need for a clean environment such in a developed country. Moreover, this agent s... Super oxide anion had been known as a critical role in a phagocytic cell when microorganisms invade inside. However, this radical seldom need for a clean environment such in a developed country. Moreover, this agent sometimes triggered as serious factor in the site of inflammation. There are many papers which concerned newly found anti-oxidative substances. However, many reports only focused on the molecular basis in vitro, how oxidative stress damaged the human tissue. The key factor for oxidative stress needs to be discussed first for immunological standpoint, such as armed reduction treaty. In other words, minimum armed force is necessary for an invasion by outer or inner irregular cells. On the basis of phagocytic function of the cell in vivo, we tried to access anti-oxidative activity by employing peritoneal murine macrophage and human monocyte. So, the purpose of this study is to establish a conventional but tailor made system for which is useful for evaluating the anti-oxidative activity to different constition. Especially in human peripheral monocyte, the sample was tested each constitution such in granulocyte rich type and lymphocyte rich typ. In order to establish the direct estimation by phagocytic cell, a murine peritoneal exudates cell suspension was obtained after one week of oral administration with anti-oxidative sample. The samples we selected were traditional Chinese medicine, Shi-Quan-Da-Bu-Tang (SDT), Bu-Zong-Ye-Qi-Tang (BYT) and Shao-Chin-Rong-Tang sCRT), Agaricus, Chlorella, and Propolis. The amount of generated super oxide anion was calculated through measuring the optical density change of this supernatant using cytochrome-C which was reduced by generated super oxide anion in the phagocytic cell. The generated super oxide anion after administration of Agaricus, Chlorella, SDT, BYT, sCRT and Propolis were 2.64, 1.95, 1.24, 1.25, 2.88, 2.55 × 10﹣5 mmol/ml, respectively, whereas 2.85 × 10﹣5 mmol/ml in control group. The fermented sample from SDT, BYT, sCRT and microfied Propolis were also tested and the value of super oxide anion were 0.62, 0.84, 1.50 and 2.55 × 10﹣5 mmol/ml, respectively. In this report, we discussed the direct method for measuring the generated super oxide anion of macrophages, especially from different constitution. 展开更多
关键词 ANTI-OXIDANT Sample Super Oxide Anion NEUTROPHIL MACROPHAGE cytochrome-c CONSTITUTION
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Metallated Schiff-Base Macromolecules as Alternative Metalloprotein Electron Transfer Intermediates
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作者 Al C. Farao Rachel Fanelwa Ayaji +1 位作者 Meryck Ward Priscilla GL Baker 《Journal of Surface Engineered Materials and Advanced Technology》 2020年第2期34-54,共21页
In the construction of biosensors, enzymes function as mediators converting biological signals generated by specific biological processes, into electrochemical signals. The ideology of bio-sensor design is retention o... In the construction of biosensors, enzymes function as mediators converting biological signals generated by specific biological processes, into electrochemical signals. The ideology of bio-sensor design is retention of electron transfer activity of the enzyme utilizing superior interfacial architecture. In this work a Schiff-base macromolecule has been synthesized by reflux of 2, 3-diaminonaphthalene and pyrrole-2-carboxaldehyde starting materials. The Schiff-base ligand was subsequently complexed with FeCl2?4H2O under reflux, to produce the Fe-Schiff-base complex. The Schiff-base ligand and Fe-Schiff-base complex were characterized using nuclear magnetic resonance (NMR) spectroscopy, Ultra Violet/Visible (UV/Vis) spectroscopy, Fourier transfer infrared resonance (FTIR) and electron energy loss spectroscopy (EELS) to confirm the structure of the synthesis products. NMR spectroscopy confirmed the imide linkage of Schiff-base formation as two symmetrical peaks at 8.1 and 7.7 ppm respectively. Comparison of starting materials and product spectra by UV/Vis spectroscopy confirmed the disappearance of the diaminonaphthalene peak at 250 nm as evidence of complete conversion to product. FTIR spectroscopy of the Schiff-base ligand confirmed the formation of the imine bond at 1595 cm-1. EELS spectra comparing FeCl2?4H2O and the Fe-Schiff-base complex, showed good agreement in the energy loss profiles associated with changes to the electronic arrangement of Fe d-orbitals. EDS clearly identified a spectral band for Fe (7 - 8 eV) in the Fe-Schiff-base complex. Electrochemical evaluation of the Fe-Schiff-base complex was compared to the electrochemical signature of denatured cytochrome-C using cyclic voltammetry and square wave voltammetry. The Fe2+/Fe3+ quasi-reversible behavior for iron in the metallated complex was observed at -0.430 V vs. Ag/AgCl, which is consistent with reference values for iron in macromolecular structures. 展开更多
关键词 cytochrome-c MACROMOLECULE Metallated METALLOPROTEINS SCHIFF-BASE
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