Picroside III,an Active Ingredient of Picrorhiza scrophulariiflora,Ameliorates Experimental Colitis by Protecting Intestinal Barrier Integrity

This study aims to explore the protective effects of Picroside III, an active ingredient of Picrorhiza scrophulariiflora, on the intestinal epithelial barrier in tumor necrosis factor-α (TNF-α) induced Caco-2 cells and dextran sulfate sodium (DSS) induced colitis in mice. Results show that Picroside III significantly alleviated clinical signs of colitis including body weight loss, disease activity index increase, colon shortening, and colon tissue damage. It also increased claudin-3, ZO-1 and occludin expressions and decreased claudin-2 expression in the colon tissues of mice with colitis. In vitro, Picroside III also significantly promoted wound healing, decreased the permeability of cell monolayer, upregulated the expressions of claudin-3, ZO-1 and occludin and downregulated the expression of claudin-2 in TNF-α treated Caco-2 cells. Mechanism studies show that Picroside III significantly promoted AMP-activated protein kinase (AMPK) phosphorylation in vitro and in vivo, and blockade with AMPK could significantly attenuate the upregulation of Picroside III in ZO-1 and occludin expressions and the downregulation of claudin-2 expression in TNF-α treated Caco-2 cells. In conclusion, this study demonstrates that Picroside III attenuated DSS-induced colitis by promoting colonic mucosal wound healing and epithelial barrier function recovery via the activation of AMPK.     

Terpenoids from Euphorbia helioscopia and Their Cytotoxic Activities against H1975 Cells

Three previously undescribed diterpenoids, helioscopnoids A–C, and eight known compounds were isolated from the whole plants of Euphorbia helioscopia. Their structures were established by extensive analysis of spectra and data comparison with previous literatures. Among them, compound 4 was identified as 24,24-dimethoxy-25,26,27-trinoreuphan-3β-ol with revised configurations of C-13, C-14, and C-17 (13R*, 14R*, 17R*). Cytotoxicity assays revealed that all compounds exhibited varying levels of cytotoxicity against H1975 cells, with compound 9 displaying the most potent activity, as indicated by cell viability rates of 18.13 % and 20.76 % at concentrations of 20 μM and 5 μM, respectively. This study expands the understanding of E. helioscopia terpenoids’ structural diversity and biological activities, contributing to the exploration of potential therapeutic applications.     

Steel Anti-Corrosion Strategy Enables Long-Cycle Zn Anode

The progress of aqueous zinc batteries (AZBs) is limited by the poor cycling life due to Zn anode instability, including dendrite growth, surface corrosion, and passivation. Inspired by the anti-corrosion strategy of steel industry, a compounding corrosion inhibitor (CCI) is employed as the electrolyte additive for Zn metal anode protection. It is shown that CCI can spontaneously generate a uniform and ≈30 nm thick solid-electrolyte interphase (SEI) layer on Zn anode with a strong adhesion via Zn O bonding. This SEI layer efficiently prohibits water corrosion and guides homogeneous Zn deposition without obvious dendrite formation. This enables reversible Zn deposition and dissolution for over 1100 h under the condition of 1 mA cm⁻² and 1 mAh cm⁻² in symmetric cells. The Zn-MnO₂ full cells with CCI-modified electrolyte deliver an ultralow capacity decay rate (0.013% per cycle) at 0.5 A g⁻¹ over 1000 cycles. Such an innovative strategy paves a low-cost way to achieve AZBs with long lifespan.     

中国东北地区三种蜜环菌的生物学特性及奥氏蜜环菌人工培养

蜜环菌属Armillaria真菌具有较高的食药用价值。由于蜜环菌的生长发育过程较复杂,还未完全实现商业化栽培,野生资源的供应受到季节性和地域性的影响。本研究以采自东北地区蜜环菌属的3个菌株为研究对象,通过培养物的形态特征及分子标记确定菌株JG19016为奥氏蜜环菌A. ostoyae,菌株JG19017为高卢蜜环菌A. gallica,菌株JG19018为中国蜜环菌生物种C。奥氏蜜环菌JG19016最适生长温度为25 ℃,高卢蜜环菌JG19017的最适生长温度为22 ℃,中国蜜环菌生物种C JG19018则在22-25 ℃时菌丝生长速度最快;3个菌株最适pH为5-6。奥氏蜜环菌JG19016对葡萄糖和蔗糖利用率较好,高卢蜜环菌JG19017对葡萄糖利用率较好,中国蜜环菌生物种C JG19018对葡萄糖和淀粉利用率较好;蛋白胨对3个菌株促进作用最强,为最适氮源。培养基中加入VB₁,对3个菌株的菌丝生长均有明显的促进作用。奥氏蜜环菌JG19016菌丝生长的最优培养基配方为：葡萄糖20 g,蛋白胨3 g,磷酸二氢钾2 g,硫酸镁1.5 g,VB₁ 10 mg,琼脂20 g,水1 L。在木屑基质中培养,其配方的最优碳氮比为38:1,最佳木屑粗细比为3:1以上。出菇条件探索结果显示,菌丝及菌索长满菌袋(17 mm×33 mm×5 mm丝聚乙烯袋)需要50-60 d,之后在18 ℃、60%湿度和12 h散射光的环境中,10 d左右可观察到原基产生。增加菇房湿度到90%-95%,2-3 d可观察到1-3 cm的幼子实体,7 d左右菌柄和菌盖完全分化,10 d左右观察到菌盖展开。     

pH对灵芝液态发酵代谢物及抗氧化活性的影响

已有研究报道灵芝栽培生长的最适pH在中性偏酸环境,在碱性范围的生长及代谢情况鲜见报道。本研究主要探究广泛pH对灵芝液态发酵代谢物及其抗氧化活性的影响。采用摇瓶液态培养后分析代谢物中灵芝三萜、胞内外多糖、菌丝体蛋白及抗氧化活性等指标,系统比较灵芝菌丝体在pH值2-11的生长和代谢情况。研究结果表明,灵芝菌丝体生长、合成灵芝三萜、胞内多糖、30E胞外多糖、菌丝体蛋白和菌丝体水解氨基酸的最适pH值分别为10、3、2、7、2和2。对应结果分别为17.13 g/L、33.86 mg/g、72.73 mg/g、7.86 g/L、71.42 mg/g和107.10 mg/g。比对照分别提高28.5%、77.3%、22.4%、96.5%、97.1%和70.8%。胞内多糖组分1和组分2最高分子量均在初始pH 4,分别为1.016×10⁸ g/mol和9.280×10⁴ g/mol,胞外多糖组分1最高分子量在初始pH 10,为4.946×10⁶ g/mol;对菌丝体的总抗氧化能力、1,1-二苯基-2-三硝基苯肼(1,1-diphenyl-2- picrylhydrazyl,DPPH)自由基清除能力、羟自由基清除能力分析结果表明最佳的初始pH分别为3、7、9。本研究为液态发酵方式下灵芝生长及其代谢物定向调控发酵的工艺优化提供参考依据,同时发现灵芝菌丝体中优质蛋白及抗氧化活性可在功能性食品和化妆品领域推广应用。     

山西糜子核心种质分子身份证构建

为快速鉴定糜子(Panicum miliaceum)资源, 建立分子标记检测平台, 以272份山西糜子核心种质为研究材料, 利用85对简单重复序列(SSR)引物, 应用ID Analysis 4.0软件, 构建DNA分子身份证。结果表明, 对85对SSR引物进行筛选, 发现20对引物组合(RYW67、RYW53、RYW37、RYW65、RYW62、RYW77、RYW5、RYW49、RYW84、RYW19、RYW11、RYW40、RYW54、RYW28、RYW31、RYW7、RYW16、RYW8、RYW9和RYW18)可区分272份材料。共检测到等位变异(Na) 60个, 平均每个位点检出3个; Shannon多样性指数(I)为0.957 8 (RYW16)-1.096 7 (RYW5), 平均值为1.055 2; 多态性信息含量(PIC)为0.604 4 (RYW77)-0.753 0 (RYW37), 平均值为0.692 1。利用20对引物构建山西糜子核心种质的字符串、条形码和二维码DNA分子身份证, 可为种质身份标识和溯源提供实践路径。     

Changes in antizyme-ornithine decarboxylase complexes in tissues of hormone-treated rats

The presence of antizyme-ornithine decarboxylase complex in thymus and kidney of rats was demonstrated using the method of Y Murakami et al. [(1985) Biochem. J. 225, 689-697]. A very small amount of complex was found in kidney of control rats, accounting for only 1-3% of total enzyme in the tissue, while in thymus, approximately one-third of the total ornithine decarboxylase in thymus occurred as an antizyme-enzyme complex. After treatment with dexamethasone, both free ornithine decarboxylase and antizyme-ornithine decarboxylase decreased in thymus, the free enzyme activity decreasing more rapidly. In kidney, the concentration of the antizyme-ornithine decarboxylase complex increased after dexamethasone treatment, but only after the induction of free enzyme activity had reached its peak and begun to decrease. The pattern of the changes in amount of antizyme-ornithine decarboxylase complex after prolactin treatment differed from those observed in the dexamethasone-treated animals. In both kidney and thymus, the concentration of antizyme-ornithine decarboxylase complex increased concurrently with the induction of free enzyme activity. Both free and complexed ornithine decarboxylase had increased at 2.5 h after prolactin treatment and continued to increase to maximum specific activities at similar rates. In thymus, the amount of ornithine decarboxylase present as a complex reached 70% of the total in the tissue. In both thymus and kidney, the concentration of antizyme-ornithine decarboxylase complex decreased more slowly than did free enzyme activity. Free antizyme was observed only in thymus of dexamethasone-treated animals. The amount of measurable inhibitor was decreased if cycloheximide was given with dexamethasone.     

Reciprocal regulation of Δ 1-pyrroline-5-carboxylate synthetase and proline dehydrogenase genes controls proline levels during and after osmotic stress in plants

Plants generally accumulate free proline under osmotic stress conditions. Upon removal of the osmotic stress, the proline levels return to normal. In order to understand the mechanisms involved in regulating the levels of proline, we cloned and characterized a proline dehydrogenase (PDH) cDNA from Arabidopsis thaliana (AtPDH). The 1745?bp cDNA contains a major open reading frame encoding a peptide of 499 amino acids. The deduced amino acid sequence has high homology with both Saccharomyces cerevisiae and Drosophila melanogaster proline oxidases and contains a putative mitochondrial targeting sequence. When expressed in yeast, the AtPDH cDNA complemented a yeast put1 mutation and exhibited proline oxidase activity. We also determined the free proline contents and the Δ¹-pyrroline-5-carboxylate synthetase (P5CS) and PDH mRNA levels under different osmotic stress and recovery conditions. The results demonstrated that the removal of free proline during the recovery from salinity or dehydration stress involves an induction of the PDH gene while the activity of P5CS declines. The reciprocal regulation of P5CS and PDH genes appears to be a key mechanism in the control of the levels of proline during and after osmotic stress. The PDH gene was also significantly induced by exogenously applied proline. The induction of PDH by proline, however, was inhibited by salt stress.