狐蝠对森林生态系统的作用

翼手目 (Chiroptera)为真正能飞翔的哺乳动物 ,现存 19科 110 7种 ,分别属于小蝙蝠亚目 (Microchiroptera)和大蝙蝠亚目 (Megachiroptera) ;其中大蝙蝠又称旧大陆狐蝠或果蝠 (flyingfox) ,分布在热带和亚热带地区 ,仅狐蝠科 188种 ,我国自然分布有 9种。部分地区因栖息地丧失和过度捕杀导致狐蝠种群数量全球性或地区性下降或灭绝 ;狐蝠通过传播种子或传粉 ,促进森林生态系统的更新和基因交流。因此 ,狐蝠对森林生态系统的稳定、扩散、生物多样性以及衰退森林的恢复有重要作用     

拖网式食鱼蝠——大足鼠耳蝠的形态、回声定位声波及捕食策略

大足鼠耳蝠(Myotisricketti)是中国特有蝙蝠,其回声定位声波和捕食策略国内外均无报道,对大足鼠耳蝠该方面的研究报导是国内首次。大足鼠耳蝠体型较大,具有强大的后足,足上有强而有力的弯曲的爪,尾膜和距很长。大足鼠耳蝠回声定位声波为FM(调频)型,一般具有1～2个谐波,主频率较低(37.78±1.04kHz),调频带较宽(第一谐波频带宽为42.02±6.98kHz,第二谐波频带宽为25.79±7.89kHz),声脉冲时间较长(2.91±0.54ms),声脉冲间隔时间变化较大(32.30±15.10ms),能率环较高(11.27±5.84%);野外观察发现,大足鼠耳蝠主要在低水面上空飞行,利用大足从水面捕食猎物(拖网式捕食),猎物主要由鱼类组成。即分析和讨论了大足鼠耳蝠形态特征、回声定位特征和捕食策略的相互适应性。     

川金丝猴摄食过程中“手”的选择使用

本文对20只川金丝猴(Rhinopithecus roxellana) 摄食过程中左右“手”的使用频次进行了观察和分析。在样本较小的条件下, 尽管被研究动物中有一半个体明显地倾向于使用右手, 但没有发现统计学上明显的种群水平的单手利现象。虽然本研究中成体金丝猴使用右手的比例在数量上高于幼体, 但在统计学上, 单手利行为不存在明显的年龄差别; 同样, 单手利用行为也不存在统计学上明显的性别差异。建议在未来的研究中采用大样本在解决复杂问题过程中对单手利行为做进一步的探讨。     

气候变化对雪豹全球潜在适生区分布的影响与评估

气候变化不仅是人类正在面临的挑战,也是野生动物需要应对的危机。雪豹(Panthera uncia)作为亚洲中部高原和山脉的旗舰种,它的生存和繁衍可以反映青藏高原等地区生态系统的健康状况。青藏高原等地区的气候变暖速度远快于全球平均水平,研究气候变化对雪豹的生境的影响对于高原物种的保护有重要意义。以雪豹为研究对象,采用第六次国际耦合模式比较计划(CMIP6)气候模式下四种共享社会经济路径(SSPs)对应的未来21世纪中期和21世纪末期的环境数据,并基于最大熵模型(MaxEnt),结合ENMTool、SDMTool、ArcGIS和R等工具对当前和未来全球不同发展模式引起的气候变化对雪豹适宜生境的影响进行了模拟预测和分析评估。研究发现：(1)影响雪豹分布的主要环境因素包括：两种气候变量(年平均气温和最冷月最低温度),两种地形变量(海拔和坡度)和一种水文变量(距离最近河流的距离)。(2)当前气候模式下雪豹的全球潜在适宜分布区的总面积约为1122.05万km²,其中低适生区面积为534.5万km²,中适生区面积为386.15万km²...     

Recombinant Clostridium difficile toxin B induces endoplasmic reticulum stress in mouse colonal carcinoma cells

Clostridium difficile is the main cause of antibiotic-associated diarrhea and pseudomembranous colitis in humans and animals. Its pathogenicity is primarily linked to the secretion of two exotoxins （TcdA and TcdB）. Although great progress in the toxic mechanism of TcdA and TcdB has been achieved, there are many conflicting reports about the apop- totic mechanism. More importantly, apoptotic endoplasmic reticulum （ER） stress has been reported in cells treated with Shiga toxins---another kind of cytotoxins that can cause diar- rhea and colitis. Herein we checked whether TcdB can induce ER stress. The results showed that recombinant TcdB （rTcdB） activated molecular markers of unfolded protein re- sponse, suggesting that rTcdB induced ER stress in CT26 cells. However, rTcdB did not induce the up-regulation of C/EBP homologous protein （CHOP）, a classic mediator of apoptotic ER stress, but it activated the precursor of cysteine aspartic acid-specific protease 12 （caspase-12）, a controver- sial mediator of apoptotic ER stress. Besides, glucosyltrans- ferase activity-deficient mutant recombinant TcdB induced ER stress, though it has no cytotoxic or cytopathic effect on CT26 cells. Altogether, these data demonstrated that ER stress induced by rTcdB is glucosyltransferase-independent, indicating that ER stress induced by rTcdB is non-apoptotic. This work also offers us a new insight into the molecular mechanism of CHOP protein expression regulation and the role of CHOP expression in ER stress.     

NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker

The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or mis-translocation. To study the structure of NTD, it was overexpressed and purified from Escherichia coli cells using affinity purification and gel filtration chromatography. The purified protein behaved as a monomer under purification conditions. Far- and near-UV, circular dichroism (CD) and solution nuclear magnetic resonance (NMR) studies showed that the purified protein was well-folded. The solution structure of NTD was obtained and the N-terminal residues 13-23 forming an amphipathic helix which may be important for the protein-protein or protein-membrane interactions. NMR titration experiment also demonstrated that residues from 88 to 94 in NTD are important for the molecular interaction with the peptide derived from the S4-S5 linker.