[Evodiamine Promotes Apoptosis of Glioma SHG-44 Cells and Its Mechanism].

Objective To explore the role of evodiamine in promoting the apoptosis of glioma SHG-44 cells and its mechanism.Methods The in vitro cultured glioma SHG-44 cells were divided into control group and evodiamine group(which was further divided into three subgroups according to the glycoside concentrations).Cell viability was determined by CCK-8 method,cells apoptosis rate by flow cytometry,and nucleus apoptosis by Hoechst 33258 nuclear staining.Cell morphological changes were observed by transmission electron microscope.Protein expressions of Cleaved Caspase-3 and Cleaved Caspase-9 were detected by Western blot analysis.Results Evodiamine significantly inhibited the proliferation of glioma SHG-44 cells.The apoptosis rate of Glioma cells increased in a dose-dependent manner as the evodiamine concentration increased.Evodiamine promoted the expressions of cleaved Caspase-3 and cleaved Caspase-9.Conclusion Evodiamine inhibits glioma cell proliferation by changing the expressions of cleaved Caspase-3 and cleaved Caspase-9.

A SAL1 Loss-of-Function Arabidopsis Mutant Exhibits Enhanced Cadmium Tolerance in Association with Alleviation of Endoplasmic Reticulum Stress.

SAL1, as a negative regulator of stress response signaling, has been studied extensively for its role in plant response to environmental stresses. However, the role of SAL1 in cadmium (Cd) stress response and the underlying mechanism is still unclear. Using an Arabidopsis thaliana loss-of-function mutant of SAL1, we assessed Cd resistance and further explored the Cd toxicity mechanism through analysis of the endoplasmic reticulum (ER) stress response. The loss of SAL1 function greatly improved Cd tolerance and significantly attenuated ER stress in Arabidopsis. Exposure to Cd induced an ER stress response in Arabidopsis as evidenced by unconventional splicing of AtbZIP60 and up-regulation of ER stress-responsive genes. Damage caused by Cd was markedly reduced in the ER stress response double mutant bzip28 bzip60 or by application of the ER stress-alleviating chemical agents, tauroursodeoxycholic acid (TUDCA) and 4-phenyl butyric acid (4-PBA), in wild-type plants. The Cd-induced ER stress in Arabidopsis was also alleviated by loss of function of SAL1. These results identified SAL1 as a new component mediating Cd toxicity and established the role of the ER stress response in Cd toxicity. Additionally, the attenuated ER stress in the sal1 mutant might also shed new light on the mechanism of diverse abiotic stress resistance in the SAL1 loss-of-function mutants.

Species Richness of Papilionidae Butterflies (Lepidoptera: Papilionoidea) in the Hengduan Mountains and Its Future Shifts under Climate Change.

The family of Papilionidae (Lepidoptera: Papilionoidea) is a group of butterflies with high ecological and conservation value. The Hengduan Mountains (HMDs) in Southwest China is an important diversity centre for these butterflies. However, the spatial distribution pattern and the climate vulnerability of Papilionidae butterflies in the HDMs remain unknown to date. The lack of such knowledge has already become an obstacle in formulating effective butterfly conservation strategies. The present research compiled a 59-species dataset with 1938 occurrence points. The Maxent model was applied to analyse the spatial pattern of species richness in subfamilies Parnassiinae and Papilioninae, as well as to predict the response under the influence of climate change. The spatial pattern of both subfamilies in the HDMs has obvious elevation prevalence, with Parnassiinae concentrated in the subalpine to alpine areas (2500-5500 m) in western Sichuan, northwestern Yunnan and eastern Tibet, while Papilioninae is concentrated in the low- to medium-elevation areas (1500-3500 m) in the river valleys of western Yunnan and western Sichuan. Under the influence of climate change, both subfamilies would exhibit northward and upward range shifts. The majority of Parnassiinae species would experience drastic habitat contraction, resulting in lower species richness across the HDMs. In contrast, most Papilioninae species would experience habitat expansion, and the species richness would also increase significantly. The findings of this research should provide new insights and a clue for butterfly diversity and climatic vulnerability in southwestern China. Future conservation efforts should be focused on species with habitat contraction, narrow-ranged distribution and endemicity with both in situ and ex situ measures, especially in protected areas. Commercialised collecting targeting these species must also be regulated by future legislation.

The ER luminal binding protein (BiP) alleviates Cd(2+)-induced programmed cell death through endoplasmic reticulum stress-cell death signaling pathway in tobacco cells.

Cadmium (Cd) is very toxic to plant cells and Cd(2+) stress induces programmed cell death (PCD) in Nicotiana tabacum L. cv. bright yellow-2 (BY-2) cells. In plants, PCD can be regulated through the endoplasmic reticulum (ER) stress-cell death signaling pathway. However, the mechanism of Cd(2+)-induced PCD remains unclear. In this study, we found that Cd(2+) treatment induced ER stress in tobacco BY-2 cells. The expression of two ER stress markers NtBLP4 and NtPDI and an unfolded protein response related transcription factor NtbZIP60 were upregulated with Cd(2+) stress. Meanwhile, the PCD triggered by prolonged Cd(2+) stress could be relieved by two ER chemical chaperones, 4-phenylbutyric acid and tauroursodeoxycholic acid. These results demonstrate that the ER stress-cell death signaling pathway participates in the mediation of Cd(2+)-induced PCD. Furthermore, the ER chaperone AtBiP2 protein alleviated Cd(2+)-induced ER stress and PCD in BY-2 cells based on the fact that heterologous expression of AtBiP2 in tobacco BY-2 cells reduced the expression of NtBLP4 and a PCD-related gene NtHsr203J under Cd(2+) stress conditions. In summary, these results suggest that the ER stress-cell death signaling pathway regulates Cd(2+)-induced PCD in tobacco BY-2 cells, and that the AtBiP2 protein act as a negative regulator in this process.