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Prion Protein Protects Cancer Cells against Endoplasmic Reticulum Stress Induced Apoptosis 认领 引用 被引量：5
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作者 Zhenxing Gao Min Peng +7 位作者 Liang Chen Xiaowen Yang Huan Li Run Shi Guiru Wu Lili Cai Qibin Song Chaoyang Li 《Virologica Sinica》 SCIE CAS CSCD 2019年第2期222-234,共13页
Unfolded protein response(UPR) is an adaptive reaction for cells to reduce endoplasmic reticulum(ER) stress. In many types of cancers, such as lung cancer and pancreatic cancer, cancer cells may harness ER stress to f... Unfolded protein response(UPR) is an adaptive reaction for cells to reduce endoplasmic reticulum(ER) stress. In many types of cancers, such as lung cancer and pancreatic cancer, cancer cells may harness ER stress to facilitate their survival and growth. Prion protein(PrP) is a glycosylated cell surface protein that has been shown to be up-regulated in many cancer cells. Since PrP is a protein prone to misfolding, ER stress can result in under-glycosylated PrP, which in turn may activate ER stress. To assess whether ER stress leads to the production of under-glycosylated PrP and whether underglycosylated PrP may contribute to ER stress thus leading to cancer cell apoptosis, we treated different cancer cells with brefeldin A(BFA), thapsigargin(Thps), and tunicamycin(TM). We found that although BFA, Thps, and TM treatment activated UPR, only ATF4 was consistently activated by these reagents, but not other branches of ER stress. However, the canonical PERK-eIF2α-ATF4 did not account for the observed activation of ATF4 in lung cancer cells. In addition, BFA,but neither Thps nor TM, significantly stimulated the expression of cytosolic PrP. Finally, we found that the levels of PrP contributed to anti-apoptosis activity of BFA-induced cancer cell death. Thus, the pathway of BFA-induced persistent ER stress may be targeted for lung and pancreatic cancer treatment. 展开更多
关键词 Endoplasmic reticulum stress Brefeldin A (BFA) Prion protein (PrP)- Glycosylation Apoptosis
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Robust LPV modeling and control of aircraft flying through wind disturbance 认领 引用 被引量：11
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作者 Zhenxing GAO Jun FU 《Chinese Journal of Aeronautics》 SCIE EI CAS CSCD 2019年第7期1588-1602,共15页
This article deals with the disturbance attenuation control of aircraft flying through wind shear via Linear Parameter Varying(LPV) modeling and control method. A Flight Dynamics Model(FDM) with wind shear effects con... This article deals with the disturbance attenuation control of aircraft flying through wind shear via Linear Parameter Varying(LPV) modeling and control method. A Flight Dynamics Model(FDM) with wind shear effects considered was established in wind coordinate system. An LPV FDM was built up based on function substitution whose decomposing function was optimized by Genetic Algorithm(GA). The wind disturbance was explicitly included in the system matrix of LPV FDM. Taking wind disturbance as external uncertainties, robust LPV control method with the LPV FDM was put forward. Based on ride quality and flight safety requirements in wind disturbance, longitudinal and lateral output feedback robust LPV controllers were designed respectively,in which the scheduling flight states in LPV model were actually dependent parameters in LPV control. The results indicate that LPV FDM can reflect the instantaneous dynamics of nonlinear system especially at the boundary of aerodynamic envelope. Furthermore, the LPV FDM also can approach nonlinear FDM’s response in wind disturbance special flight. Compared with a parameter-invariant LQR controller designed with a small-disturbance FDM, the LPV controllers show preferable robustness and stability for disturbance attenuation. 展开更多
关键词 Function substitution Linear parameter varying LPV control Robust control Wind shear
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Tumor Necrosis Factor a Reduces SNAP29 Dependent Autolysosome Formation to Increase Prion Protein Level and Promote Tumor Cell Migration 认领 引用 被引量：1
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作者 Huan Li Ren Wang +9 位作者 Ze Yu Run Shi Jie Zhang Shanshan Gao Ming Shao Shuzhong Cui Zhenxing Gao Jiang Xu Man-Sun Sy Chaoyang Li 《Virologica Sinica》 SCIE CAS CSCD 2021年第3期458-475,共18页
Tumor Necrosis Factor α(TNFα) is best known as a mediator of inflammation and immunity, and also plays important roles in tumor biology. However, the role of TNFα in tumor biology is complex and not completely unde... Tumor Necrosis Factor α(TNFα) is best known as a mediator of inflammation and immunity, and also plays important roles in tumor biology. However, the role of TNFα in tumor biology is complex and not completely understood. In a human melanoma cell line, M2, and a lung carcinoma cell line, A549, TNFα up-regulates prion protein(PrP) level, and promotes tumor cell migration in a PrP dependent manner. Silencing PRNP abrogates TNFα induced tumor cell migration;this phenotype is reversed when PRNP is re-introduced. Treatment with TNFα activates nuclear factor kappa B(NF-κB)signaling, which then mitigates autophagy by reducing the expression of Forkhead Box P3(FOXP3). Down regulation of FOXP3 reduces the transcription of synaptosome associated protein 29(SNAP29), which is essential in the fusion of autophagosome and lysosome creating autolysosome. FOXP3 being a bona fide transcription factor for SNAP29 is confirmed in a promoter binding assay. Accordingly, silencing SNAP29 in these cell lines also up-regulates PrP, and promotes tumor cell migration without TNFα treatment. But, when SNAP29 or FOXP3 is silenced in these cells, they are no longer respond to TNFα. Thus, a reduction in autophagy is the underlying mechanism by which expression of PrP is up-regulated,and tumor cell migration is enhanced upon TNFα treatment. Disrupting the TNFα-NF-κB-FOXP3-SNAP29 signaling axis may provide a therapeutic approach to mitigate tumor cell migration. 展开更多
关键词 Tumor necrosis factorα(TNFα) Prion protein Synaptosome associated protein 29(SNAP29) Autophagy Nuclear factor kappa B(NF-κB) Forkhead box P3(FOXP3)
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Binding between Prion Protein and Aβ Oligomers Contributes to the Pathogenesis of Alzheimer’s Disease 认领 引用 被引量：5
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作者 Chang Kong Hao Xie +7 位作者 Zhenxing Gao Ming Shao Huan Li Run Shi Lili Cai Shanshan Gao Taolei Sun Chaoyang Li 《Virologica Sinica》 SCIE CAS CSCD 2019年第5期475-488,共14页
A plethora of evidence suggests that protein misfolding and aggregation are underlying mechanisms of various neurodegenerative diseases,such as prion diseases and Alzheimer's disease(AD).Like prion diseases,AD has... A plethora of evidence suggests that protein misfolding and aggregation are underlying mechanisms of various neurodegenerative diseases,such as prion diseases and Alzheimer's disease(AD).Like prion diseases,AD has been considered as an infectious disease in the past decades as it shows strain specificity and transmission potential.Although it remains elusive how protein aggregation leads to AD,it is becoming clear that cellular prion protein(PrP^c)plays an important role in AD pathogenesis.Here,we briefly reviewed AD pathogenesis and focused on recent progresses how PrP^c contributed to AD development.In addition,we proposed a potential mechanism to explain why infectious agents,such as viruses,conduce AD pathogenesis.Microbe infections cause AD deposition and upregulation of PrP^c,which lead to high affinity binding between AD oligomers and PrP^c.The interaction between PrP^c and AP oligomers in turn activates the Fyn signaling cascade,resulting in neuron death in the central nervous system(CNS).Thus,silencing PrP^c expression may turn out be an effective treatment for PrP^c dependent AD. 展开更多
关键词 Alzheimer’s disease(AD) Amyloid-βprotein Neurodegenerative disease Cellular prion protein(PrP^c)
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