pHD2沉默提高脂肪来源干细胞移植...
心肌梗死是一种严重的心血管疾病，发病率和病死率高，严重威胁人类健康。大量心肌细胞的不断丢失是心肌梗死发展为心力衰竭并最终导致死亡的重要病理机制。由于成年心肌自我再生能力极弱，挽救和修复受损的心脏组织是治疗心肌梗死的目标。干细胞治疗心肌梗死成为近年的研究热点和未来的发展方向。目前全球已有上百个干细胞治疗心肌梗死的临床试验，这些结果虽然证明干细胞移植有一定疗效，但其效果并不理想。其中一个重要原因是干细胞在缺血缺氧、超氧应激的移植微环境下的存活率及功能低下，这也是本领域亟待解决的难题。
pHD2沉默提高脂肪来源干细胞移植
心肌梗死是一种严重的心血管疾病，发病率和病死率高，严重威胁人类健康。大量心肌细胞的不断丢失是心肌梗死发展为心力衰竭并最终导致死亡的重要病理机制。
由于成年心肌自我再生能力极弱，挽救和修复受损的心脏组织是治疗心肌梗死的目标。干细胞治疗心肌梗死成为近年的研究热点和未来的发展方向。
目前全球已有上百个干细胞治疗心肌梗死的临床试验，这些结果虽然证明干细胞移植有一定疗效，但其效果并不理想。其中一个重要原因是干细胞在缺血缺氧、超氧应激的移植微环境下的存活率及功能低下，这也是本领域亟待解决的难题。
ChristopHer deCharms:即时扫描大脑的技术
神经科学家和发明家ChristopHer deCharms展示一种新的方式利用功能磁共振成像显示大脑活动-思想，情感，痛苦-当它正在发生时。换句话说，你可以看到你的感受。
StepHen Friend：猎寻未知的遗传英雄
我们从那些的了遗传性疾病的人那里获知了什么－在大部分遗传病中，只有部分的急停成员发生了疾病，而其他带有同样基因的却能避开它。斯蒂文.弗兰德建议我们应该开始研究那些没有得病的家庭成员。听听这个弹性课题，以巨大的努力来搜集基因资料可以帮助解码遗传性的失调。
秦正红：DRAM1 regulates autopHagy flux and Bid-mediated cell death via lysosomes
秦正红，博士，教授，神经药理专业博士生导师。1994年在美国宾州医学院研究生院获博士学位，先后在美国国家卫生研究院(NIH)及麻省总医院和哈佛大学医学院从事研究工作。2003年从哈佛大学引进，现为苏州大学医学部基础医学与生物科学学院科研中心实验室主任，中国药理学会生化药理学专业委员会委员，中国药理学会神经药理学专业委员会委员，美国神经科学学会会员。
Damage-regulated autopHagy modulator1 (DRAM1), a novel TP53 target gene, is an evolutionarily conserved lysosomal protein and plays an essential role in TP53-dependent autopHagy activation and apoptosis (Crighton et al, 2006). However, the mechanisms by which DRAM1 promotes autopHagy and apoptosis are not clear.
3-Nitropropionic acid (3-NP) is an inhibitor of mitochondrial respiratory complex II. Intrastriatal administration of 3-NP produces neuropathology resemble to Huntington disease. 3-NP-induced neuronal death was involved in autopHagy and apoptosis. In vitro studies with 3-NP in TP53 wt and null cells, 3-NP or CCCP increased the protein levels of DRAM1 in a TP53-dependent or independent manner. DRAM1 induction contributed to 3-NP-induced autopHagy activation. Knock-down of DRAM1 with siRNA inhibited the activity of V-ATPase, acidification of lysosomes and activation of lysosomal proteases. Knock-down of DRAM1 reduced the clearance of autopHagososmes.
3-NP also induced a transcription independent upregulation of BAX protein levels. Knock-down of DRAM1 suppressed the increase in BAX levels. Co-immunoprecipitation and pull-down studies revealed an interaction of DRAM1 and BAX protein. Stably expression of exogenous DRAM1 increased the half-life of BAX. Upregulation of DRAM1 recruited BAX to lysosomes and induced cathepsin B-dependent cleavage of Bid and cytochrome c release. Knockdown of DRAM1, BAX or inhibition of lysosomal enzymes reduced 3-NP-induced cytochrome c release and cell death.
These data suggest that DRAM1 plays important roles in regulating autopHagy flux and apoptosis. DRAM1 promotes autopHagy flux through a mechanism involves activation of V-ATPase and enhances the acidification of lysosomes. DRAM1 promotes apoptosis via a mechanism involving recruitment of BAX to lysosomes to trigger cathepsin B-mediated Bid cleavage.
Generating B-lympHoblastoid cell lines using Epstein Barr virus transformation.
Generating immortalized B-lympHoblastoid cell lines via Epstein Barr virus transformation using the B95-8 EBV-infected and producing marmoset cell line.
Western Blot Using The invitrogen NuPAGE Novex Bis-Tris MiniGel System(Aubin Penna.pH.D)
Western Blot Using The invitrogen NuPAGE Novex Bis-Tris MiniGel System(Aubin Penna.pH.D)
病毒结构的一般原则 - StepHen Harrison P1
本视频由科普中国和生物医学大讲堂出品
StepHen Harrison (Harvard) Part 1: Virus structures: General principles
Harrison begins his talk by asking why most non-enveloped viruses and some enveloped viruses are symmetrical in shape. He proceeds to show us lovely images of the structures obtained by x-ray crystallograpHy of numerous viral coat proteins. DecipHering these structures allowed scientists to understand that viral coat proteins form multimers, such as dimers and pentamers, which in turn interact with a scaffold that ensures that the coat proteins are correctly placed. This arrangement results in symmetrically shaped viruses.
In Part 1, Harrison also explains that enveloped viruses infect cells by inducing the fusion of the viral and host cell membranes. He delves deeper into the molecular mechanism of membrane fusion driven by the hemagglutinin or HA protein of the influenza virus in Part 2 of his talk.
Non-enveloped viruses, on the other hand, must enter cells by a mechanism other than membrane fusion. This is the focus of Part 3. Using rotavirus as a model, Harrison and his colleagues have used a combination of Xray crystallograpHy and electron cryomicroscopy to decipHer how the spike protein on the viral surface changes its conformation and perforates the cell membrane allowing the virus to enter the cell.
病毒的膜融合 - StepHen Harrison P2
本视频由科普中国和生物医学大讲堂出品
StepHen Harrison (Harvard) Part 2: Viral membrane fusion
Harrison begins his talk by asking why most non-enveloped viruses and some enveloped viruses are symmetrical in shape. He proceeds to show us lovely images of the structures obtained by x-ray crystallograpHy of numerous viral coat proteins. DecipHering these structures allowed scientists to understand that viral coat proteins form multimers, such as dimers and pentamers, which in turn interact with a scaffold that ensures that the coat proteins are correctly placed. This arrangement results in symmetrically shaped viruses.
In Part 1, Harrison also explains that enveloped viruses infect cells by inducing the fusion of the viral and host cell membranes. He delves deeper into the molecular mechanism of membrane fusion driven by the hemagglutinin or HA protein of the influenza virus in Part 2 of his talk.
Non-enveloped viruses, on the other hand, must enter cells by a mechanism other than membrane fusion. This is the focus of Part 3. Using rotavirus as a model, Harrison and his colleagues have used a combination of Xray crystallograpHy and electron cryomicroscopy to decipHer how the spike protein on the viral surface changes its conformation and perforates the cell membrane allowing the virus to enter the cell.
非包膜病毒如何侵入细胞 - StepHen Harrison P3
本视频由科普中国和生物医学大讲堂出品
StepHen Harrison (Harvard) Part 3: Non-enveloped virus entry
Harrison begins his talk by asking why most non-enveloped viruses and some enveloped viruses are symmetrical in shape. He proceeds to show us lovely images of the structures obtained by x-ray crystallograpHy of numerous viral coat proteins. DecipHering these structures allowed scientists to understand that viral coat proteins form multimers, such as dimers and pentamers, which in turn interact with a scaffold that ensures that the coat proteins are correctly placed. This arrangement results in symmetrically shaped viruses.
In Part 1, Harrison also explains that enveloped viruses infect cells by inducing the fusion of the viral and host cell membranes. He delves deeper into the molecular mechanism of membrane fusion driven by the hemagglutinin or HA protein of the influenza virus in Part 2 of his talk.
Non-enveloped viruses, on the other hand, must enter cells by a mechanism other than membrane fusion. This is the focus of Part 3. Using rotavirus as a model, Harrison and his colleagues have used a combination of Xray crystallograpHy and electron cryomicroscopy to decipHer how the spike protein on the viral surface changes its conformation and perforates the cell membrane allowing the virus to enter the cell.