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线粒体和内质网的稳态在维持心血管正常功能中发挥重要作用,线粒体或内质网的结构功能异常参与了众多心血管疾病的发生发展。近年来研究发现线粒体与内质网存在物理和功能的交互,其交互作用调控线粒体、内质网功能,进而影响心肌细胞和平滑肌细胞的线粒体动力学平衡、钙转运及磷脂合成和转运。内质网–线粒体交互异常被认为是冠心病、心力衰竭、肺动脉高压和动脉粥样硬化等心血管疾病的关键机制。因此,理解内质网-线粒体交互机制可为预防和改善心血管疾病提供崭新靶点。 相似文献
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细胞线粒体动力学相关功能是指线粒体通过不断地融合与分裂、线粒体自噬及线粒体-内质网结构偶联来维持细胞正常生理功能的过程。其异常与神经退行性病变、肿瘤、视神经萎缩及糖尿病等疾病的发生发展关系密切。近年来,血管内皮细胞(vascular endothelial cell,VEC)线粒体相关功能在心血管疾病中的研究受到广泛关注,研究发现VEC线粒体相关功能异常在心肌缺血/再灌注(I/R)损伤、冠状动脉粥样硬化、肺动脉高压及扩张型心肌病等疾病的发生发展中发挥重要作用。本文就VEC线粒体动力学相关功能及与心血管疾病的关系进行简要阐述。 相似文献
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线粒体是一个处于不断地融合与分裂过程中的动态细胞器。线粒体融合蛋白2(Mfn2)作为广泛分布于线粒体外膜和线粒体结合内质网膜上具有多重功能的蛋白,参与维持正常细胞功能。除了参与线粒体融合外,Mfn2还能够调节线粒体代谢、促进损伤线粒体的自噬、增强线粒体与内质网交流、维持内质网功能及通过调控线粒体外膜通透性和渗透性钙转运孔道的启闭参与细胞死亡过程等。另外,Mfn2基因还可通过调控Ras-Raf-ERK/MAPK和Ras-PI3K-Akt信号通路分别参与调控血管平滑肌细胞的增殖和凋亡过程。Mfn2的这一系列重要的生物学功能有助于其参与高血压、肺动脉高压、动脉粥样硬化、急性缺血/再灌损伤、扩张性心肌病、心肌肥大、心衰和肥胖糖尿病等多种心血管疾病的发生发展过程。研究Mfn2与心血管疾病的相关性也许能为临床提供一个心血管疾病潜在治疗的靶点。因此,本文将综述Mfn2在心血管疾病相关研究中的现状。 相似文献
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阿尔茨海默病(AD)与帕金森病(PD)病是严重威胁老年人健康的最常见神经退行性疾病,其涉及多种生理代谢异常:线粒体功能损伤、Ca2+稳态失调、氧化应激、错误折叠蛋白聚集、自噬和炎症,然而,此类疾病的发病机制仍没有被明确阐明,导致其治疗水平停滞不前.近年来研究发现,同时影响线粒体与内质网功能的特殊结构线粒体相关内质网膜(... 相似文献
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线粒体相关内质网膜是指内质网和线粒体之间高度动态的紧密连接部分,参与维持内质网和线粒体的正常功能,与细胞脂质代谢、钙稳态、线粒体动力学、自噬和凋亡、内质网应激和炎症等密切相关。研究显示线粒体相关内质网膜功能异常或者数量和结构改变参与心血管疾病的发生发展。本文总结了线粒体相关内质网膜的功能,阐述了其在心血管疾病中的作用及可能机制,为线粒体相关内质网膜成为心血管疾病治疗的新靶点提供理论参考。 相似文献
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心磷脂是主要存在于线粒体内膜的一种结构独特的磷脂, 在线粒体稳态和功能调节中发挥重要作用。线粒体稳态方面, 心磷脂参与线粒体分裂、融合和自噬, 调节线粒体的含量与结构;线粒体功能方面, 心磷脂在线粒体介导的氧化磷酸化、代谢物转运和细胞凋亡等过程中发挥了独特的作用。心磷脂稳态的失衡, 具体表现为含量的改变、酰基链的重塑和过氧化, 可导致线粒体功能障碍并参与多种与线粒体功能障碍相关疾病的病理生理过程。本文综述了心磷脂参与线粒体稳态维持和功能调节的研究进展, 并介绍了心磷脂在线粒体功能障碍相关内分泌疾病中的作用, 以期对心磷脂功能研究和相关疾病的治疗起到启发作用。 相似文献
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实验性氟中毒小鼠肝细胞超策结构的观察 总被引:1,自引:0,他引:1
目的 进一步研究氟中毒对肝损伤的机制。方法 以实验性氟中毒小鼠为实验对象,在透射电镜下观察其肝细胞超微结构的变化。结果 实验性氟中毒导致小鼠肝细胞广泛损伤,包括肝细胞粗面内质网变得扁平并断裂,线粒体可见明显肿大,其嵴消失或模糊。结论氟中毒对粗面内质网和线粒体内膜的影响至少是导致肝细胞损伤的机制之一。 相似文献
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Superresolution Imaging of Human Cytomegalovirus vMIA Localization in Sub-Mitochondrial Compartments
Shivaprasad Bhuvanendran Kyle Salka Kristin Rainey Sen Chandra Sreetama Elizabeth Williams Margretha Leeker Vidhya Prasad Jonathan Boyd George H. Patterson Jyoti K. Jaiswal Anamaris M. Colberg-Poley 《Viruses》2014,6(4):1612-1636
The human cytomegalovirus (HCMV) viral mitochondria-localized inhibitor of apoptosis (vMIA) protein, traffics to mitochondria-associated membranes (MAM), where the endoplasmic reticulum (ER) contacts the outer mitochondrial membrane (OMM). vMIA association with the MAM has not been visualized by imaging. Here, we have visualized this by using a combination of confocal and superresolution imaging. Deconvolution of confocal microscopy images shows vMIA localizes away from mitochondrial matrix at the Mitochondria-ER interface. By gated stimulated emission depletion (GSTED) imaging, we show that along this interface vMIA is distributed in clusters. Through multicolor, multifocal structured illumination microscopy (MSIM), we find vMIA clusters localize away from MitoTracker Red, indicating its OMM localization. GSTED and MSIM imaging show vMIA exists in clusters of ~100–150 nm, which is consistent with the cluster size determined by Photoactivated Localization Microscopy (PALM). With these diverse superresolution approaches, we have imaged the clustered distribution of vMIA at the OMM adjacent to the ER. Our findings directly compare the relative advantages of each of these superresolution imaging modalities for imaging components of the MAM and sub-mitochondrial compartments. These studies establish the ability of superresolution imaging to provide valuable insight into viral protein location, particularly in the sub-mitochondrial compartments, and into their clustered organization. 相似文献
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Horner SM Liu HM Park HS Briley J Gale M 《Proceedings of the National Academy of Sciences of the United States of America》2011,108(35):14590-14595
RIG-I is a cytosolic pathogen recognition receptor that engages viral RNA in infected cells to trigger innate immune defenses through its adaptor protein MAVS. MAVS resides on mitochondria and peroxisomes, but how its signaling is coordinated among these organelles has not been defined. Here we show that a major site of MAVS signaling is the mitochondrial-associated membrane (MAM), a distinct membrane compartment that links the endoplasmic reticulum to mitochondria. During RNA virus infection, RIG-I is recruited to the MAM to bind MAVS. Dynamic MAM tethering to mitochondria and peroxisomes then coordinates MAVS localization to form a signaling synapse between membranes. Importantly, the hepatitis C virus NS3/4A protease, which cleaves MAVS to support persistent infection, targets this synapse for MAVS proteolysis from the MAM, but not from mitochondria, to ablate RIG-I signaling of immune defenses. Thus, the MAM mediates an intracellular immune synapse that directs antiviral innate immunity. 相似文献
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内质网应激反应是细胞面对应激时的一种自我保护性机制,通过三种反应调节途径以减少蛋白质翻译,增强内质网分子伴侣和内质网相关降解基因的表达,诱导细胞凋亡来达到保护细胞及器官的目的。在心血管系统中,内质网应激作为多种应激过程的共同通路,广泛地参与多种心血管疾病的发生。现将介绍内质网应激反应及其心血管系统疾病中的研究进展。 相似文献
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Sharon-Friling R Goodhouse J Colberg-Poley AM Shenk T 《Proceedings of the National Academy of Sciences of the United States of America》2006,103(50):19117-19122
The human CMV UL37x1-encoded protein, also known as the viral mitochondria-localized inhibitor of apoptosis, traffics to the endoplasmic reticulum and mitochondria of infected cells. It induces the fragmentation of mitochondria and blocks apoptosis. We demonstrate that UL37x1 protein mobilizes Ca(2+) from the endoplasmic reticulum into the cytosol. This release is accompanied by cell rounding, cell swelling, and reorganization of the actin cytoskeleton, and these morphological changes can be substantially blocked by a Ca(2+) chelating agent. The UL37x1-mediated release of Ca(2+) from the endoplasmic reticulum likely has multiple consequences, including induction of the unfolded protein response, modulation of mitochondrial function, induction of mitochondrial fission, and protection against apoptotic stimuli. 相似文献