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内体分选转运复合体Ⅲ(ESCRT-III)途径促进心肌细胞释放含cBIN1的微粒。

The ESCRT-III pathway facilitates cardiomyocyte release of cBIN1-containing microparticles.

作者信息

Xu Bing, Fu Ying, Liu Yan, Agvanian Sosse, Wirka Robert C, Baum Rachel, Zhou Kang, Shaw Robin M, Hong TingTing

机构信息

Cedars-Sinai Heart Institute, Cedars-Sinai Medical Center, Los Angeles, California, United States of America.

Department of Medicine, Division of Cardiovascular Medicine, Stanford University, Stanford, California, United States of America.

出版信息

PLoS Biol. 2017 Aug 14;15(8):e2002354. doi: 10.1371/journal.pbio.2002354. eCollection 2017 Aug.

Abstract

Microparticles (MPs) are cell-cell communication vesicles derived from the cell surface plasma membrane, although they are not known to originate from cardiac ventricular muscle. In ventricular cardiomyocytes, the membrane deformation protein cardiac bridging integrator 1 (cBIN1 or BIN1+13+17) creates transverse-tubule (t-tubule) membrane microfolds, which facilitate ion channel trafficking and modulate local ionic concentrations. The microfold-generated microdomains continuously reorganize, adapting in response to stress to modulate the calcium signaling apparatus. We explored the possibility that cBIN1-microfolds are externally released from cardiomyocytes. Using electron microscopy imaging with immunogold labeling, we found in mouse plasma that cBIN1 exists in membrane vesicles about 200 nm in size, which is consistent with the size of MPs. In mice with cardiac-specific heterozygous Bin1 deletion, flow cytometry identified 47% less cBIN1-MPs in plasma, supporting cardiac origin. Cardiac release was also evidenced by the detection of cBIN1-MPs in medium bathing a pure population of isolated adult mouse cardiomyocytes. In human plasma, osmotic shock increased cBIN1 detection by enzyme-linked immunosorbent assay (ELISA), and cBIN1 level decreased in humans with heart failure, a condition with reduced cardiac muscle cBIN1, both of which support cBIN1 release in MPs from human hearts. Exploring putative mechanisms of MP release, we found that the membrane fission complex endosomal sorting complexes required for transport (ESCRT)-III subunit charged multivesicular body protein 4B (CHMP4B) colocalizes and coimmunoprecipitates with cBIN1, an interaction enhanced by actin stabilization. In HeLa cells with cBIN1 overexpression, knockdown of CHMP4B reduced the release of cBIN1-MPs. Using truncation mutants, we identified that the N-terminal BAR (N-BAR) domain in cBIN1 is required for CHMP4B binding and MP release. This study links the BAR protein superfamily to the ESCRT pathway for MP biogenesis in mammalian cardiac ventricular cells, identifying elements of a pathway by which cytoplasmic cBIN1 is released into blood.

摘要

微粒(MPs)是源自细胞表面质膜的细胞间通讯囊泡,尽管目前尚不清楚它们是否起源于心室心肌。在心室心肌细胞中,膜变形蛋白心脏桥连整合素1(cBIN1或BIN1+13+17)会产生横管(t-小管)膜微褶,这有助于离子通道运输并调节局部离子浓度。微褶产生的微结构域不断重组,以响应压力来调节钙信号传导装置。我们探讨了cBIN1微褶从心肌细胞外部释放的可能性。通过免疫金标记的电子显微镜成像,我们在小鼠血浆中发现cBIN1存在于大小约为200 nm的膜囊泡中,这与MPs的大小一致。在心脏特异性杂合性Bin1缺失的小鼠中,流式细胞术检测到血浆中的cBIN1-MPs减少了47%,支持其心脏起源。在培养分离的成年小鼠心肌细胞纯群体的培养基中检测到cBIN1-MPs也证明了其心脏释放。在人血浆中,渗透压休克通过酶联免疫吸附测定(ELISA)增加了cBIN1的检测,并且在心力衰竭患者中cBIN1水平降低,心力衰竭是一种心肌cBIN1减少的疾病,这两者都支持人心脏中cBIN1以MPs形式释放。在探索MP释放的推定机制时,我们发现膜裂变复合物转运所需的内体分选复合物(ESCRT)-III亚基带电多囊泡体蛋白4B(CHMP4B)与cBIN1共定位并共免疫沉淀,肌动蛋白稳定会增强这种相互作用。在cBIN1过表达的HeLa细胞中,敲低CHMP4B会减少cBIN1-MPs的释放。使用截短突变体,我们确定cBIN1中的N端BAR(N-BAR)结构域是CHMP4B结合和MP释放所必需的。这项研究将BAR蛋白超家族与哺乳动物心室细胞中MP生物发生的ESCRT途径联系起来,确定了细胞质cBIN1释放到血液中的途径要素。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7253/5570487/f03a0d251058/pbio.2002354.g001.jpg

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