Multiscale Imaging Reveals the Hierarchical Organization of Fibrillin Microfibrils.
Multiscale Imaging Reveals the Hierarchical Organization of Fibrillin Microfibrils.
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多尺度成像揭示了纤维蛋白微纤维的分层组织。
DOI：
10.1016/j.jmb.2018.08.012
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发表时间：
2018-10-19
影响因子：
5.6
通讯作者：
Baldock C
中科院分区：
文献类型：
--
作者：
Godwin ARF;Starborg T;Smith DJ;Sherratt MJ;Roseman AM;Baldock C
原纤蛋白微纤维是在哺乳动物弹性组织中发现的进化上古老的、结构复杂的细胞外聚合物，它们赋予弹性性质、隔离生长因子并介导细胞信号传导;因此，了解它们的结构和组织对于更完整地理解细胞功能和组织形态发生是必不可少的。通过结合多种成像技术，我们可视化三个层次的层次组织的cervin结构，从微米级的纤维束在睫状小带的纳米级的个人微原纤维。连续块面扫描电子显微镜成像表明，束小带纤维结合在一起的圆周包裹纤维，这是反映在一个较短的长度尺度，其中个别小带纤维交织的较小的纤维。电子断层扫描显示，微原纤维方向性从高度对齐和平行，连接到基底膜，在小带纤维周边的网状结构，和小带内的微原纤维连接的短横桥，可能形成的原纤维蛋白结合蛋白。三维重建的负染电子显微镜图像的纯化微纤维证实，微纤维具有中空的管状结构，具有明确的珠和interbead区域，类似于我们的断层扫描成像的组织微纤维。这些微原纤维是高度对称的，具有珠中的外环和交织的核心以及珠间区域中的四个线性叉，每个叉容纳一个二聚体。这些数据一起显示了一个单一的分子构建块是如何组织成从微纤维到组织结构的不同层次，跨越纳米到宏观长度尺度。此外，这些组合成像方法的应用对其他组织系统具有广泛的适用性。微纤维中的细胞外基质聚集形成眼韧带。单个珠状微纤维是高度对称的生物聚合物。小带纤维是由排列整齐、排列有序的微纤维组成的。小带纤维束被大纤维包裹，提供结构支撑。原纤维蛋白的组织结构显示了单个构建单元如何构建弹性组织。
Fibrillin microfibrils are evolutionarily ancient, structurally complex extracellular polymers found in mammalian elastic tissues where they endow elastic properties, sequester growth factors and mediate cell signalling; thus, knowledge of their structure and organization is essential for a more complete understanding of cell function and tissue morphogenesis. By combining multiple imaging techniques, we visualize three levels of hierarchical organization of fibrillin structure ranging from micro-scale fiber bundles in the ciliary zonule to nano-scale individual microfibrils. Serial block-face scanning electron microscopy imaging suggests that bundles of zonule fibers are bound together by circumferential wrapping fibers, which is mirrored on a shorter-length scale where individual zonule fibers are interwoven by smaller fibers. Electron tomography shows that microfibril directionality varies from highly aligned and parallel, connecting to the basement membrane, to a meshwork at the zonule fiber periphery, and microfibrils within the zonule are connected by short cross-bridges, potentially formed by fibrillin-binding proteins. Three-dimensional reconstructions of negative-stain electron microscopy images of purified microfibrils confirm that fibrillin microfibrils have hollow tubular structures with defined bead and interbead regions, similar to tissue microfibrils imaged in our tomograms. These microfibrils are highly symmetrical, with an outer ring and interwoven core in the bead and four linear prongs, each accommodating a fibrillin dimer, in the interbead region. Together these data show how a single molecular building block is organized into different levels of hierarchy from microfibrils to tissue structures spanning nano- to macro-length scales. Furthermore, the application of these combined imaging approaches has wide applicability to other tissue systems. Extracellular matrix fibrillin microfibrils assemble to form ocular ligaments. Individual beaded fibrillin microfibrils are highly symmetric biological polymers. Zonule fibers are composed of aligned, organized arrays of fibrillin microfibrils. Bundles of zonule fibers are wrapped by large fibers providing structural support. Fibrillin organization shows how a single building block constructs an elastic tissue.
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影响因子：
4.8
作者：
Ono, Robert N.;Sengle, Gerhard;Sakai, Lynn Y.
通讯作者：
Sakai, Lynn Y.
影响因子：
5.6
作者：
Reinhardt, DP;Keene, DR;Sakai, LY
通讯作者：
Sakai, LY
影响因子：
3.5
作者：
Collin, Gayle B.;Hubmacher, Dirk;Nishina, Patsy M.
通讯作者：
Nishina, Patsy M.
影响因子：
3
作者：
Kremer, JR;Mastronarde, DN;McIntosh, JR
通讯作者：
McIntosh, JR
DOI：
10.1073/pnas.0601609103
发表时间：
2006-08-08
影响因子：
11.1
作者：
Baldock, Clair;Siegler, Veronique;Wess, Tim J.
通讯作者：
Wess, Tim J.