The structure of tip links and kinocilial links in avian sensory hair bundles.

The structure of tip links and kinocilial links in avian sensory hair bundles.
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DOI:
10.1529/biophysj.104.049031
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发表时间:
2004-12
影响因子:
3.4
通讯作者:
V. Tsuprun;R. Goodyear;G. Richardson
V. Tsuprun;R. Goodyear;G. Richardson
中科院分区:
生物学3区
文献类型:
--
作者:
V. Tsuprun;R. Goodyear;G. Richardson

文献摘要

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最近的研究表明,内耳感觉毛束的尖端链接和动纤毛链接具有相似的特性,并共享一个共同的表位,钙粘蛋白23也可能是每种链接类型的组成部分。因此,透射电子显微镜被用来研究和比较鸟类感觉毛束的尖端链接和动纤毛链接的精细结构。鞣酸处理揭示了150-200 nm长和8-11 nm厚的细链,存在于两种连接类型中。对连接图像的傅立叶分析表明,两种连接类型的链由以螺旋状排列盘绕的两条细丝形成,轴向周期为20-25 nm,每条细丝由直径约4 nm的球状结构组成。螺旋状结构的半径和周期的差异可能是观察到的尖端和动纤毛链接的长度变化的基础。尖端连接和动纤毛连接的类似螺旋状结构与共同细胞表面抗原(TLA抗原)的存在以及两种连接类型的物理和化学性质的相似性雅阁。包含两种连接类型的每个丝的球状结构的间距与球状钙粘蛋白重复报道的4.3 nm中心间距相似,并且与钙粘蛋白23是尖端连接的建议一致。
Recent studies have indicated that the tip links and kinocilial links of sensory hair bundles in the inner ear have similar properties and share a common epitope, and that cadherin 23 may also be a component of each link type. Transmission electron microscopy was therefore used to study and compare the fine structure of the tip links and kinocilial links in avian sensory hair bundles. Tannic acid treatment revealed a thin strand, 150-200 nm long and 8-11 nm thick, present in both link types. Fourier analysis of link images showed that the strand of both link types is formed from two filaments coiled in a helix-like arrangement with an axial period of 20-25 nm, with each filament composed of globular structures that are approximately 4 nm in diameter. Differences in the radius and period of the helix-like structure may underlie the observed variation in the length of tip and kinocilial links. The similar helix-like structure of the tip links and kinocilial links is in accord with the presence of a common cell-surface antigen (TLA antigen) and similarities in the physical and chemical properties of the two link types. The spacing of the globular structures comprising each filament of the two link types is similar to the 4.3 nm center-to-center spacing reported for the globular cadherin repeat, and is consistent with the suggestion that cadherin 23 is the tip link.