Molecular organization and fine structure of the human tectorial membrane: is it replenished?

Hayashi, Hisamitsu; Schrott‐Fischer, Anneliese; Glueckert, Rudolf; Liu, Wei; Salvenmoser, Willi; Santi, Peter A.; Rask‐Andersen, Helge

doi:10.1007/s00441-015-2225-5

Cited by 4 publications

(3 citation statements)

References 51 publications

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“…Note that the total amount of soluble proteins in the endolymph is 4.7- to 6.4-fold lower than the perilymph and more than 100-fold less than the plasma ( 31 ). Soluble proteins that are not incorporated into the matrix may be actively cleared from the endolymph, a process that may play a role in maintaining a protective, protease-free environment to preserve the long-term stability of the TM, which persists throughout the life ( 32 ).…”

Section: Resultsmentioning

confidence: 99%

The release of surface-anchored α-tectorin, an apical extracellular matrix protein, mediates tectorial membrane organization

Kim

Park

et al. 2019

Sci. Adv.

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The tectorial membrane (TM) is an apical extracellular matrix (ECM) that hovers over the cochlear sensory epithelium and plays an essential role in auditory transduction. The TM forms facing the luminal endolymph-filled space and exhibits complex ultrastructure. Contrary to the current extracellular assembly model, which posits that secreted collagen fibrils and ECM components self-arrange in the extracellular space, we show that surface tethering of α-tectorin (TECTA) via a glycosylphosphatidylinositol anchor is essential to prevent diffusion of secreted TM components. In the absence of surface-tethered TECTA, collagen fibrils aggregate randomly and fail to recruit TM glycoproteins. Conversely, conversion of TECTA into a transmembrane form results in a layer of collagens on the epithelial surface that fails to form a multilayered structure. We propose a three-dimensional printing model for TM morphogenesis: A new layer of ECM is printed on the cell surface concomitant with the release of a preestablished layer to generate the multilayered TM.

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Section: Resultsmentioning

confidence: 99%

The release of surface-anchored α-tectorin, an apical extracellular matrix protein, mediates tectorial membrane organization

Kim

Park

et al. 2019

Sci. Adv.

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“…TM travelling waves have been documented, explaining that the TM's variable radial stiffness and longitudinal coupling may contribute to the electromotor responses of OHCs [27,28]. The TM was studied in several animal models over the years but there have been relatively few investigations in humans [29][30][31][32][33].…”

Section: The Human Tectorial Membranementioning

confidence: 99%

“…Inset D is from 'Molecular Organization and Fine Structure of the Human Tectorial Membrane: is It replenished?' by Hisamitsu Hayashi et al, Cell and Tissue Research, June 18, 2015[33]. It is used here with permission from Springer Nature, licence and terms provided by Springer Nature and Copyright Clearance Centre, licence number 4821850025140.…”

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confidence: 99%

Human cochlear microanatomy – an electron microscopy and super-resolution structured illumination study and review

Liu

Glueckert

Schrott-Fischer

et al. 2020

Hearing, Balance and Communication

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Objective: Studies of the human cochlea are particularly challenging due its exceptional vulnerability and surrounding hard bone. Swift fixation and mild decalcification are necessary to maintain its structural integrity and preserve antigenicity. Such procedures may allow immunohistochemistry, gene analyses, and molecular imaging using super resolution illumination microscopy (SR-SIM) with nanometer resolution. Design: This presentation updates recent studies of the human cochlear microanatomy and immunohistochemistry by our laboratory, discussed in the context of current and past anatomic findings and the available literature. Results: Human studies are necessary, and there are intriguing discrepancies compared with experimental animal studies, highlighting that "men are not simply big mice." The results may improve our understanding of the function of the human hearing organ, the diseases related to it, and how this better understanding can be extended to impact future treatment. Conclusion: The first human inner ear gene therapy trials are in progress, and the accessibility of human cochlear tissue for future stem cell treatment and gene transfer needs further elucidation.

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Microanatomy of the human tunnel of Corti structures and cochlear partition‐tonotopic variations and transcellular signaling

Giese,

Li,

Liu

et al. 2024

Journal of Anatomy

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Auditory sensitivity and frequency resolution depend on the optimal transfer of sound‐induced vibrations from the basilar membrane (BM) to the inner hair cells (IHCs), the principal auditory receptors. There remains a paucity of information on how this is accomplished along the frequency range in the human cochlea. Most of the current knowledge is derived either from animal experiments or human tissue processed after death, offering limited structural preservation and optical resolution. In our study, we analyzed the cytoarchitecture of the human cochlear partition at different frequency locations using high‐resolution microscopy of uniquely preserved normal human tissue. The results may have clinical implications and increase our understanding of how frequency‐dependent acoustic vibrations are carried to human IHCs. A 1‐micron‐thick plastic‐embedded section (mid‐modiolar) from a normal human cochlea uniquely preserved at lateral skull base surgery was analyzed using light and transmission electron microscopy (LM, TEM). Frequency locations were estimated using synchrotron radiation phase‐contrast imaging (SR‐PCI). Archival human tissue prepared for scanning electron microscopy (SEM) and super‐resolution structured illumination microscopy (SR‐SIM) were also used and compared in this study. Microscopy demonstrated great variations in the dimension and architecture of the human cochlear partition along the frequency range. Pillar cell geometry was closely regulated and depended on the reticular lamina slope and tympanic lip angle. A type II collagen‐expressing lamina extended medially from the tympanic lip under the inner sulcus, here named “accessory basilar membrane.” It was linked to the tympanic lip and inner pillar foot, and it may contribute to the overall compliance of the cochlear partition. Based on the findings, we speculate on the remarkable microanatomic inflections and geometric relationships which relay different sound‐induced vibrations to the IHCs, including their relevance for the evolution of human speech reception and electric stimulation with auditory implants. The inner pillar transcellular microtubule/actin system's role of directly converting vibration energy to the IHC cuticular plate and ciliary bundle is highlighted.

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Molecular organization and fine structure of the human tectorial membrane: is it replenished?

Cited by 4 publications

References 51 publications

The release of surface-anchored α-tectorin, an apical extracellular matrix protein, mediates tectorial membrane organization

The release of surface-anchored α-tectorin, an apical extracellular matrix protein, mediates tectorial membrane organization

Human cochlear microanatomy – an electron microscopy and super-resolution structured illumination study and review

Microanatomy of the human tunnel of Corti structures and cochlear partition‐tonotopic variations and transcellular signaling

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