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 5 publications

(5 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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“…Osmium/toluidine staining. (c) Positive collagen type II expression in the BM (arrow) and BM ac beneath the IS and the tectorial membrane (TM) (from Hayashi et al., 2015 ). There is no OSL collagen staining at the bridge (staple).…”

Section: Resultsmentioning

confidence: 99%

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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“…The TM is not a firm acellular membrane merely mediating the bending of hair cells’ stereocilia but constitutes a complex organelle 15. The different pivot points of the TM to the basilar membrane, as the first is attached to the lip of the limbus and the latter to the osseous spiral lamina, make them move relative to one another.…”

Section: Discussionmentioning

confidence: 99%

Lateral semicircular canal dilatation in a patient with congenital hearing loss due to α-tectorin mutation: microanatomical considerations

et al. 2023

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The tectorial membrane is crucial in the physiology of the auditory neuroepithelium. Mutations in one of its functional molecules, α-tectorin, lead to autosomal dominant and recessive congenital mid-frequency, non-syndromic hearing loss.Typically, α-tectorin mutations are not accompanied by any morphological abnormalities of the labyrinth. For the first time, we present a case of a toddler boy with congenital hearing loss due toTECTAgene mutation and concomitant bilateral dilation of the lateral semicircular canals.The expression of glycoproteins, like α-tectorin, varies between the distinct labyrinth acellular membranes. Various mutations in theTECTAgene may affect additional glycoproteins that share a high percentage of sequence similarity at the amino acid level with α-tectorin. The mutated glycoproteins differ in the hydration level of their side chains of glycosaminoglycans. Hydration level could affect the mass of the ampullary cupula of the lateral semicircular canal leading to its dilation during embryogenesis.

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

Cited by 5 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

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

Lateral semicircular canal dilatation in a patient with congenital hearing loss due to α-tectorin mutation: microanatomical considerations

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