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Modified protein expression in the tectorial membrane of the cochlea reveals roles for the striated sheet matrix

Modified protein expression in the tectorial membrane of the cochlea reveals roles for the striated sheet matrix
Modified protein expression in the tectorial membrane of the cochlea reveals roles for the striated sheet matrix
The tectorial membrane (TM) of the mammalian cochlea is a complex extracellular matrix which, in response to acoustic stimulation, displaces the hair bundles of outer hair cells (OHCs), thereby initiating sensory transduction and amplification. Here, using TM segments from the basal, high-frequency region of the cochleae of genetically modified mice (including models of human hereditary deafness) with missing or modified TM proteins, we demonstrate that frequency-dependent stiffening is associated with the striated sheet matrix (SSM). Frequency-dependent stiffening largely disappeared in all three TM mutations studied where the SSM was absent either entirely or at least from the stiffest part of the TM overlying the OHCs. In all three TM mutations, dissipation of energy is decreased at low (<8 kHz) and increased at high (>8 kHz) stimulus frequencies. The SSM is composed of polypeptides carrying fixed charges, and electrostatic interaction between them may account for frequency-dependent stiffness changes in the material properties of the TM. Through comparison with previous in vivo measurements, it is proposed that implementation of frequency-dependent stiffening of the TM in the OHC attachment region facilitates interaction among tones, backward transmission of energy, and amplification in the cochlea.
cochlear amplifier, cochlear model, cochlear sensory processing, organ of corti, genetically related deafness
0006-3495
203-210
Jones, Gareth P.
1dcfbd96-44ca-4afd-8423-6cc000c1952f
Elliott, Stephen J.
721dc55c-8c3e-4895-b9c4-82f62abd3567
Russell, Ian J.
00b693dd-bb6e-45b3-8561-15d59290c4c0
Lukashkin, Andrei N.
f9126c0c-8e77-4ef0-941e-6795142bb457
Jones, Gareth P.
1dcfbd96-44ca-4afd-8423-6cc000c1952f
Elliott, Stephen J.
721dc55c-8c3e-4895-b9c4-82f62abd3567
Russell, Ian J.
00b693dd-bb6e-45b3-8561-15d59290c4c0
Lukashkin, Andrei N.
f9126c0c-8e77-4ef0-941e-6795142bb457

Jones, Gareth P., Elliott, Stephen J., Russell, Ian J. and Lukashkin, Andrei N. (2015) Modified protein expression in the tectorial membrane of the cochlea reveals roles for the striated sheet matrix. Biophysical Journal, 108 (1), 203-210. (doi:10.1016/j.bpj.2014.11.1854). (PMID:25564867)

Record type: Article

Abstract

The tectorial membrane (TM) of the mammalian cochlea is a complex extracellular matrix which, in response to acoustic stimulation, displaces the hair bundles of outer hair cells (OHCs), thereby initiating sensory transduction and amplification. Here, using TM segments from the basal, high-frequency region of the cochleae of genetically modified mice (including models of human hereditary deafness) with missing or modified TM proteins, we demonstrate that frequency-dependent stiffening is associated with the striated sheet matrix (SSM). Frequency-dependent stiffening largely disappeared in all three TM mutations studied where the SSM was absent either entirely or at least from the stiffest part of the TM overlying the OHCs. In all three TM mutations, dissipation of energy is decreased at low (<8 kHz) and increased at high (>8 kHz) stimulus frequencies. The SSM is composed of polypeptides carrying fixed charges, and electrostatic interaction between them may account for frequency-dependent stiffness changes in the material properties of the TM. Through comparison with previous in vivo measurements, it is proposed that implementation of frequency-dependent stiffening of the TM in the OHC attachment region facilitates interaction among tones, backward transmission of energy, and amplification in the cochlea.

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Published date: 6 January 2015
Keywords: cochlear amplifier, cochlear model, cochlear sensory processing, organ of corti, genetically related deafness
Organisations: Signal Processing & Control Grp

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Local EPrints ID: 373277
URI: http://eprints.soton.ac.uk/id/eprint/373277
ISSN: 0006-3495
PURE UUID: 9467aab8-f0fe-4991-b987-3e17866bb8ec

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Date deposited: 13 Jan 2015 14:15
Last modified: 14 Mar 2024 18:51

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Contributors

Author: Gareth P. Jones
Author: Ian J. Russell
Author: Andrei N. Lukashkin

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