Heat Shock Proteins in Human Perilymph: Implications for Cochlear Implantation

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Heike Schmitt
  • Ariane Roemer
  • Carsten Zeilinger
  • Rolf Salcher
  • Martin Durisin
  • Hinrich Staecker
  • Thomas Lenarz
  • Athanasia Warnecke

Externe Organisationen

  • Medizinische Hochschule Hannover (MHH)
  • University of Kansas (KU)
  • Exzellenzcluster Hearing4all
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Details

OriginalspracheEnglisch
Seiten (von - bis)37-44
Seitenumfang8
FachzeitschriftOtology and Neurotology
Jahrgang39
Ausgabenummer1
PublikationsstatusVeröffentlicht - 1 Jan. 2018

Abstract

Objective: Biomarkers reflecting the etiology and pathophysiology of inner ear diseases are limited. Evaluation of proteins in the perilymph may improve our understanding of inner ear disease. Heat shock proteins (HSP) belong to a superfamily of stress proteins and promote refolding of denatured proteins. The aim of the study was to analyze HSP in human perilymph and to identify possible correlation with audiological and etiologic data. Methods: Sampling of the perilymph was performed during cochlear implantation and vestibular schwannoma removal. Individual proteins were identified by a shot-gun proteomics approach by orbitrap mass spectrometry. Expression of HSP genes was determined in human cochlear tissue that was obtained during transcochlear surgeries. Results: Ten subgroups of HSP were identified in human perilymph samples. Increased levels of HSP were detected in a higher percentage in the perilymph of patients with residual hearing when compared with patients with no residual hearing in cochlear implantation. In patients with complete preservation of residual hearing, HSP 90 is identified in a lower percentage whereas HSP 70 1A/1B and 6 was identified in all the samples. Constitutive expression of HSP family members was verified in normal cochlear tissue. Conclusion: The 10 HSP variants are not identified in all the perilymph samples, but in a higher proportion in patients with residual hearing compared with patients with no residual hearing. In-depth proteome analysis of perilymph samples in correlation to patients' audiogram data shows an increased concentration of HSP in patients with residual hearing. An increase in specific HSP in patients with loss of residual hearing after cochlear implantation was not observed.

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Heat Shock Proteins in Human Perilymph: Implications for Cochlear Implantation. / Schmitt, Heike; Roemer, Ariane; Zeilinger, Carsten et al.
in: Otology and Neurotology, Jahrgang 39, Nr. 1, 01.01.2018, S. 37-44.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Schmitt, H, Roemer, A, Zeilinger, C, Salcher, R, Durisin, M, Staecker, H, Lenarz, T & Warnecke, A 2018, 'Heat Shock Proteins in Human Perilymph: Implications for Cochlear Implantation', Otology and Neurotology, Jg. 39, Nr. 1, S. 37-44. https://doi.org/10.1097/MAO.0000000000001625
Schmitt, H., Roemer, A., Zeilinger, C., Salcher, R., Durisin, M., Staecker, H., Lenarz, T., & Warnecke, A. (2018). Heat Shock Proteins in Human Perilymph: Implications for Cochlear Implantation. Otology and Neurotology, 39(1), 37-44. https://doi.org/10.1097/MAO.0000000000001625
Schmitt H, Roemer A, Zeilinger C, Salcher R, Durisin M, Staecker H et al. Heat Shock Proteins in Human Perilymph: Implications for Cochlear Implantation. Otology and Neurotology. 2018 Jan 1;39(1):37-44. doi: 10.1097/MAO.0000000000001625
Schmitt, Heike ; Roemer, Ariane ; Zeilinger, Carsten et al. / Heat Shock Proteins in Human Perilymph : Implications for Cochlear Implantation. in: Otology and Neurotology. 2018 ; Jahrgang 39, Nr. 1. S. 37-44.
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title = "Heat Shock Proteins in Human Perilymph: Implications for Cochlear Implantation",
abstract = "Objective: Biomarkers reflecting the etiology and pathophysiology of inner ear diseases are limited. Evaluation of proteins in the perilymph may improve our understanding of inner ear disease. Heat shock proteins (HSP) belong to a superfamily of stress proteins and promote refolding of denatured proteins. The aim of the study was to analyze HSP in human perilymph and to identify possible correlation with audiological and etiologic data. Methods: Sampling of the perilymph was performed during cochlear implantation and vestibular schwannoma removal. Individual proteins were identified by a shot-gun proteomics approach by orbitrap mass spectrometry. Expression of HSP genes was determined in human cochlear tissue that was obtained during transcochlear surgeries. Results: Ten subgroups of HSP were identified in human perilymph samples. Increased levels of HSP were detected in a higher percentage in the perilymph of patients with residual hearing when compared with patients with no residual hearing in cochlear implantation. In patients with complete preservation of residual hearing, HSP 90 is identified in a lower percentage whereas HSP 70 1A/1B and 6 was identified in all the samples. Constitutive expression of HSP family members was verified in normal cochlear tissue. Conclusion: The 10 HSP variants are not identified in all the perilymph samples, but in a higher proportion in patients with residual hearing compared with patients with no residual hearing. In-depth proteome analysis of perilymph samples in correlation to patients' audiogram data shows an increased concentration of HSP in patients with residual hearing. An increase in specific HSP in patients with loss of residual hearing after cochlear implantation was not observed.",
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author = "Heike Schmitt and Ariane Roemer and Carsten Zeilinger and Rolf Salcher and Martin Durisin and Hinrich Staecker and Thomas Lenarz and Athanasia Warnecke",
note = "Funding information: Address correspondence and reprint requests to Athanasia Warnecke, M.D., Carl-Neuberg-Street 1, 30625 Hannover, Germany; E-mail: warnecke.athanasia@mh-hannover.de H.S. and A.R. contributed equally. This work is supported by NICHD HD 002528 and by the German Research Foundation (DFG Cluster of Excellence EXC 1077/1 {\textquoteleft}{\textquoteleft}Hearing4all{\textquoteright}{\textquoteright}). The authors disclose no conflicts of interest.",
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Download

TY - JOUR

T1 - Heat Shock Proteins in Human Perilymph

T2 - Implications for Cochlear Implantation

AU - Schmitt, Heike

AU - Roemer, Ariane

AU - Zeilinger, Carsten

AU - Salcher, Rolf

AU - Durisin, Martin

AU - Staecker, Hinrich

AU - Lenarz, Thomas

AU - Warnecke, Athanasia

N1 - Funding information: Address correspondence and reprint requests to Athanasia Warnecke, M.D., Carl-Neuberg-Street 1, 30625 Hannover, Germany; E-mail: warnecke.athanasia@mh-hannover.de H.S. and A.R. contributed equally. This work is supported by NICHD HD 002528 and by the German Research Foundation (DFG Cluster of Excellence EXC 1077/1 ‘‘Hearing4all’’). The authors disclose no conflicts of interest.

PY - 2018/1/1

Y1 - 2018/1/1

N2 - Objective: Biomarkers reflecting the etiology and pathophysiology of inner ear diseases are limited. Evaluation of proteins in the perilymph may improve our understanding of inner ear disease. Heat shock proteins (HSP) belong to a superfamily of stress proteins and promote refolding of denatured proteins. The aim of the study was to analyze HSP in human perilymph and to identify possible correlation with audiological and etiologic data. Methods: Sampling of the perilymph was performed during cochlear implantation and vestibular schwannoma removal. Individual proteins were identified by a shot-gun proteomics approach by orbitrap mass spectrometry. Expression of HSP genes was determined in human cochlear tissue that was obtained during transcochlear surgeries. Results: Ten subgroups of HSP were identified in human perilymph samples. Increased levels of HSP were detected in a higher percentage in the perilymph of patients with residual hearing when compared with patients with no residual hearing in cochlear implantation. In patients with complete preservation of residual hearing, HSP 90 is identified in a lower percentage whereas HSP 70 1A/1B and 6 was identified in all the samples. Constitutive expression of HSP family members was verified in normal cochlear tissue. Conclusion: The 10 HSP variants are not identified in all the perilymph samples, but in a higher proportion in patients with residual hearing compared with patients with no residual hearing. In-depth proteome analysis of perilymph samples in correlation to patients' audiogram data shows an increased concentration of HSP in patients with residual hearing. An increase in specific HSP in patients with loss of residual hearing after cochlear implantation was not observed.

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