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Bottom-up and Shotgun Proteomics to Identify a Comprehensive Cochlear Proteome

Bottom-up and Shotgun Proteomics to Identify a Comprehensive Cochlear Proteome

Published on: March 7, 2014

Comparing perilymph proteomes across species.

Jonathan C Palmer¹, Megan S Lord¹, Jeremy L Pinyon²

¹Graduate School of Biomedical Engineering, University of New South Wales Sydney, Sydney, New South Wales, Australia.

The Laryngoscope

|November 3, 2017

Summary

This summary is machine-generated.

Comparing perilymph proteomes in humans, cats, and guinea pigs reveals that cats are a more suitable model for human cochlear implants due to greater protein overlap.

Keywords:

Perilymph proteome cat cochlear implant guinea pig human impedance

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Last Updated: Feb 19, 2026

Bottom-up and Shotgun Proteomics to Identify a Comprehensive Cochlear Proteome

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Published on: March 7, 2014

Mass Spectrometry-Based Proteomics Analyses Using the OpenProt Database to Unveil Novel Proteins Translated from Non-Canonical Open Reading Frames

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Sample Preparation for Endopeptidomic Analysis in Human Cerebrospinal Fluid

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Published on: December 4, 2017

Area of Science:

Biochemistry
Otolaryngology
Proteomics

Background:

The biological components of perilymph influence cochlear implant electrical performance.
Understanding perilymph composition in animal models is crucial for interpreting research and its relevance to human outcomes.

Purpose of the Study:

To analyze and compare the proteomes of human, guinea pig, and cat perilymph.
To assess the suitability of guinea pig and cat models for human cochlear research.

Main Methods:

Perilymph samples from guinea pigs and cats were analyzed using liquid chromatography-tandem mass spectrometry.
Protein identification was performed using the Mascot database; human data were sourced from existing literature.
Proteomes were refined for each species, identifying over 200 proteins per species.

Main Results:

Identified 81 human, 39 guinea pig, and 64 cat proteins; 21 proteins were common across all three species.
Cat perilymph proteome showed 52% overlap with humans, while guinea pig perilymph showed 31% overlap.
Albumin levels were significantly higher in human perilymph; immunoglobulins were more abundant in human than cat perilymph.

Conclusions:

Comparative analysis of perilymph proteomes across species was conducted.
The protein overlap suggests guinea pigs and cats are suitable models for the human cochlea.
Cat perilymph demonstrated a closer proteomic match to human perilymph, indicating its greater suitability.