Proteomic analysis of formalin-fixed celloidin-embedded whole cochlear and laser microdissected spiral ganglion tissues

Abstract

Conclusion: The results of this study demonstrate that proteomic analysis can be successfully performed on formalin-fixed celloidin-embedded (FFCE) archival human cochlear tissues. Objective: To investigate the feasibility of analyzing protein expression in archival cochlear tissues. Material and methods: A new methodology, referred to as Liquid Tissue^TM, was used to extract proteins from human cochlear tissue sections and spiral ganglion tissue isolated by laser microdissection (LMD). Protein identification was performed by bioinformatic analysis of high resolution tandem mass spectrometric data from fractionated tryptic peptide samples. Results: Twenty-six proteins were identified with a minimum of 2 unique peptides and 450 proteins were identified with 1 unique peptide at a confidence level of 95% in cochlear tissue. Ten proteins were identified with a minimum of 2 unique peptides and 485 proteins were identified with 1 unique peptide at a confidence level of 95% in spiral ganglion tissue.

Keywords::

• Archival human cochlear tissue
• Liquid Tissue

Acknowledgments

This research was supported by the Bloom Endowment Fund and a 2009 Deafness Research Foundation Grant provided by the Burch-Safford Foundation.

Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.