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


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.
Section of Otolaryngology - Head and Neck Surgery, Department of Surgery, University of Chicago, IL 60637,, USA.
Adam
A
Markaryan
Erik G
EG
Nelson
Lawrence D
LD
Helseth
Raul
R
Hinojosa
D005404:Fixatives; D005557:Formaldehyde; D006801:Humans; D007834:Lasers; D042282:Microdissection; D040901:Proteomics; D013136:Spiral Ganglion / Q000378:metabolism*; D016707:Tissue Fixation
D005404:Fixatives; D005557:Formaldehyde