This work was supported by Grant Number 5 R01 DC 006848-02 from the National Institutes of Health (NIH) and its contents are solely the responsibility of the authors and do not necessarily represent the official views of the NIH or the U.S. government.
Proteomics analysis of perilymph and cerebrospinal fluid in mouse†
Version of Record online: 8 APR 2009
Copyright © 2009 The American Laryngological, Rhinological, and Otological Society, Inc.
Volume 119, Issue 5, pages 953–958, May 2009
How to Cite
Leary Swan, E. E., Peppi, M., Chen, Z., Green, K. M., Evans, J. E., McKenna, M. J., Mescher, M. J., Kujawa, S. G. and Sewell, W. F. (2009), Proteomics analysis of perilymph and cerebrospinal fluid in mouse. The Laryngoscope, 119: 953–958. doi: 10.1002/lary.20209
- Issue online: 20 APR 2009
- Version of Record online: 8 APR 2009
- Manuscript Accepted: 13 JAN 2009
- Manuscript Revised: 9 JAN 2009
- Manuscript Received: 21 NOV 2008
- drug delivery;
- inner ear;
Proteins in perilymph may alter the delivery profile of implantable intracochlear drug delivery systems through biofouling. Knowledge of protein composition will help anticipate interactions with delivered agents.
Analysis of mouse perilymph.
Protein composition of perilymph and cerebrospinal fluid (CSF) was analyzed using a capillary liquid chromatography-mass spectrometry-based iTRAQ quantitative proteomics approach. We searched against a mouse subset of the Uniprot FASTA protein database. We sampled perilymph from the apex of the mouse cochlea to minimize CSF contamination.
More than 50 explicit protein isoforms were identified with very high confidence. iTRAQ reporter ions allowed determination of relative molar amounts of proteins between perilymph and CSF. Protein in perilymph was almost three times more concentrated than in CSF. More than one-third of the proteins in perilymph comprised protease inhibitors, with serpins being the predominant group. Apolipoproteins constituted 16%. Fifteen percent of the proteins were enzymes. Albumin was the most abundant single protein (14%). Proteins with relatively high perilymph/CSF ratios included broad-spectrum protease inhibitors and apolipoproteins.
Some proteins found in perilymph, such as albumin and HMW kininogen, have been implicated in biofouling through adsorption to device materials. The relatively large quantities of apolipoprotein and albumin may serve as a reservoir for acidic and lipophillic drugs. Alpha-2-glycoprotein can bind basic drugs.
Perilymph is similar in protein composition to CSF, though amounts are 2.8 times higher. Protease inhibitors comprise the largest category of proteins. Laryngoscope, 2009