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Submitted on June 18, 2002
Revised on June 21, 2002
Accepted on June 21, 2002

A proteomic analysis of human cilia: Identification of novel components

Lawrence E. Ostrowski, Kevin Blackburn, Kristen M. Radde, Mary B. Moyer, Daniela M. Schlatzer, Arthur Moseley, and Richard C. Boucher

Cystic Fibrosis Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7248

Corresponding Author: ostro{at}med.unc.edu

Cilia play an essential role in protecting the respiratory tract by providing the force necessary for mucociliary clearance. While the major structural components of human cilia have been described, a complete understanding of cilia function and regulation will require identification and characterization of all ciliary components. Estimates from studies ofChlamydomonas flagella predict that an axoneme contains > 250 proteins. To identify all the components of human cilia, we have begun a comprehensive proteomic analysis of isolated ciliary axonemes. Analysis by 2-D PAGE resulted in a highly reproducible 2-D map consisting of over 240 well-resolved components. Individual protein spots were digested with trypsin and sequenced using liquid chromatography/tandem mass spectrometry (LC/MS/MS). Peptide matches were obtained to 38 potential ciliary proteins by this approach. To identify ciliary components not resolved by 2-D PAGE, axonemal proteins were separated on a 1-D gel. The gel lane was divided into 45 individual slices, each of which was analyzed by LC/MS/MS. This experiment resulted in peptide matches to an additional 110 proteins. In a third approach, preparations of isolated axonemes were digested with lys-C and the resulting peptides were analyzed directly by LC/MS/MS or by multi-dimensional LC/MS/MS, leading to the identification of a further 66 proteins. Each of the four approaches resulted in the identification of a subset of the proteins present. In total, sequence data was obtained on over 1400 peptides and over 200 potential axonemal proteins were identified. Peptide matches were also obtained to over 200 human ESTs. As an approach to validate the mass spectrometry results, additional studies examined the expression of several identified proteins (annexin I, sperm protein Sp17, retinitis pigmentosa protein RP1) in cilia or ciliated cells. These studies represent the first proteomic analysis of the human ciliary axoneme, and have identified many potentially novel components of this complex organelle.


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