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Originally published In Press as doi:10.1074/mcp.M200037-MCP200 on June 21, 2002.
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Molecular & Cellular Proteomics 1:451-465, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

A Proteomic Analysis of Human Cilia

Identification of Novel Components*,S

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

{ddagger} Cystic Fibrosis/Pulmonary Research and Treatment Center, The University of North Carolina, Chapel Hill, North Carolina 27599-7248
Department of Proteomic Technologies, GlaxoSmithKline, Research Triangle Park, North Carolina 27709

Cilia play an essential role in protecting the respiratory tract by providing the force necessary for mucociliary clearance. Although 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 of Chlamydomonas 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 two-dimensional (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 one-dimensional 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 multidimensional 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 were obtained on over 1400 peptides, and over 200 potential axonemal proteins were identified. Peptide matches were also obtained to over 200 human expressed sequence tags. 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.

§ To whom correspondence should be addressed: The University of North Carolina at Chapel Hill, School of Medicine, Cystic Fibrosis/Pulmonary Research and Treatment Center, CB# 7248, 6123A Thurston-Bowles Bldg., Chapel Hill, NC 27599-7248. Tel.: 919-843-7177; Fax: 919-966-7524; ostro{at}med.unc.edu


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Q. Liu, A. Lyubarsky, J. H. Skalet, E. N. Pugh Jr, and E. A. Pierce
RP1 Is Required for the Correct Stacking of Outer Segment Discs
Invest. Ophthalmol. Vis. Sci., October 1, 2003; 44(10): 4171 - 4183.
[Abstract] [Full Text] [PDF]

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 BloodHome page
M. Chiriva-Internati, F. Grizzi, B. Franceschini, P. L. Hermonat, R. K. Bright, K. Bumm, N. Dioguardi, and W. M. Kast
Is sperm protein 17 a useful target for tumor immunotherapy?
Blood, September 15, 2003; 102(6): 2308 - 2309.
[Full Text] [PDF]

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 Proc. Natl. Acad. Sci. USAHome page
J. P. Calvet
New insights into ciliary function: Kidney cysts and photoreceptors
PNAS, May 13, 2003; 100(10): 5583 - 5585.
[Full Text] [PDF]

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 J. Cell Sci.Home page
F. Pfannenschmid, V. C. Wimmer, R.-M. Rios, S. Geimer, U. Krockel, A. Leiherer, K. Haller, Y. Nemcova, and W. Mages
Chlamydomonas DIP13 and human NA14: a new class of proteins associated with microtubule structures is involved in cell division
J. Cell Sci., April 15, 2003; 116(8): 1449 - 1462.
[Abstract] [Full Text] [PDF]

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 J. Biol. Chem.Home page
C. M. Sadek, A. Jimenez, A. E. Damdimopoulos, T. Kieselbach, M. Nord, J.-A. Gustafsson, G. Spyrou, E. C. Davis, R. Oko, F. A. van der Hoorn, et al.
Characterization of Human Thioredoxin-like 2. A NOVEL MICROTUBULE-BINDING THIOREDOXIN EXPRESSED PREDOMINANTLY IN THE CILIA OF LUNG AIRWAY EPITHELIUM AND SPERMATID MANCHETTE AND AXONEME
J. Biol. Chem., April 4, 2003; 278(15): 13133 - 13142.
[Abstract] [Full Text] [PDF]

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 Hum Mol GenetHome page
I. Ibanez-Tallon, N. Heintz, and H. Omran
To beat or not to beat: roles of cilia in development and disease
Hum. Mol. Genet., April 2, 2003; 12(90001): R27 - 35.
[Abstract] [Full Text] [PDF]


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