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High abundance protein profiling of cystic fibrosis lung epithelial cells.

Pollard HB, Ji XD, Jozwik C, Jacobowitz DM

Department of Anatomy, Physiology and Genetics, Uniformed Services University School of Medicine, USUHS, Bethesda, MD 20814, USA.

Protein profiles of cultured cystic fibrosis (CF) lung epithelial cells were analyzed by two-dimensional gel electrophoresis and mass spectrometry (MS). The analysis gave rise to a protein map over the pI range of 4-7, and a molecular weight range of ca. 100-10 kDa. The map contains 194 identified proteins, which were detectable by silver stain. All silver stained features were identified by matrix-assisted laser desorption/ionization-time of flight MS of tryptic peptides. Some proteins were found to be represented by multiple features on the 2-D gel. Among the high abundance proteins identified were sets of proteins associated with inflammation, including the classical NFkappaB, p65 (RelA) and NFkappaB, p65 (RelB). We suggest that this composite atlas of the high abundance CF lung epithelial proteome will serve as a reference database for future studies of candidate CF drugs, validating different approaches to CFTR gene therapy, and analogous investigations of other types of human lung disorders.

Published 1 June 2005 in Proteomics, 5(8): 2210-26.
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Cystic Fibrosis Research Today Archive:

Volume 1 (2004)
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Volume 2 (2005)
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