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High abundance protein profiling of cystic fibrosis lung epithelial cells
Author(s) -
Pollard Harvey B.,
Ji Xiaoduo,
Jozwik Catherine,
Jacobowitz David M.
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200401120
Subject(s) - proteome , cystic fibrosis , mass spectrometry , proteomics , microbiology and biotechnology , lung , biology , silver stain , two dimensional gel electrophoresis , chemistry , biochemistry , gene , chromatography , medicine , genetics
Abstract 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 p I 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 NFκB, p65 (RelA) and NFκB, 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.