Quantitative Proteomic Profiling
Reveals Differentially
Regulated Proteins in Cystic Fibrosis Cells
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Abstract
The
most prevalent cause of cystic fibrosis (CF) is the deletion
of a phenylalanine residue at position 508 in CFTR (ΔF508-CFTR)
protein. The mutated protein fails to fold properly, is retained in
the endoplasmic reticulum via the action of molecular chaperones,
and is tagged for degradation. In this study, the differences in protein
expression levels in CF cell models were assessed using a systems
biology approach aided by the sensitivity of MudPIT proteomics. Analysis
of the differential proteome modulation without a priori hypotheses
has the potential to identify markers that have not yet been documented.
These may also serve as the basis for developing new diagnostic and
treatment modalities for CF. Several novel differentially expressed
proteins observed in our study are likely to play important roles
in the pathogenesis of CF and may serve as a useful resource for the
CF scientific community
