Comparative proteome analysis was performed between human normal (BEAS 2B)
and malignant (A549) lung epithelial cells in an attempt to identify novel
biomarkers of lung cancer. Approximately 500 protein spots could be separat
ed by mini two-dimensional electrophoresis and visualized with Coomassie bl
ue R-250. Among those relatively abundant proteins, eight spots were change
d more than twofold reproducibly and identified by peptide mass fingerprint
s using mass spectrometry and database search. The increased proteins in A5
49 were aldehyde dehydrogenase, peroxiredoxin I, fatty acid binding protein
, aldoketoreductase, and destrin, whereas the decreased proteins were galec
tin-1, transgelin, and stathmin. Since human lung is exposed to continuous
oxidative stress, antioxidant enzyme peroxiredoxin I was selected for furth
er investigation and its augmented expression was confirmed in cancer tissu
es compared to normal tissues from lung cancer patients, suggesting peroxir
edoxin I as a potential biomarker of lung cancer. (C) 2001 Elsevier Science
.