Application of SELDI-TOF mass spectrometry for the identification of differentially expressed proteins by formaldehyde exposure

Abstract

SELDI-TOF-MS technology was applied to profile differentially expressed proteins in formaldehyde-exposed cell culture and animal model systems. Protein profiling with an anion exchanger chip, Q-10, revealed sixteen and twelve differentially expressed proteins in formaldehyde-treated human tracheal Hs 680 cells and sera isolated from formaldehyde-inhaled rats, respectively. We further isolated three potential biomarkers of 14600, 16700, and 33800 Da, which were identified by partial protein sequencing as ribosomal phosphoprotein, large, P2, calmodulin, and Apolipoprotein E, respectively. Taken together, we provide experimental basis for understanding the toxic mechanism of formaldehyde as well as potential biomarker candidates by applying the powerful SELDI-TOF-MS technology.