一般社団法人
日本質量分析学会

第121回　関東談話会講演会

The Identification and Characterization of Lung Cancer Protein Biomarkers using MALDI-TOF-MS
Michael C. Fitzgerald¹, Michael Z. Wang¹, Michael J. Camp², Brandon Howard², and Edward F. Patz²

¹Department of Chemistry, Duke University, Durham, NC 27708.
²Department of Radiology, Duke University Medical Center, Durham, NC 27708

Abstract:

  MALDI-TOF mass spectrometry is an attractive method for generating protein expression profiles of biological samples for proteomic research. Unique proteins that are detected in the MALDI analysis of biological specimens from individuals that are affected with disease can be of tremendous diagnostic and therapeutic utility. Here we describe the results of our studies to identify protein biomarkers of lung cancer. We have identified two unique protein ion signals in the MALDI-TOF mass spectra of lung tumor cell lysates. Extensive purification of the proteins giving rise to these ion signals, and subsequent peptide mapping and sequencing experiments on the purified protein samples revealed that these protein biomarkers were macrophage migration inhibitory factor and cyclophilin A. As part of this work we also report on the use of a MALDI and H/D exchange-based approach to facilitate the characterization and unambiguous identification of a protein biomarker for lung cancer. This approach relies on the use of a new technique termed SUPREX (Stability of Unpurified Proteins from Rates of H/D Exchange) to detect protein specific ligand binding interactions in unpurified protein fractions. Our work to identify these and other protein biomarkers in blood with also be summarized.